text/Cofactor_ids.tsv

Without Zn(2+) acting as a cofactor, this protein's function is compromised.
Binds 1 zinc ion.
Without Mg(2+) acting as a cofactor, this protein's function is compromised.
Without Mn(2+) acting as a cofactor, this protein's function is compromised.
Binds 2 magnesium or manganese ions per subunit.
Without iron-sulfur cluster acting as a cofactor, this protein's function is compromised.
Binds 1 iron-sulfur cluster per subunit.
Binds 2 magnesium ions per subunit.
Without heme acting as a cofactor, this protein's function is compromised.
Binds 2 magnesium ions per tetramer.
Binds 3 Mg(2+) ions per subunit.
Without [4Fe-4S] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [4Fe-4S] cluster per subunit.
Divalent metal cations. Mn(2+) is the preferred ion.
Binds 1 zinc ion per subunit.
Without a divalent metal cation acting as a cofactor, this protein's function is compromised.
Binds 1 divalent metal cation per subunit.
Binds 1 Mg(2+) ion per subunit.
Binds 2 Zn(2+) ions per subunit.
Without Fe(2+) acting as a cofactor, this protein's function is compromised.
Binds 1 Fe(2+) ion.
Binds 2 manganese ions per subunit.
Without Cu cation acting as a cofactor, this protein's function is compromised.
Binds a dinuclear copper A center per subunit.
Without [2Fe-2S] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [2Fe-2S] cluster per subunit.
Binds 2 [4Fe-4S] clusters per subunit. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 2 Zn(2+) ions.
Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 [2Fe-2S] cluster.
Without [3Fe-4S] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [3Fe-4S] cluster.
Binds 1 [4Fe-4S] cluster.
Binds 2 [4Fe-4S] clusters per subunit.
Binds 1 copper ion per subunit.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Without pyridoxal 5'-phosphate acting as a cofactor, this protein's function is compromised.
Without Co(2+) acting as a cofactor, this protein's function is compromised.
Binds 1 Co(2+) ion per subunit.
Without Fe(3+) acting as a cofactor, this protein's function is compromised.
Binds 1 zinc or iron ion per subunit.
Without Mo-molybdopterin acting as a cofactor, this protein's function is compromised.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Mg(2+). Can also accept Mn(2+).
Binds 2 heme A groups non-covalently per subunit.
Binds a copper B center.
Binds 1 Mg(2+) or Mn(2+) ion per subunit.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Without heme b acting as a cofactor, this protein's function is compromised.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 cysteines and 1 arginine.
Binds 2 heme b groups non-covalently.
Without thiamine diphosphate acting as a cofactor, this protein's function is compromised.
Binds 1 thiamine pyrophosphate per subunit.
Binds two magnesium or manganese ions per subunit.
Without FAD acting as a cofactor, this protein's function is compromised.
Without FMN acting as a cofactor, this protein's function is compromised.
Binds 1 FMN per monomer.
Without Fe cation acting as a cofactor, this protein's function is compromised.
Binds 2 Mg(2+) ion per subunit.
Binds 1 zinc ion per monomer.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution. The PSII complex binds additional chlorophylls, carotenoids and specific lipids.
Binds 3 Zn(2+) ions per subunit. Two zinc ions appear to be catalytic, while the third one seems to be structural.
Binds 2 Zn(2+) ions per monomer.
Binds 1 FMN per subunit.
Without dipyrromethane acting as a cofactor, this protein's function is compromised.
Binds 1 dipyrromethane group covalently.
Without NH4(+) acting as a cofactor, this protein's function is compromised.
Without K(+) acting as a cofactor, this protein's function is compromised.
A monovalent cation. Ammonium or potassium.
Without FMNH2 acting as a cofactor, this protein's function is compromised.
Reduced FMN (FMNH(2)).
Without Ni cation acting as a cofactor, this protein's function is compromised.
Binds 2 nickel ions per subunit.
May bind 1 zinc ion per subunit.
Binds 2 heme groups non-covalently per subunit.
Binds 1 Fe cation per subunit.
Binds 1 pyridoxal phosphate per subunit.
Binds 2 Mg(2+) ions per subunit.
With its partner (PsbE) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Without NADP(+) acting as a cofactor, this protein's function is compromised.
Binds 1 NADP(+) per subunit.
Binds 2 [4Fe-4S] clusters.
Without prenyl-FMN acting as a cofactor, this protein's function is compromised.
Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Without Mo-bis(molybdopterin guanine dinucleotide) acting as a cofactor, this protein's function is compromised.
Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit.
Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding.
Without (R)-lipoate acting as a cofactor, this protein's function is compromised.
Binds 1 lipoyl cofactor covalently.
Binds 1 Fe(2+) ion per subunit.
Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Binds 2 Zn(2+) ions per subunit. One is catalytic and the other provides a structural contribution.
Without NADPH acting as a cofactor, this protein's function is compromised.
Binds 1 Zn(2+) ion per subunit.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS.
Binds 2 lipoyl cofactors covalently.
Without pyruvate acting as a cofactor, this protein's function is compromised.
Binds 1 pyruvoyl group covalently per subunit.
Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Without Ca(2+) acting as a cofactor, this protein's function is compromised.
Binds 1 Ca(2+) ion per subunit.
Binds 1 Mg(2+) ion per trimer.
Without L-ascorbate acting as a cofactor, this protein's function is compromised.
Binds 2 magnesium ions per monomer.
Binds 1 FAD per subunit.
Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domains.
Binds 1 potassium ion per subunit.
Binds 2 Zn(2+) or Co(2+) ions per subunit.
Without NAD(+) acting as a cofactor, this protein's function is compromised.
Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+).
Binds 2 iron ions per subunit.
Binds 4 Cu cations per monomer.
Binds 1 Mn(2+) ion per subunit.
Without Ni(2+) acting as a cofactor, this protein's function is compromised.
Without S-adenosyl-L-methionine acting as a cofactor, this protein's function is compromised.
Binds 1 S-adenosyl-L-methionine per subunit.
Binds 3 Zn(2+) ions.
Binds 1 nickel or zinc ion per subunit.
Can utilize both FAD and FMN.
Binds 1 or 2 [4Fe-4S] clusters.
Without Fe-coproporphyrin III acting as a cofactor, this protein's function is compromised.
Fe-coproporphyrin III acts as both substrate and redox cofactor.
Binds 1 Mg(2+) ion per subunit. The magnesium ion binds only when substrate is bound.
Binds 2 Mg(2+) per subunit. Only one magnesium ion has a direct interaction with the protein, the other interactions are indirect.
Binds 1 K(+) per subunit. The potassium ion strongly increases the affinity for DNA.
Divalent metal cations. Mg(2+) or Mn(2+).
Binds 3 Fe cations per monomer.
Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Binds 2 cobalt ions per subunit.
Binds 1 Mg(2+) ion per subunit. May bind a second metal ion at a regulatory site, or after substrate binding.
Binds 1 NAD(+) per subunit.
Binds 1 Ca(2+) ion.
Binds 2 potassium ions per subunit.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
Binds 2 calcium ions per subunit.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues.
Binds 2 divalent metal cations per subunit. Magnesium or manganese.
Divalent metal cations. Prefers magnesium or manganese.
Mg(2+) and Mn(2+) are more tightly associated with the active site motifs (D(D/E)XX(D/E) and NSE) and thus lead to more efficient removal of PPi (PubMed:26239156). In the presence of Co(2+) and Ni(2+) the activity is retained and delta(6)-protoilludene is the major volatile sesquiterpene produced (PubMed:26239156). In the presence of Ca(2+), the major sesquiterpene produced switches to beta-elemene (PubMed:26239156).
Expected to bind 2 Fe(2+) ions per subunit.
Without Na(+) acting as a cofactor, this protein's function is compromised.
Binds 1 sodium ion per monomer.
Binds two Mg(2+) per subunit.
Binds 1 [4Fe-4S] cluster per heterodimer. The cluster is bound at the heterodimer interface by residues from both subunits.
Ca(2+). Requires micromolar level (PIP2-dependent).
Binds 1 heme group covalently.
Binds 1 Mg(2+) ion per monomer.
Binds 1 nickel ion per subunit.
Binds 1 Fe(2+) cation per monomer.
Binds 1 nickel ion per monomer.
Binds 2 divalent ions per subunit.
Binds two Mg(2+) per subunit. The active form of the enzyme binds two Mg(2+) ions in its active site. The first Mg(2+) forms only one salt bridge with the protein.
Binds 1 FMN.
Without Cu(2+) acting as a cofactor, this protein's function is compromised.
Binds 2 copper ions per subunit.
Binds 4 Mg(2+) or Mn(2+) ions per subunit.
Binds 2 [4Fe-4S] clusters. Cluster 2 is most probably the spectroscopically characterized electron acceptor FA and cluster 1 is most probably FB.
Without siroheme acting as a cofactor, this protein's function is compromised.
Binds 1 siroheme per subunit.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NBP35 and two labile, bridging clusters between subunits of the NBP35-CFD1 heterotetramer.
Binds 1 or 2 manganese ions.
Binds either 1 Fe or Ni cation per monomer. Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate.
Requires one Fe(2+) ion for activity.
Requires an additional second metal ion that could be Fe(2+) or Zn(2+).
Binds 1 Mg(2+) ion.
Binds 1 Ca(2+) ion per heterodimer.
Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per heterodimer.
Binds 3 Mg(2+) or Mn(2+) ions per subunit.
A monovalent cation. NH4(+) and K(+) are the most effective.
Deglycase activity does not require glutathione as a cofactor, however, glycated glutathione constitutes a PARK7 substrate.
Binds 2 divalent metal cations per subunit.
Binds 2 divalent ions per subunit. The ions interact primarily with the substrate.
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate.
Binds 5 heme groups per subunit (PubMed:17139260, PubMed:18597779). The catalytic lysine-coordinated high spin heme 1 redox potential value indicates that a driving force for a downhill electron transfer is ensured in the NrfH2A4 complex (PubMed:22519292).
Binds multiple chlorophylls. PSII binds additional chlorophylls, carotenoids and specific lipids.
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate.
Binds 1 [4Fe-4S] cluster per dimer.
Binds 2 Zn(2+) ions per subunit. Zn(2+) ion 1 is bound in the active site. Zn(2+) ion 2 is bound at the dimer interface by residues from both subunits.
Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate.
Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer (Arg-167 and Ser-172 from 1 monomer, Ser-126 of the other). The Ca(2+) ion may have a role in catalysis.
Binds 1 Fe cation.
Binds 3 [4Fe-4S] clusters.
Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute.
Binds 1 divalent metal cation per subunit. Most active with Zn(2+) and Mn(2+) ions. The physiological cofactor is most likely Ca(2+) or Mg(2+).
Zn(2+). The heterohexamer contains tightly bound iron, manganese and zinc ions.
Without coenzyme F420-(gamma-Glu)n acting as a cofactor, this protein's function is compromised.
Binds 1 coenzyme F420 non-covalently per subunit.
Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+).
Monovalent cations. Ammonium or potassium.
Binds 1 heme b group per subunit, that coordinates a highly solvent-exposed Fe(III) atom.
Binds 2 iron ions per dimer. The dimer may bind additional iron ions.
Binds 1 NAD(+) per subunit. The NAD(+) cannot dissociate.
Low activity with Mg(2+).
Binds 1 heme group per subunit.
P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Binds 1 Mg(2+) per homodimer, shared between the Asp-8 pair; divalent cations support activity in decreasing order, Mg(2+) >> Mn(2+) > Fe(2+) > Ni(2+) > Ca(2+).
Binds 3 Ca(2+) ions per C2 domain.
Binds a copper A center.
Without heme c acting as a cofactor, this protein's function is compromised.
Binds 2 magnesium ions. Also active with manganese.
Binds 1 zinc ion per homodimer.
Without chloride acting as a cofactor, this protein's function is compromised.
Binds 1 Cl(-) ion per heavy chain.
Binds 1 heme c group covalently per subunit.
Binds 1 heme d1 group per subunit.
Without a metal cation acting as a cofactor, this protein's function is compromised.
Binds 1 metal ion per subunit.
Binds 1 Zn(2+) ion per subunit. Zn(2+) is required for autocatalytic cleavage.
Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells. Mn(2+) or Mg(2+) are required for glucosyltransferase activity.
Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate (By similarity). Can utilize magnesium, manganese or cobalt (in vitro) (By similarity).
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate (By similarity).
Without adenosylcob(III)alamin acting as a cofactor, this protein's function is compromised.
Mn(2+) will also substitute in autophosphorylation assays, while Ca(2+) is a poor substitute (PubMed:17600145).
Binds 1 heme group per monomer (PubMed:16213520, PubMed:17371046, PubMed:17600145, PubMed:21536032, PubMed:27729224).
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Binds 1 Mg(2+) ion per subunit. This ion is required for catalysis, binding to the active site transiently (at the TMP-binding site), and probably acting as a clamp between the phosphoryl donor and acceptor.
Binds 1 2Fe-2S cluster.
Magnesium. Can also use Mn(2+) instead of Mg(2+).
Binds 2 Zn(2+) ions per subunit. One of the zinc atoms is essential for catalytic activity while the other has a structural function.
Binds multiple chlorophylls and provides some of the ligands for the Ca-4Mn-5O cluster of the oxygen-evolving complex. It may also provide a ligand for a Cl- that is required for oxygen evolution. PSII binds additional chlorophylls, carotenoids and specific lipids.
Binds 1 or 2 heme groups per heterodimer.
Optimal in vitro activity occurs in the presence of Mg(2+), but there is weak activity in its absence (PubMed:26593719). A more complete study shows a preference for Mn(2+), although activity is seen with Mg(2+) and Ca(2+) also (PubMed:27989439).
Without pantetheine 4'-phosphate acting as a cofactor, this protein's function is compromised.
Binds 1 phosphopantetheine covalently.
Binds 2 [2Fe-2S] clusters per subunit.
Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas the other seems to have a structural role.
Binds 3 Zn(2+) ions per subunit.
Binds 4 Ca(2+) ions per subunit.
Binds 1 zinc ion per monomer, a water molecule forms the fourth ligand.
Without pyrroloquinoline quinone acting as a cofactor, this protein's function is compromised.
Binds 1 PQQ group per subunit.
Binds 1 heme b (iron(II)-protoporphyrin IX) group.
Ca(2+) and Mn(2+) stimulate processing of pre-crRNA.
PSII binds multiple chlorophylls, carotenoids and specific lipids.
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions.
Binds 2 divalent metal cations per subunit. Site 2 has a preference for magnesium ions.
Binds 1 FAD covalently per subunit.
Binds 2 divalent metal cations per subunit (By similarity). Can use cobalt, zinc, and possibly also magnesium ions (PubMed:10406960).
Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Without cob(II)alamin acting as a cofactor, this protein's function is compromised.
Binds 2 [4Fe-4S] clusters per monomer.
Binds 1 [4Fe-4S] cluster per subunit. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per molecule.
Without methylcob(III)alamin acting as a cofactor, this protein's function is compromised.
Without 1D-myo-inositol hexakisphosphate acting as a cofactor, this protein's function is compromised.
Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Binds 1 manganese ion per subunit. The iron and manganese ions form a dinuclear manganese-iron cluster.
Magnesium is required for nucleotidyltransferase activity.
Nickel for phosphatase activity.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-cfd1 heterotetramer.
Binds 1 Cl(-) ion per subunit.
Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
Binds up to 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
Binds 1 FAD.
Without (6R)-L-erythro-5,6,7,8-tetrahydrobiopterin acting as a cofactor, this protein's function is compromised.
Tetrahydrobiopterin (BH4). May stabilize the dimeric form of the enzyme.
Shows highest activity with Mn(2+). The Mn(2+) ions can be effectively replaced by Co(2+) ions. Shows less activity with other divalent metal ions such as Fe(2+), Ca(2+) and Mg(2+).
The heme is bound between the two transmembrane subunits.
Without hybrid [4Fe-2O-2S] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 hybrid [4Fe-2O-2S] cluster.
Binds at least 14 chlorophylls (8 Chl-a and 6 Chl-b) and carotenoids such as lutein and neoxanthin.
Binds 1 Ca(2+) ion per monomer.
Binds 5 heme c groups covalently per monomer.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site.
Binds 2 Mg(2+) or Mn(2+) ions per subunit.
Binds 2 calcium ions per subunit. Calcium is inhibitory at high concentrations.
Without lysine tyrosylquinone residue acting as a cofactor, this protein's function is compromised.
Contains 1 lysine tyrosylquinone.
Without biotin acting as a cofactor, this protein's function is compromised.
Binds 2 Fe(3+) ions per subunit.
Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits.
Binds 4 heme c groups covalently per monomer.
Binds 1 zinc ion per homodimer. The zinc ion is bound between 2 subunits and mediates dimerization.
Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Binds 1 copper B ion per subunit.
Binds 2 heme groups per subunit.
Without 5-hydroxybenzimidazolylcob(I)amide acting as a cofactor, this protein's function is compromised.
Binds 1 5-hydroxybenzimidazolylcobamide group.
Binds 1 magnesium or manganese ion per subunit.
Mg(2+) is required for catalysis and for stabilizing the dimer.
Binds 1 Fe(3+) ion per subunit.
Binds 3 Mg(2+) ions per monomer.
With its partner (PsbF) binds heme. PSII binds additional chlorophylls, carotenoids and specific lipids.
Binds 2 Mg(2+) ions.
Binds 1 divalent metal cation.
Can bind about 5 Ca(2+) ions per subunit.
Binds 2 magnesium ions per subunit. Is also active with manganese (in vitro).
Binds 1 FAD per subunit non-covalently.
Magnesium, manganese, cobalt or nickel, but not zinc or copper. Binds 3 magnesium ions per subunit.
Binds 2 metal cations per subunit in the catalytic exonuclease domain.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is presumably bound at the interface of two monomers.
Binds 2 Fe(2+) ions per subunit.
The heme b is bound between the two transmembrane subunits SDHC and SDHD.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone.
Without chlorophyll a acting as a cofactor, this protein's function is compromised.
Binds 16 chlorophyll a molecules per subunit.
Without all-trans-beta-carotene acting as a cofactor, this protein's function is compromised.
Binds 2 beta-carotene molecules per subunit.
Without echinenone acting as a cofactor, this protein's function is compromised.
Binds 1 echinenone molecule per subunit.
Without all-trans-zeaxanthin acting as a cofactor, this protein's function is compromised.
Binds 1 zeaxanthin molecule per subunit.
Binds 2 magnesium ions, but the ions interact each with only 1 or 2 residues.
Binds 1 FAD molecule per subunit.
Can also use Mn(2+).
Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Tightly binds zinc.
Binds 1 Mg(2+) ions per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium. Binds magnesium less tightly than zinc.
Binds 1 zinc ion per subunit (PubMed:15107500, PubMed:16846233).
Binds 1 FAD per subunit. The flavin in the dark is in the oxidized (bright yellow) redox state, whereas it becomes reduced subsequent to light activation and formation of the neutral radical (pale yellow).
Without (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate acting as a cofactor, this protein's function is compromised.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
Divalent metal cations. Co(2+), Mn(2+), Zn(2+), Fe(2+) or Ni(2+).
The active site binds 2 Mg(2+) ions (PubMed:10911996, PubMed:15257292). According to PubMed:10704304, no transposition occurs with Mg(2+) (PubMed:10704304).
Binds Ca(2+) via the C2 domains in absence of phospholipids.
Binds 2 zinc ions per subunit.
Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Binds 4 [4Fe-4S] clusters.
Binds 3 [4Fe-4S] clusters per subunit.
Also able to use Co(2+).
Ca(2+) has 50% activity (PubMed:26396239).
Binds 2 heme C groups per subunit.
Binds 5 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound to the C2 domain.
Exhibits highest activity with Mg(2+). Shows also good activity with Zn(2+) and Cu(2+), and lower activity with Co(2+) and Cd(2+).
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of NUBP1 and two labile, bridging clusters between subunits of the NUBP1-NUBP2 heterotetramer.
Binds 1 Mg(2+) ion per subunit. This ion appears to have a structural role and is required for catalytic activity.
Can also use Zn(2+) or Mn(2+) in vitro, although with much less efficiency than Mg(2+).
Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in the proper positioning of the enzyme along the DNA strand.
Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Binds 2 heme groups non-covalently.
MftE appears to bind one Fe(2+) and one Zn(2+) ion per subunit. Fe(2+) seems to be catalytically active while Zn(2+) could play an auxiliary role.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe with a free coordination site may bind a small ligand, such as exogenous sulfide, thus acting as a sulfur carrier.
Without glutathione acting as a cofactor, this protein's function is compromised.
Binds 1 FAD per dimer.
Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Binds 1 AdoCbl between the large and small subunits, with 6 cofactors per holoenzyme.
Mn(2+) was used in the in vitro kinase assay but Mg(2+) is likely to be the in vivo cofactor.
Binds 1 Fe(3+) ions per subunit.
Isoform Testis-specific only binds 1 Zn(2+) ion per subunit.
Binds 3 chloride ions per subunit.
Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE.
Divalent metal cations. Mg(2+) confers the highest activity.
Binds 2 divalent metal cations per subunit. Can use cobalt, zinc, and possibly also magnesium ions.
Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per subunit.
Probably binds two magnesium or manganese ions per subunit.
Without W-bis(molybdopterin guanine dinucleotide) acting as a cofactor, this protein's function is compromised.
Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD) cofactor per subunit.
Binds 3 Mg(2+) cations per subunit. The strongest magnesium site (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water molecules complete its coordination sphere.
Binds 2 magnesium ions per subunit. One of the ions does not make direct protein contacts.
Can also use Co(2+), Ca(2+) or Ni(2+) in vitro.
Binds 1 Fe(2+) cation per subunit. Zn(2+) can be used to a much lesser extent (PubMed:17135237). Ni(2+) can be used to a lesser extent (By similarity).
The manganese ion interacts primarily with the substrate UDP-N-acetylglucosamine.
Binds 2 Mn(2+) ions per subunit. The xylosyltransferase part binds one Mn(2+) and the beta-1,3-glucuronyltransferase part binds one Mn(2+).
Binds 3 calcium ions per subunit.
PSI electron transfer chain: 5 chlorophyll a, 1 chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a chlorophyll a/chlorophyll a' dimer, A0 is one or more chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Binds 2 magnesium ions per subunit. Has high activity with manganese and zinc ions (in vitro).
Binds 2 heme groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme.
Binds 3 phosphopantetheines covalently.
Divalent metal cation.
Binds 1 divalent metal cation per subunit. Active with Co(2+), Fe(2+), Mn(2+) and Zn(2+).
Binds 1 Mn(2+) or Fe(3+) ion per subunit.
Contains a di-nuclear catalytic Mg(2+) center.
Binds 2 divalent metal cations per subunit with RNAase activity being higher in presence of Mn(2+) than of Mg(2+) or Co(2+).
Binds 4 [4Fe-4S] cluster.
Chlorophyll a.
Without [8Fe-7S] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [8Fe-7S] cluster per heterodimer.
Without [7Fe-Mo-9S-C-homocitryl] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme.
Divalent metal cations; Mg(2+) > Mn(2+) > Ca(2+).
Binds 1 Zn(2+) ion per subunit. This ion is coordinated with 2 cysteines, 1 glutamate and a water molecule that dissociates from the zinc ion to allow the coordination of the amino group of the serine substrate, which is essential for catalysis.
Binds 1 Zn(2+) per monomer.
Contains a mixture of adenosylcobalamin and oxygen-stable cob(II)alamin.
Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+).
Either Mg(2+) or Zn(2+) can occupy the active site.
Binds 2 manganese ions per monomer.
Without ATP acting as a cofactor, this protein's function is compromised.
ATP is required for the transferase activity but it does not seem to be hydrolyzed during the reaction.
Binds 1 FAD per subunit. Only a minority of the protein molecules contain bound FAD. Contrary to the situation in photolyases, the FAD is bound in a shallow, surface-exposed pocket.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit.
Binds 1 divalent cation per subunit. Mg(2+) or Mn(2+).
Binds 2 copper ions per heterodimer.
Binds 3 Ca(2+) ions per subunit.
Binds 6 Cu cations per monomer.
The isolated catalytic domain prefers Mn(2+) over Mg(2+) as a cofactor.
Without 6-hydroxy-FAD acting as a cofactor, this protein's function is compromised.
Binds 2 Zn(2+) ions per subunit. Required for NAALADase activity.
Binds 2 divalent metal cations per subunit (By similarity). Is most efficient with Zn(2+) and Co(2+), has only a small activity with Ni(2+) and Mn(2+) and no activity with Mg(2+), Fe(3+), and Fe(2+) (PubMed:35584544).
Without a monovalent cation acting as a cofactor, this protein's function is compromised.
Binds 1 monovalent cation per monomer in the active site. Structural cofactor that stabilizes the GTP-bound 'on' state. May also act as a transition state stabilizer of the hydrolysis reaction.
Binds 2 Mn(2+) ions per subunit.
Binds 1 Ca(2+) per subunit.
Binds 2 Zn(2+) ions per subunit. Can be replaced by Mn(2+) or Co(2+) which results in altered specificities (PubMed:8444149).
Without AMP acting as a cofactor, this protein's function is compromised.
Binds 1 AMP per subunit.
Binds 1 Mg(2+) per subunit.
Binds 2 [4Fe-4S] cluster.
Binds 4 Zn(2+) ions per subunit.
Binds 1 FAD per monomer.
Magnesium. Can also use other divalent metal cations as manganese, cobalt or zinc.
Activity is highest with Mn(2+).
Divalent metal ions. Mg(2+) is the most effective.
Without L-topaquinone acting as a cofactor, this protein's function is compromised.
Contains 1 topaquinone per subunit.
Binds 1 copper ion per subunit (By similarity). Can also use zinc ion as cofactor (By similarity).
Ca(2+). Can also use Mg(2+), but with lower efficiency.
Binds nucleotide much more tightly and catalyzes nucleotide insertion much more efficiently in the presence of Mg(2+) than in the presence of Mn(2+).
Without (6S)-5,6,7,8-tetrahydrofolate acting as a cofactor, this protein's function is compromised.
Without hydrogencarbonate acting as a cofactor, this protein's function is compromised.
Ca(2+) or Mg(2+). Has lower efficiency with Mg(2+).
Zinc or magnesium.
Binds 1 [4Fe-4S] cluster per heterodimer.
Binds 1 FMN per heterodimer.
Binds at least 4 zinc ions per subunit.
Binds 1 Ca(2+) ion. Required for its activity.
Binds 2 Ni ions per subunit.
Binds 7 Ca(2+) ions.
Phosphatase activity is strongly promoted by several divalent cations but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.
Binds 7 Ca(2+) ions per subunit.
Mn(2+) can substitute for iron, but in higher concentrations. Cannot use Fe(3+), Ni(2+) or Mg(2+).
Without ferriheme a acting as a cofactor, this protein's function is compromised.
Heme A3.
Binds 1 Zn(2+) ion per subunit; 2 are expected compared to other organisms.
Binds 1 zinc ion per subunit. The metal center contained within the active site of LigJ is not used to activate the water molecule but is utilized to activate the substrate via polarization of the carbonyl oxygen.
Binds 1 FAD covalently per monomer.
Binds 2 Mg(2+) ions per subunit (By similarity). Mg(2+) is required for catalysis and for stabilizing the dimer (By similarity). Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformation (By similarity). Inhibited by high levels of Mg(2+) (By similarity).
Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is redox-active and pH labile and is significantly less stable at pH 4.5 as compared with pH 7.0.
Binds 2 Mg(2+) ions per subunit, one in each domain. Mg(2+) is required for hexamerization and phosphatase activity.
Without [8Fe-9S-C-homocitryl] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [8Fe-9S-C-homocitryl] cluster per subunit.
Binds 4 Cu cations per monomer. The Cu cations are bound as 3 distinct Cu centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear.
Binds between the large and small subunits.
Can also use Mg(2+) and Zn(2+), with lower efficiency. Important for nucleotidylyltransferase activity.
5'-deoxyadenosylcobalamine (coenzyme B12).
Without corrinoid acting as a cofactor, this protein's function is compromised.
Binds 1 Mg(2+) ion by subunit.
Manganese. Mg(2+), Co(2+), Ni(2+), Ca(2+), Cu(2+) and Zn(2+) cannot support activity.
Binds 1 copper ion per dimer.
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center.
Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer. The Ca(2+) ion may have a role in catalysis.
Binds 2 [2Fe-2S] clusters.
Binds 1 divalent metal cation per subunit. Fully active with Mg(2+) and active at 70% with Mn(2+). Active at 40% with Co(2+) ion and less than 10% with Ca(2+) or Zn(2+) ions.
Binds 1 zinc ion per subunit. Can also use Ni(2+) and Co(2+) (PubMed:12930831).
Binds at least 2 Zn(2+) per subunit.
Binds 2 [4Fe-4S] clusters. In this family the first cluster has a non-standard and varying [4Fe-4S] binding motif CX(2)CX(2)CX(4-5)CP.
Evidence supports a metal cofactor but evidence for cobalt is inconsistent.
Binds 1 ascorbate molecule per subunit.
Binds 2 manganese ions per subunit. Can also use nickel and cobalt with lower activity.
Binds 1 Fe(2+) ion per monomer.
Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain.
Binds 1 nickel ion per heterotetramer.
Binds 3 Fe(3+) ions per subunit.
Binds 6 Cu cations per subunit. Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction.
Binds 2 Zn(2+) ions per subunit. Can also use Co(2+).
Binds 2 Fe(2+) ions per subunit (PubMed:9312093). The two iron ions could form a binuclear cluster (Probable).
Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true cofactor in vivo.
Binds 2 Zn(2+) ions per subunit (PubMed:6142052, PubMed:11401542, PubMed:15826651). In vitro, can also use Co(2+) or Cd(2+) (PubMed:1671037, PubMed:15610022).
Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate (Probable). Also active with manganase (PubMed:16784868).
Binds 1 [2Fe-2S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein.
Mn(2+) required for ssDNA cleavage activity. Can also utilize Co(2+) and to a lesser extent Mg(2+).
The enzyme activity depends on the nature of the second cofactor. Enzyme containing simultaneously Zn(2+) and either Co(2+), Ni(2+) or Mn(2+) exhibits high activity. Enzyme containing two Zn(2+) is poorly active.
Divalent metal cations. Mn(2+) or Co(2+).
Binds two Mg(2+) per subunit. Required for catalysis and for stabilizing the dimer.
Pyrophosphatase activity requires a divalent metal cation.
Binds 1 protoheme IX center (heme b558) per subunit.
Binds 1 protoheme IX center (heme b595) per heterodimer, in conjunction with CydB.
Without heme d cis-diol acting as a cofactor, this protein's function is compromised.
Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in conjunction with CydB.
The Mn(2+) ion enhances activity.
Binds 1 divalent cation per subunit.
Bind 1 Zn(2+) per subunit.
Without [7Fe-V-9S-C-homocitryl] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [7Fe-V-9S-C-homocitryl] cluster per subunit.
Magnesium. Can also use other divalent metal cations such as manganese, cobalt or zinc.
Cofactor binding induces a conformational change.
Binds 1 or 2 heme groups per heterodimer. Heme is required for responding to nitric oxide, but not for catalytic activity.
1-5 mM manganese gives higher cleavage activity than the same concentration of magnesium.
Zinc is required for the N-terminal methylation of the mature pilin, but not for signal peptide cleavage.
Uses Mg(2+) and Mn(2+) equivalently.
It can also use Fe(2+).
Binds 1 nickel ion per subunit. Is not active with other divalent metal cations such as Zn(2+), Cu(2+), Ca(2+), Mg(2+), Mn(2+) or Fe(2+).
Binds 4 Mn(2+); 2 Mn(2+) for polymerase/primase activity, 1 each for 3-phosphoesterase and ligase.
Binds 4 heme groups per subunit.
Divalent metal cations. Binds Zn(2+).
Without [Ni-Fe-S] cluster acting as a cofactor, this protein's function is compromised.
Binds 1 [Ni-Fe-S] cluster.
Binds 2 magnesium ions.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer.
PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a' dimer, A0 is one or more divinyl chlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Binds 1 heme group. The heme group is called cytochrome b-557.
Binds 2 divalent metal cations per subunit. The ions could be magnesium and/or manganese.
Monovalent cation. The ion could be potassium.
Binds 3 [4Fe-4S] clusters per monomer. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two others probably act as substrate.
Anaerobically binds 1 [4Fe-4S] cluster per subunit; cluster is lost on exposure to O(2). Cluster is stabilized in the presence of mycothiol. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can also utilise Cu(2+).
Binds 1 [4Fe-4S] cluster per subunit. It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.
Binds 1 sodium ion per subunit.
Binds 2 Mn(2+) ions per subunit in a binuclear metal center (PubMed:23897835, PubMed:27780190). May bind a third metal with significantly weaker affinity that might facilitate the catalysis but only binds LpxH in the presence of the substrate (PubMed:23897835).
The corrinoid cofactor is norpseudovitamin B12 (norpseudo-B12), a natural B12 cofactor that lacks a characteristic methyl group of the cobamide structure (Ref.6, PubMed:24433392, PubMed:28671181). In vitro, can function with singly substituted benzimidazolyl-norcobamides cofactors (PubMed:29378885).
In the different crystal structures Zn(2+), Ni(2+) and Mn(2+) have been detected (PubMed:15159544, Ref.7, PubMed:22352945). The divalent cation used in Chanchaem is not stated (PubMed:11914056). Mg(2+) was used in de Carvalho (PubMed:16846242). A fourth metal ligand is only seen in the truncated enzyme in the absence of substrate (PubMed:22352945).
Binds 2 Mg(2+) ions per monomer.
Binds 2 Mg(2+) or Mn(2+) cations per subunit.
Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as allosteric activator.
Binds 1 [3Fe-4S] cluster per subunit.
Glutathione is required for the prostaglandin D synthase activity.
Binds 1 heme b group per subunit.
Binds 1 Zn(2+) ions per subunit.
Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-135-Cys-136 and the indole ring of Trp-275.
Binds 4 Ca(2+) ions.
Binds 3 [4Fe-4S] clusters (By similarity). The first cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Binds 2 manganese or zinc ions per subunit.
Binds 2 divalent metal cations. Magnesium or manganese.
Binds 1 FAD per subunit in a bicovalent manner.
Binds 12 [4Fe-4S] clusters.
Divalent metal cation. Prefers Mn(2+) over Mg(2+).
Binds 7 [4Fe-4S] clusters per heterotetramer.
Without [Ni-4Fe-4S] cluster acting as a cofactor, this protein's function is compromised.
Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.
Binds 1 zinc ion per subunit. May play a cocatalytic role and/or a structural role.
Divalent metal cations; Mn(2+) and Mg(2+) are preferred over Co(2+) or Ni(2+).
Without coenzyme F430 acting as a cofactor, this protein's function is compromised.
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state.
Binds 2 magnesium ions per subunit (PubMed:16766715, PubMed:19243146). Is also active with manganese (in vitro) (PubMed:11087399, PubMed:16766715).
Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph-1 subunit.
There are 2 Zn(2+) ions per monomer; Zn(2+) and CoA bind inbetween the 2 domains in each monomer.
Divalent cations stabilize the toxin the in alpha-helix conformation.
Requires divalent cations for activity. The maximum activity is observed at 20 mM of MgCl(2).
Binds Ca(2+). The ions are bound to the C2 1 domain.
Binds 3 Mn(2+) ions per subunit.
Binds 2 Mg(2+) ions per subunit (By similarity). Mg(2+) is required for catalysis and for stabilizing the dimer (By similarity). Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformation (By similarity). Inhibited by high levels of Mg(2+) (PubMed:15606772).
Binds 1 iron-sulfur cluster.
Binds 2 divalent metal cations.
Can also utilize the flavins FMN and riboflavin.
Mg(2+) is required for dsDNA cleavage (PubMed:32246713). Mg(2+) and Mn(2+) support ssDNA cleavage equally (PubMed:30337455).
Homodimeric Cas12f in complex with sgRNA and target DNA binds only 3 Zn(2+) ions.
Binds 3 Ca(2+) ions.
Divalent metal cations; Mn(2+) or Mg(2+).
Contains bound zinc ions after heterologous expression in insect cells.
Divalent cations such as magnesium or manganese.
Binds one Zn(2+) ion per subunit.
Binds 2 Cu(2+) ions per subunit.
Binds 2 Mg(2+) ions per subunit. Can also use Mn(2+) ions instead of Mg(2+).
Binds 2 metal cations per subunit. The catalytic dinuclear metal-binding site could be either a di-iron or a manganese-iron cofactor.
Without tryptophan tryptophylquinone residue acting as a cofactor, this protein's function is compromised.
Uses a protein-derived tryptophan tryptophylquinone (TTQ) cofactor.
Binds 2 [4Fe-4S] clusters (PubMed:23043105). Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Can also use Fe(2+) and Co(2+).
Binds 1 zinc ion per subunit. Zinc binding seems to play a structural role.
Endonuclease activity on target dsDNA requires Mg(2+).
Binds 3 Zn(2+) per subunit.
Can also utilize other divalent cations, such as Mn(2+) and Co(2+) (in vitro).
In the presence of Zn(2+), Mn(2+), Cu(2+), Fe(2+) or Co(2+) ions, activity is very low. In the absence of metal ions, there is no activity.
1 Fe(2+) ion per subunit.
Binds 1 zinc ion per subunit. The zinc ion is necessary for the toxin interaction with MHC class II.
Binds 3 Mg(2+) or Mn(2+) ions per subunit (PubMed:28272876). The best cofactor is Mn(2+) (PubMed:28272875). No effect with monovalent cations (PubMed:28272875).
Binds 1 heme group per homodimer.
Binds 1 low-spin heme b per subunit.
Without Fe(II)-heme o acting as a cofactor, this protein's function is compromised.
Binds 1 high-spin heme o per subunit, also named heme o(3).
Binds 4 FAD per tetramer. Each FAD binding site is formed by three monomers.
Binds 2 Mg(2+) or Mg(2+) ions per subunit.
Binds 1 Fe cation per subunit. Ni(2+) and Zn(2+) can be used to a lesser extent.
Without riboflavin acting as a cofactor, this protein's function is compromised.
Requires a flavin cofactor. Displays no significant preference, and FMN, FAD and riboflavin can all be used efficiently.
Binds 1 Fe(2+) cation per subunit.
Despite some sequence similarity to zinc-containing alcohol dehydrogenases, this enzyme does not bind any metals.
Ca(2+) requirement for activity depends on pH. Active either under acidic conditions with micromolar levels of calcium (PIP2-dependent) or at neutral pH with millimolar levels of calcium (PIP2-independent).
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:27467699). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (By similarity).
Divalent metal ions, such as manganese, cobalt and nickel.
Activity is metal ion dependent and can be restored upon addition of excess Mn(2+).
Binds 1 Zn(2+) per subunit.
Binds 3 Mg(2+) ions per subunit. The third one is coordinated by ATP.
Divalent metal cation. Can use Mn(2+), Mg(2+) or Co(2+).
Mg(2+) and Mn(2+) were both present in the kinase buffer but Mg(2+) is likely to be the in vivo cofactor.
Zn(2+) is required for the lyase reaction.
Binds 2 copper ions per subunit for the monooxygenase reaction.
ATP is required for the deamidation reaction but is not hydrolyzed during this reaction.
Can also use Fe(2+) or Zn(2+), with lower efficiency.
Without NADH acting as a cofactor, this protein's function is compromised.
Magnesium and/or manganese. Specific for polynucleotide RNA in the presence of magnesium, but becomes specific for nucleotide triphosphates in the presence of manganese.
Binds 2 heme b molecules per subunit, called the proximal (bP) and distal (bD) hemes.
Binds 1 zinc ion per subunit (PubMed:8505288, PubMed:16128577).
Without divinyl chlorophyll a acting as a cofactor, this protein's function is compromised.
Without divinyl chlorophyll b acting as a cofactor, this protein's function is compromised.
Binds 1 Fe cation per subunit. Iron is tightly bound.
Binds 1 [2Fe-2S] cluster per homodimer.
Binds 2 Mg(2+) per subunit. Mn(2+) also supports catalytic activity.
Binds 1 monovalent cation per monomer in the active site, which can be sodium or potassium. This structural cofactor stabilizes the GTP-bound 'on' state, and may also act as a transition state stabilizer of the hydrolysis reaction.
Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion.
Ni(2+) ion bind each monomer of the trimer.
According to a report, does not bind any metal ion as cofactor (PubMed:20378650). A crystal structure complexed with 2 Fe(2+) ions has however been observed for an ortholog, suggesting that it binds 2 divalent metal cation ions per subunit (By similarity).
Without binuclear copper center (CuA) acting as a cofactor, this protein's function is compromised.
Binds a binuclear copper A center per subunit.
Binds 3 Mg(2+) ions per homodimer. The enzyme can also utilize Mn(2+) or Co(2+), but has lower cleavage activity with Ni(2+) or Zn(2+). Ca(2+) Co(2+) give no enzyme activity.
Binds 1 Mg(2+) ion per subunit (PubMed:22753070). Can also use Mn(2+) (PubMed:18344366).
Binds 2 manganese ions per subunit (By similarity). Can also use Zn(2+) (PubMed:16475788).
Binds 2 divalent metal cations, probably Mg(2+) in vivo, Zn(2+) ions are found in the crystal structure.
Binds 1 Mg(2+) or Mn(2+) per subunit.
Binds 2 Ca(2+) ions per subunit.
Requires a divalent cation for activity. Displays highest activities with MgCl(2).
Has the highest in vitro activity with 20 mM Mn(2+), a concentration entirely out of the physiological range. Can also utilize Mg(2+), suggesting this may be the physiological cofactor.
The catalytic copper is required to activate oxygen and catalyze oxidative C-H activation.
A zinc-binding site contributes directly to formation of the homodimer.
Without vanadium cation acting as a cofactor, this protein's function is compromised.
The magnesium does not function as an allosteric effector but is essential for glycolytic reaction.
Binds 1 K(+) ion per subunit.
May bind up to 3 heme groups per complex.
Binds 1 divalent metal cation per subunit. Most active with Co(2+), and may utilize Mg(2+) or Mn(2+), though with less activity.
Binds 10 [4Fe-4S] clusters.
Does not require divalent cations.
Binds two metal ions per subunit. Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals: site 1 is occupied by Zn(2+), Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be occupied by only Zn(2+) or Co(2+). One Zn(2+) ion is tightly bound to site 2 and essential for enzyme activity in vivo, while site 1 can be occupied by different metals to give different enzymatic activities. Mn(2+) is required for Cys-Gly hydrolysis activity. A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain.
Binds 1 or 2 FAD per subunit.
Three His residues, the carboxyl oxygen of the C-terminal Ile or Val residue, and a fifth residue, usually Asn, ligate the metal, which binds water to form a catalytic base Mn(2+)OH(2) for hydrogen abstraction.
Does not need divalent cations.
Binds 2 FAD per dimer.
Binds 1 Ca(2+) ion per subunit. The binding is important for enzyme stability.
Without vanadate acting as a cofactor, this protein's function is compromised.
Binds 1 vanadate ion per subunit.
Binds 1 NADP(+) per subunit. NAD(+) can substitute for NADP(+), but enzymatic activity is reduced.
Coordinates 2 Zn(2+) ions. One protomer coordinates the metal ions and the opposing protomer provides the catalytic residues required for cCMP hydrolysis.
Binds 2 divalent ions per subunit. The metal ions interact primarily with the substrate (By similarity). Can utilize magnesium, manganese or cobalt (in vitro) (PubMed:9037140).
Binds 1 potassium ion per subunit. The potassium ion interacts primarily with the substrate (By similarity). Potassium can be replaced by NH(4) (in vitro) (PubMed:9037140).
Pre-crRNA processing is metal independent, while crRNA-guided target RNA cleavage is dependent on divalent metal.
Contains a nonheme dinuclear iron cluster that stabilizes a peroxo intermediate (PubMed:16927313, PubMed:18458342, PubMed:19731912, PubMed:20798054). Was originally suggested to contain a binuclear manganese cluster or an heterodinuclear manganese/iron cluster (PubMed:17765264, PubMed:17718517).
Binds 1 [4Fe-4S] cluster per subunit (PubMed:11940598, PubMed:15491155, PubMed:16289027, PubMed:17010373). The cluster is required for activity and may play a role in binding and activating the substrate for thiol-mediated reduction (PubMed:15491155, PubMed:16289027, PubMed:17010373).
Mn(2+) is the preferable metal for phosphatase activity. Phosphodiesterase activity is observed in the presence of Co(2+), Mn(2+) or Fe(2+).
Binds 2 Zn(2+) and 1 Mn(2+) ions.
Binds 6 Cu cations. Each subunit contains 2 copper centers; Cu(A) (binuclear) and Cu(Z) (tetranuclear). Cu(Z) is thought to be the site of nitrous oxide reduction.
Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo. The polymerase activity incorporates correct dNTPs with much higher efficiency with Mn(2+) than with Mg(2+). The fidelity is slightly more accurate when Mg(2+) is the cofactor compared to Mn(2+). In the presence of Mn(2+), a conformational transition step from non-productive to productive PRIMPOL:DNA complexes limits the enzymatic turnover, whereas in the presence of Mg(2+), the chemical step becomes rate limiting.
Binds 1 Mg(2+) ion per subunit. Is more efficient when using Ni(2+) ion, although it is not likely to be the physiologically relevant active site metal.
Binds 1 zinc ion per subunit (PubMed:1429690, PubMed:15157097, PubMed:15938619, PubMed:19118561).
Binds 2 Mg(2+) ions per subunit (Ref.6). Also able to bind Co(2+), Mn(2+) and Ca(2+) ion (PubMed:1973929).
Mn(2+) required for nuclease activity. Can also utilize Co(2+) and to a lesser extent Mg(2+) or Ni(2+).
Binds 1 [4Fe-4S] cluster per subunit. Not required for nuclease activity, since mutation of the Cys residues leads to a colorless but active protein.
Divalent metal ions. Preferably magnesium.
Binds 2 Zn(2+) ions per subunit. The enzyme can also function with only 1 Zn(2+) ion (PubMed:9761898).
Binds 4 [4Fe-4S] clusters per subunit.
The enzyme may harbor two different cation-binding sites, one that interacts specifically with the nucleotide, and the other that is involved in the binding of the protein substrate.
Ca(2+). Requires millimolar level (PIP2-dependent).
Binds 1 Mg(2+) ion per subunit (PubMed:19237750, PubMed:19121323, Ref.7, Ref.8, PubMed:23485416). Can also use Co(2+) ion to a lesser extent (Ref.8) (PubMed:23485416).
Divalent metal cations. Maximum activity was observed with Mg(2+).
Magnesium. Also active with cobalt or copper.
Binds 1 copper ion per subunit, denoted as copper B.
Binds 2 heme b groups per subunit, denoted as high- and low-spin.
Shows higher activity with Mn(2+) than Mg(2+).
Binds 2 FAD per heterotetramer.
Mg(2+) appears to be the physiologically relevant metal ion cofactor for both transferase and uridylyl-removing activities.
Binds 3 divalent metal cations.
Binds 1 [4Fe-4S] cluster per heterodimer (PubMed:20400946). The cluster is bound at the heterodimer interface by residues from both subunits (PubMed:20400946).
Can use both Mg(2+) and Mn(2+) in vitro and shows higher activity with Mn(2+) but Mg(2+) is likely to be the in vivo cofactor.
Binds 1 heme b group.
Divalent metal cations. Magnesium or manganese are required for activity.
Nickel. 100-fold less efficiency with manganese.
Binds 3 Zn(2+) ions. Can also bind Mn(2+) ions.
Binds 1 Fe(3+) ion per subunit. The iron ion 1 is coordinated via 4 cysteine residues.
Binds 1 Fe(2+) ion per subunit. The iron ion 2 is coordinated via four histidines and one cysteine residue.
Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo.
Contains bound zinc ions after heterologous expression in insect cells, giving rise to a protein that lacks DHICA oxidase activity.
Binds 1 calcium ion per subunit.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit. Binds the MTHF cofactor more tightly than the FAD cofactor.
Binds 1 Fe(3+) cation per subunit.
Binds 2 Mg(2+) ions per subunit (Potential). Can also use Mn(2+) (PubMed:21085589, PubMed:21045009).
Branch migration by the RuvA-RuvB complex requires Mg(2+).
Requires a divalent cation for activity.
Active with either Mg(2+) or Mn(2+), but activity is highest when both are present.
Binds 2 cations, such as magnesium or calcium, per subunit.
Binds 2 magnesium ions per subunit. The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
The CyTase reaction requires a divalent metal ion. Highest activity is observed with Co(2+), but it can also use Mg2(+), Ni2(+), Fe2(+) or Mn2(+).
Magnesium. Can also use other divalent cations like manganese or cobalt.
Co(2+) (for PMI).
Binds 2 Ca(2+) ions; binding site 1 has a 10-fold higher affinity binding site 2 (PubMed:10635330, PubMed:15020228). Loss of Ca(2+)-binding has no measurable effect on host receptor activation or invasion by Listeria, suggesting ion-binding is fortuitous (PubMed:15020228).
Binds 1 divalent metal cation per subunit that could be manganese.
Zn(2+) ion is involved in the catalytic reaction through maintaining the proper configuration of active site.
Binds 5 Ca(2+) ions per subunit.
Zn(2+) is required for amidase activity.
Tetramer binds heme in a 1:1 ratio (PubMed:24855650). Addition of hemin to purified protein yields a tetrameric protein (Probable).
Binds Fe(3+) ion per subunit.
Mg(2+) interacts primarily with the phosphate groups of the bound guanine nucleotide.
Divalent metal cations. Mg(2+) is the most probable.
Binds 2 magnesium or manganese ions per subunit. Manganese is about 20 times more efficient than magnesium.
Without an oxidized flavin acting as a cofactor, this protein's function is compromised.
Binds 2 calcium ions.
Binds 6-hydroxy-FAD non-covalently.
Magnesium. Can also use iron, nickel, cobalt and manganese, but not zinc ions.
Does not need Ca(2+) as cofactor.
Divalent cations. Mg(2+) and to a lesser extent, Mn(2+), Co(2+) and Ca(2+).
Flavinylated by SdhE, flavinylation occurs at a very low level in the absence of SdhE.
Binds to transition metal ions via His-148 and His-263, but also binds metal via other residues.
Binds 1 Cu(2+) ion. The Cu(2+) ion is held by residues from each of 2 monomers of the trimer. Nitrite is bound to the Cu(2+) ion site. Pseudoazurin is the physiological electron donor for the Cu-NIR in vitro.
Without Cu(+) acting as a cofactor, this protein's function is compromised.
Binds 1 Cu(+) ion. The Cu(+) ion is bound within a single monomer.
Without 6,7-dimethyl-8-(1-D-ribityl)lumazine acting as a cofactor, this protein's function is compromised.
Binds 1 6,7-dimethyl-8-(1'-D-ribityl)lumazine non-covalently.
Binds 1 heme per subunit.
Binds 2 heme b groups non-covalently per subunit.
The crystal structure with reduced Cu(1+) has also been determined (PubMed:22883960).
Binds 2 magnesium ions, but the ions are only loosely bound to the protein.
Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-127-Cys-128 and the plane of Trp-254.
Binds 1 heme c group per subunit.
Binds 1 Fe(2+) ion per subunit. Other divalent metal cations can support activity.
Binds 2 cobalt ions per subunit. Co(2+) can be replaced by Mn(2+), resulting in a 25% decrease in activity, but not by Mg(2+), Ca(2+), Fe(2+), Zn(2+), Cu(2+), or Ni(2+).
Binds 2 divalent metal cations per subunit (By similarity). Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions (By similarity).
Divalent metal cation. Can use Mg(2+), Co(2+) or Ni(2+) with similar efficiencies, but is not active in the presence of Mn(2+).
Binds 1 Zn(2+) ion; this is probably a substitute for Fe-S centers.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per subunit. The occupancy is 0.2. Usually had equal molar flavin and folate.
Binds 1 [2Fe-2S] cluster. This [2Fe-2S] cluster is referred to as N1a.
The crystal structure with reduced Cu(1+) has also been determined (PubMed:10206999, PubMed:10529231).
Binds 2 phosphopantetheines covalently.
Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently.
Magnesium. Can also use other divalent metal cations, except copper and calcium.
Without Sr(2+) acting as a cofactor, this protein's function is compromised.
Magnesium. It could be replaced to some extent by nickel, manganese, cobalt, calcium, zinc or strontium.
The 3Fe-4S cluster is redox-responsive, probably binds 1 cluster per monomer.
Binds 1 Mn(2+) or Co(2+) ion per subunit. Can also use Mg(2+), Fe(2+) and Ni(2+) ions to a lesser extent.
May possess two different forms of flavin adenine dinucleotide, classical FAD and so-called modified FAD (mFAD), a stereochemical FAD analog, in which the C2 carbon of the ribityl chain has changed from the R to the S configuration. Conversion of FAD into mFAD was observed both in purified preparations of the enzyme and in cells grown in batch and continuous culture. The relative amount of mFAD in the enzyme varied from 5 to 95%, depending on the growth or storage conditions. The presence of mFAD led to a slight decrease in Vmax and a significant decrease in the KM of alcohol oxidase with respect to methanol.
Mg(2+). Co(2+) or Mn(2+) could partially replace magnesium.
Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit. Electron spin resonance indicates the presence of a mixture of protein molecules that contain either Fe(2+) or Zn(2+).
Without 3'-hydroxyechinenone acting as a cofactor, this protein's function is compromised.
Binds 1 carotenoid molecule per subunit (3'-hydroxyechinenone is the physiological carotenoid, echinenone (70%), 3'-hydroxyechinenone (16%) or zeaxanthin (14%) were all detected in overexpressed, crystallized protein), makes contacts with both domains of the whole protein (PubMed:20368334). Upon RCP generation the carotenoid translocates 12 Angstroms into the N-terminal domain, altering its binding and photochemical properties (PubMed:26113721).
Mg(2+) is probably required for activity in addition to its role in forming the Mg-ATP complex.
Binds 1 divalent metal cation per subunit. Highest nucleotidase activity with Mn(2+), followed by Co(2+), Ni(2+) and Mg(2+). Highest exopolyphosphatase activity with Mg(2+), followed by Co(2+) and Zn(2+).
DNA nicking and nucleotidyltransferase are strictly dependent on Mn(2+); Mg(2+) is able to substitute in DNA nicking 5X less efficiently.
Endonuclease activity partially supported by Mn(2+).
Binds 2 Mg(2+) ions per subunit (PubMed:28031352). Mn(2+) is also accepted, but the activity is less than 15% of that obtained with Mg(2+), when assayed at pH 9.5 (PubMed:16288921).
Divalent cations; Mn(2+) and Mg(2+) are preferred over Co(2+) or Ni(2+). Divalent cations are required for folding and substrate-binding, while divalent cations and NaCl are required for maximal protein stability.
Strongly and equally activated by either Ca(2+) or Mg(2+).
Thr-243 of one partner binds the pyridoxal phosphate moiety of the other.
Binds 1 [4Fe-4S] cluster (PubMed:14961129, PubMed:25995449). The cluster has a structural role (PubMed:14961129).
Binds 2 Zn(2+) ions per subunit. One metal ion is located at the active-site region and has been termed catalytic, while the second metal ion has been termed structural.
Binds 3 or 4 divalent metal cations. Acts specifically on U8 snoRNA with magnesium as cofactor. Has broad substrate specificity with bound manganese or cobalt (in vitro).
Mg(2+) enhances the activity by 30%, followed by Ca(2+) and then Zn(2+).
Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested s that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatases.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nubp1 and two labile, bridging clusters between subunits of the nubp1-nubp2 heterotetramer.
Mg(2+) is the preferred cation for DNA-guided cleavage while Mn(2+) supports both DNA- and RNA-guided cleavage of an RNA target. Ca(2+), which is found in the structure, does not support cleavage (PubMed:16061186). Cleavage probaby requires 2 divalent metal cations (By similarity).
Binds 1 [4Fe-4S] cluster per subunit. May not be required for nuclease activity.
Mn(2+) required for nuclease activity.
Binds 2 Zn(2+) ions per subunit that likely form a catalytic dimetal center.
Divalent metal cations, possibly Mg(2+) or Mn(2+).
Manganese > magnesium.
Binding of Ca(2+) triggers a conformation change that is essential for catalytic activity.
Cu(2+) or Zn(2+).
The ssDNA endonuclease activity (residues 6-260) is stimulated by Mn(2+), Co(2+), Ni(2+), Cu(2+) and Zn(2+), but not by Mg(2+) or Ca(2+). A Ni(2+) ion is seen in crystals upon soaking.
Binds 1 [4Fe-4S] cluster (By similarity). In the presence of oxygen, the [4Fe-4S] cluster may be converted to [2Fe-2S] (By similarity).
Divalent metal cations; Mg(2+) and Co(2+) are better than Mn(2+), Fe(2+) or Ca(2+).
Can also use Mn(2+), with lower efficiency.
Divalent metal ions. Both Ca(2+) and Mn(2+) ions are more effective activators than zinc, cobalt, copper and magnesium ions at low concentrations.
Binds about 7 Ca(2+) per subunit (PubMed:6087888). The metallopeptidase and PKD domains each bind 1 Ca(2+), while each CDB binds 2 (PubMed:12682007, Ref.21, PubMed:23144249, Ref.27).
Binds 1 catalytic Zn(2+) per subunit, a Zn-free form has been crystallized (PubMed:21947205).
Fe-coproporphyrin III acts as both substrate and redox cofactor (By similarity). Was originally thought to use heme as a cofactor (PubMed:15965735).
Binds 2 heme c groups.
Requires the presence of a divalent metal cation for activity. Can use zinc, manganese, cobalt or magnesium.
Divalent metal cations. Prefers Ca(2+) or Mg(2+).
Was shown to bind 1 [3Fe-4S] cluster per subunit (PubMed:19035630). However, it likely initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (By similarity).
The purified enzyme contains a mixture of Fe(2+) and Zn(2+) bound in the active site, and a single equivalent of metal is required for full catalytic activity. After removal of the metal, the reconstitution of the enzyme with Fe(2+) gives the highest activity, followed by Mn(2+), and, to a much lesser extent, Co(2+) and Zn(2+).
Divalent metal cations. Zn(2+) confers higher activity as compared to Mg(2+).
Binds 2 Zn(2+) ions per subunit. To a lesser extent, can also use Co(2+) or Mn(2+) instead of Zn(2+).
Binds 3 zinc ions per subunit, but unlike the enzyme from mammals, shows full activity in the absence of metal ions.
Probably bound by a single Cys residue from each subunit; which protein provides the fourth ligand is unknown.
Divalent metal cations. Mg(2+) or, to a lesser extent, Mn(2+), but not Ca(2+) or Zn(2+).
Binds 1 molecule of NAD(+) or NADH per subunit.
Binds 1 Fe cation per subunit (PubMed:16611640). Ni(2+) and Zn(2+) can be used to a lesser extent (By similarity).
Binds 1 divalent metal cation per subunit. Active with Fe(2+), and probably also with Mn(2+), Zn(2+) and Co(2+).
Binds 1 PQQ per subunit. PQQ is inserted between disulfide Cys-105-Cys-106 and the indole ring of Trp-239.
Binds 1 Mg(2+) ion per subunit; Mn(2+) is also functional. The Me2+-thiamine diphosphate complex is the true cofactor.
Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery to the Rieske protein is mediated by components of the iron sulfur (Fe-S) cluster assembly machinery that reside in the mitochondrial matrix (including HSC20 and LYRM7) (By similarity).
Binds 2 Zn(2+) ions per subunit. It can also bind Cd(2+) and Co(2+) to a lesser extent (PubMed:9416622).
Binds 1 FMN covalently per subunit.
Binds 2 Zn(2+) ions per homotetramer. Zinc ions are bound between subunits.
Lower concentrations of MgCl(2) are required to obtain optimum polyP synthetic activity, whereas higher concentrations of MgCl(2) are necessary for optimum PAP activity.
Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+).
Binds 1 [4Fe-4S] cluster which readily converts to a stable [3Fe-4S] form.
Binds 2 FMN per subunit.
Without Se-Mo-molybdopterin cytosine dinucleotide acting as a cofactor, this protein's function is compromised.
Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD) cofactor per heterotetramer. The cofactor is bound between the NdhL and NdhM subunits.
Magnesium. Can also use Mn(2+), and, to a lesser extent, Co(2+). Cannot use Ni(2+), Ca(2+) and Fe(2+).
Binds 2 iron ions per monomer.
Binds 2 Zn(2+) ion per subunit.
Binds 4 Mg(2+) ions per subunit.
Magnesium. Can also use zinc with lower efficiency.
Was shown to bind 1 [3Fe-4S] cluster per subunit (PubMed:19569147, PubMed:20080550, PubMed:15469281). However, it initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (PubMed:12706830, PubMed:22137895, PubMed:20080550, PubMed:22687151).
Unlike bacterial phosphonoacetate hydrolase, does not require zinc as a cofactor.
Binds 1 heme b (iron(II)-protoporphyrin IX) group non-covalently per monomer.
Binds 2 heme b (iron-protoporphyrin IX) groups per molecule.
Mn(2+) ion is required for highest activity. Can also utilize magnesium ions.
Has been crystallized with Cu(2+) but reconstitutes with Zn(2+).
Mg(2+) is required for helicase activity.
Binds 1 magnesium ion per subunit.
Binds 2 FAD.
Binds 2 FMN.
Binds 4 [4Fe-4S] clusters. Contains approximately 16 iron atoms per subunit.
Binds up to 3 divalent metal cations.
Binds 8 heme c groups per subunit. One specific heme c group is called heme P460.
May also use Mn(2+).
The magnesium ions are essentially bound to the substrate and have few direct interactions with the protein.
Binds 2 Mg(2+) ions per subunit. Mn(2+) and Fe(2+) ions also support activity.
Binds 1 FAD or 1 FMN per subunit.
Unlike other protein kinases, does not require a divalent cation such as magnesium for catalytic activity.
Manganese or cobalt, but not calcium, nickel or zinc can replace Mg(2+) but results in reduced reaction rates.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. Also zinc has been proposed to be the physiological cofactor for yeast.
Manganese. Divalent cations.
A divalent metal cation. Highest activity with Co(2+), followed by Mn(2+) and Cu(2+).
Binds 2 divalent metal cations per subunit (By similarity). Site 2 has a preference for magnesium and/or manganese ions (By similarity).
Binds up to 3 divalent cations (Ca(2+) or Mg(2+)); increasing concentrations of divalent cations allows better binding to phospholipids.
Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization.
Binds 2 [4Fe-4S] clusters. The clusters are coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 2 S-adenosyl-L-methionine per subunit.
Can also use Mn(2+) and Co(2+).
Binds 1 Ca(2+) ion per dimer.
Catalytic activity is higher with Mg(2+).
Binds 1 divalent metal cation per subunit. Most active with Zn(2+) and Mn(2+) ions. The physiological cofactor for gluconolactonase activity is most likely Ca(2+) or Mg(2+). Mg(2+), Mn(2+) and Co(2+) are equally efficient for the hydrolysis of diisopropyl phosphorofluoridate.
Can use Ni(2+) or Co(2+) in vitro, and, to a lesser extent, Fe(2+) or Mn(2+), but not Ca(2+) or Cu(2+).
Without chlorophyll b acting as a cofactor, this protein's function is compromised.
Chlorophyll b.
Binds 1 5,10-methylenetetrahydrofolate (MTHF) non-covalently per subunit. The occupancy is 0.2. Binds the FAD cofactor more tightly than the MTHF cofactor.
Binds 1 divalent metal cation per subunit. Can use Mn(2+), Fe(2+) or Co(2+).
The iron-sulfur cluster may be a [4Fe-4S] cluster.
Highest activity with zinc and cobalt ions, and low activity with manganese or divalent iron ions (PubMed:27023914). Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the ZNG1 zinc chaperone (By similarity).
Binds 2 divalent metal cations per subunit. Can use zinc, nickel, cobalt or manganese.
Requires divalent cations for activity. The maximum activity is observed between 20 and 75 mM of MgCl(2).
The maleylacetate reductase family of enzymes does not require any metal ion for activity, despite being related to the family III metal-dependent polyol dehydrogenases.
Uses preferentially Mn(2+) and, to a lesser extent, Mg(2+) as cofactors.
Divalent metal cations. Can also use Mn(2+) ion.
Binds 1 [4Fe-4S] cluster per subunit. This [4Fe-4S] cluster is referred to as N3.
In the GTP-gamma-S-bound filament structure all subunits bind Mg(2+), in the GDP-bound filament less than half the subunits bind Mg(2+).
Binds 1 heme b (iron(II)-protoporphyrin IX) group per tetramer.
Binds 2 irons ions per subunit via 4 cysteine residues per iron.
Phosphotransfer to CpxR is stimulated by Mg(2+) and/or Mn(2+).
Binds 1 [4Fe-4S] cluster per subunit (PubMed:24171432). It may be important for protein stability, since mutation of the Cys that bind the cofactor leads to a colorless, insoluble protein.
Divalent cations such as manganese, cobalt, nickel and magnesium.
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:11023796). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (By similarity).
Binds 2 divalent metal cations per subunit. Site 2 has a preference for magnesium and/or manganese ions.
Binds 1 FAD per subunit. The bound form of FAD in the inactive state of cry is oxidized FAD, not reduced. After activation by blue light the FAD is in an anionic radical state, which would be paramagnetic. Green light, which reduces levels of radical intermediate, has an antagonistic effect on function.
Mg(2+) is the most effective ion. It can be efficiently replaced with Mn(2+) or Co(2+) and to some extent with Ni(2+).
Mg(2+). To a lesser extent, can also use Mn(2+).
There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of the FRH.
Binds 3 divalent metal cations per subunit (PubMed:22153510). Can use either Mg(2+) or Mn(2+) (PubMed:9618485).
Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270.
At pH 5.0 Mg(2+), Zn(2+) or Cu(2+) is required for maximal activity (PubMed:10387109, PubMed:18801468). Mg2(+) shows low affinity with respect to Zn(2+) as a cofactor, but it is probably the preferred cation due to its abundance and its ability to work in a broad range of pH conditions (PubMed:20135339).
Binds 1 [4Fe-4S] cluster per subunit. Contains 1 [2Fe-2S] cluster after reconstitution of overexpressed protein from E.coli. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Divalent cations such as magnesium, calcium and to a lesser extent manganese, nickel and cobalt.
Monovalent cations such as NH4(+), Rb(+), Cs(+), K(+), Li(+) or Na(+) are required for enzyme activity.
Binds 1 Fe(2+) ion per subunit. Mn(2+) and Zn(2+) can be used to a lesser extent, but not at a relevant physiological concentration.
Binds 2 Mg(2+) per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn(2+) results in partial activity.
Binds 1 protoheme IX center (heme b595, originally called cytochrome a1) per heterodimer, in conjunction with CydA.
Binds 1 iron-chlorin (heme d or cytochrome d) per heterodimer, in conjunction with CydA.
Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits.
Activity is highest with Rb(+), followed by K(+), NH4(+) and Cs(+).
One Mg(2+)is bound by the enzyme, a second binds only to the beta-phosphate of DdrA-bound ADP (PubMed:16338403). Co(2+), Mn(2+) and Ni(2+) can substitute in vitro (PubMed:21040475).
Without Cd(2+) acting as a cofactor, this protein's function is compromised.
Binds 2 Zn(2+) ions per subunit. Co(2+) and Cd(2+) can exchange for Zn(2+) (PubMed:2007567). Probably contains one structural ion and one catalytic ion that seems to be less tightly bound at the site (PubMed:9784233).
Binds 1 divalent cation per subunit. The enzyme is active with manganese, cobalt or cadmium ions.
Binds 2 Zn(2+) per subunit.
Binds Mg(2+) or Mn(2+).
Mg(2+). Mn(2+) is able to replace Mg(2+).
Binds 1 PQQ group non-covalently per subunit (PubMed:10736230, PubMed:3144289). PQQ is embedded between the ring structure formed from a disulfide bridge between adjacent cysteines Cys-139 and Cys-140 and the indole ring of Trp-282 (PubMed:10736230).
Binds 2 calcium ions per subunit. One is located in the active-site cavity near PQQ and the second calcium binds at the N-terminus and contributes to the stability of the native enzyme.
Binds 2 Mg(2+) or Mn(2+) ions per subunit, however the activity with Mg(2+) is about 10-fold higher than with Mn(2+).
Binds 3 Ca(2+) cations per subunit. Binds 1 Ca(2+) as a zymogen, and binds 2 more Ca(2+) cations, or other divalent metal cations, after proteolytic processing.
The zinc ion likely plays a structural role.
Ca(2+) or Mg(2+). Mn(2+) cannot be used.
The zinc ions have a structural role.
Divalent metal cations. Mg(2+), Ni(2+) and Mn(2+) are the most effective. Co(2+) and Ca(2+) are only minimally effective.
A monovalent cation.
Mg(2+) is the most effective ion. It can be partially replaced with Co(2+), Mn(2+), Ni(2+), Cu(2+) or Ca(2+).
Binds 3 zinc ions per subunit. The zinc ions have a structural role.
Binds 3 [4Fe-4S] clusters (PubMed:18558715). The first cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Binds 1 flavin covalently per subunit.
The yeast vacuole plays an important role in Zn(2+) storing and sequestering. Therefore, the changes in Zn(2+) concentration may regulate the enzyme's activity.
Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster is known as N1b.
Binds 2 [4Fe-4S] clusters per subunit. The [4Fe-4S] cluster 1 is known as N5 and [4Fe-4S] cluster 3 as N4.
Binds 2 Zn(2+) ions per subunit (PubMed:33303633). Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals (PubMed:33303633). Site 1 binds metal with low affinity and can be occupied by Zn(2+), Mn(2+), Co(2+) or Mg(2+) (By similarity). While Zn(2+) has the highest affinity for site 1, catalytic activity is the highest with Mn(2+) or Co(2+) and less with Mg(2+) (PubMed:33303633). Site 2 binds tightly to the metal ion and can be occupied only by Zn(2+) or Co(2+) (By similarity). A third metal binding site is also present in an inactive conformation of the hexamer; in this conformation only the metal binding sites 1 and 3 are occupied (By similarity).
Binds 2 iron ions.
Mg(2+) is required for pseudaminic acid cytidylyltransferase activity.
Some of the cofactor binding sites show unusual localization within the protein.
Binds 1 heme (probably heme b) per subunit.
Binds 2 Mn(2+) per subunit.
Binds 6 [4Fe-4S] clusters per heterotetramer.
Binds 1 Mn(2+) ion per monomer.
Binds 1 [2Fe-2S] cluster; whether or not the Fe-S cluster is necessary for transcriptional regulation depends on the type of IscR-binding sequence.
Binds 1 divalent metal cation ion per homodimer with both subunits providing Cys ligands; Fe(2+) gives most activity and is possibly the physiological cofactor, followed by Zn(2+) and Co(2+) (PubMed:24336938, PubMed:28045498). Activity stimulated by Mn(2+) (PubMed:16636051).
Can also use Mn(2+) ion.
Magnesium or zinc; or manganese at a lesser extent, but not calcium.
Binds 1 zinc ion per subunit; it is not clear where this binding occurs.
Shows a preference for FMN. Activity with FAD or riboflavin is 3-fold lower.
Mg(2+), Mn(2+) and Cd(2+) support DNA cleavage whereas Ca(2+) and Zn(2+) do not.
Binds 3 Zn(2+) ions per subunit (for dihydroorotase activity).
Also able to use Mn(2+) and Zn(2+), but the activity is less than that obtained with Mg(2+) ions.
Binds 1 heme group non-covalently.
Binds 4 Cu cations per subunit.
Activity is highest with Mg(2+). Can also use Co(2+), Zn(2+) and Ni(2+).
Divalent metal cation such as Co(2+).
Mg(2+); Mn(2+), Cu(2+), Ni(2+) or Co(2+) also support ATPase activity.
Binds 2 divalent metal cations per subunit (By similarity). Co(2+) is the most effection cation. Can also use Ca(2+), Mn(2+), Zn(2+) or Mg(2+) (PubMed:15752699).
Divalent metal ions.
Binds 1 manganese ion per subunit.
Can also use copper and nickel with lower efficiency.
Without a bacteriochlorophyll acting as a cofactor, this protein's function is compromised.
Binds 4 bacteriochlorophylls per trimer.
Without a bacteriopheophytin acting as a cofactor, this protein's function is compromised.
Binds 2 bacteriopheophytins per trimer.
Binds 1 Fe cation per trimer.
Binds 4 Mg(2+) ions per trimer.
Without a ubiquinone acting as a cofactor, this protein's function is compromised.
Binds 2 ubiquinone per trimer.
Without a menaquinone acting as a cofactor, this protein's function is compromised.
Binds 1 menaquinone per trimer.
Binds 1 ubiquinone per trimer.
Divalent metal cations. Highest activities are measured with Co(2+), Mn(2+) and Cd(2+).
Magnesium. Can also use manganese.
Binds 3 calcium ions or 2 calcium ions and 1 sodium ion per subunit. The sodium ion is bound at calcium concentrations up to 5 mM. At 100 mM calcium 3 calcium ions are bound.
Divalent metal cations are not required for the alpha-2,3-sialyltransferase activity.
Binds 1 divalent metal ion per subunit. Mn(2+).
Binds FAD non-covalently.
Without decylplastoquinone acting as a cofactor, this protein's function is compromised.
Without 6-decylubiquinone acting as a cofactor, this protein's function is compromised.
Lipophilic quinones such as decyl-plastoquinone or decyl-ubiquinone.
Exposure to oxygen reduces copper binding and leads to the formation of a disulfide bond between the two Cys residues that bind the copper ion.
Binds 8 heme c groups covalently per monomer.
Binds 1 adenosylcobalamin.
Binds 1 nickel ion per tetramer.
Binds 1 protoheme IX group (heme b).
Binds 2 Zn(2+) ion per subunit. The Zn(2+) bound by the N-terminus is required for anti-sigma function, the function of the Zn(2+) bound by the C-terminus is unknown.
Magnesium or zinc. Manganese can be used to a lesser extent.
Mn(2+) is a poor substitute (PubMed:12758145).
Manganese is efficient to a lesser extent.
Binds 1 FAD (per monomer/chain).
Binds about 5 Ca(2+) per subunit (PubMed:6087888). The metallopeptidase and PKD domains each bind 1 Ca(2+), while CDB binds 2 (PubMed:23144249, PubMed:23703618, PubMed:25760606, PubMed:28820255). The protein is less elongated in the presence of EGTA (which chelates Ca(2+)) (PubMed:23561530).
Binds 1 Zn(2+) per subunit (PubMed:6087888, PubMed:10217773, PubMed:23703618, PubMed:28820255). A fourth ligand (Asp-421) not found in paralogs ColG and ColT is seen in the absence of inhibitor, which probably plays a role in substrate selection (PubMed:23703618). In the crystal with the N-aryl mercaptoacetamide-based inhibitor Zn is ligated only by the thiolate of the inhibitor (PubMed:28820255).
Contains an active site Fe binuclear center, which is coordinated by Cys-382 and by non-protein ligands.
It can also use manganese, cobalt, iron, calcium and copper ions.
Binds 3 copper ions per subunit. Two of these (copper ion 1 and 3) form a binuclear cluster.
Divalent metal ions (calcium or magnesium).
Binds 5 Mg(2+) ions per homodimer.
Binds 2 Fe(2+) or Co(2+) ions per subunit.
Binds 1 divalent metal cation per subunit (PubMed:15134446). Enhanced by the addition of divalent metal ions such as Co(2+), Mn(2+) and Fe(2+) (PubMed:7766084).
Contains a nonheme dinuclear iron cluster.
Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (PubMed:10933787).
Binds 3 Mg(2+) ions per subunit (PubMed:25004978). Active also with Mn(2+) or Co(2+) (PubMed:25004978).
Can also utilize FMN (PubMed:30337524). Can also utilize riboflavin.
Binds 2 heme groups per subunit via the 2 magnetochrome (MCR) motifs.
Binds 1 Mg(2+) ion per subunit (PubMed:30007416). Is also active with Mn(2+) (PubMed:32814054). Mn(2+)-activated enyzme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over (By similarity). Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues (By similarity).
Undergoes a liquid-like phase transition after binding to DNA, which is dependent on zinc.
Ni(2+) and Mn(2+), but not Mg(2+), Ca(2+), Zn(2+), Co(2+), or Cu(2+), is required for ssDNase activity.
Binds 2 heme groups per subunit. Heme 1, called the proximal or heme Bp in PubMed:12910261, is located at the cytoplasmic interface, heme 2, called the distal or heme Bd, is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme (PubMed:12910261). Heme may be transferred to this protein by HemW (Probable).
Magnesium or manganese or cobalt at a lesser extent.
Binds 1 Fe(2+) ion per monomer. Can be replaced by Mg(2+), but with lower activity.
Binds 1 nickel ion per monomer. Can be replaced by manganese or cobalt ions.
Binds 2 metal ions per subunit; upon overexpression in E.coli the enzyme purifies with various amounts of iron, zinc and manganese. The endogenous metal is unknown.
Manganese cannot be used.
Binds 1 heme group per monomer.
Does not require a metal cofactor.
Binds 5 [4Fe-4S] clusters.
Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells (PubMed:27089365). Mn(2+) or Mg(2+) are required for glucosyltransferase activity (PubMed:8626575, PubMed:27089365).
Binds 1 zinc ion per subunit. The bound metal seen in the crystal structure was tentatively identified as zinc, and its requirement for activity has not been shown.
Binds 2 Zn(2+) ions per subunit. Has highest activity with Zn(2+) ions, but is also active with Co(2+) ions.
Enzymatic activity is fifteen time stronger with Mn(2+) than with Mg(2+).
Contains a dinuclear iron cluster that becomes oxo-bridged (Fe-O-Fe) during O(2) activation.
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (PubMed:3350018, PubMed:9367957). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (PubMed:9030728).
Binds 2 Mg(2+) ions per subunit (Probable). Mn(2+), Co(2+) and Cd(2+) are also accepted (PubMed:3009477, PubMed:2542328, PubMed:8679571, PubMed:9125530, PubMed:10954724).
Binds 3 lipoyl cofactors covalently.
Binds 1 Zn(2+) ion per subunit. Absence of the Zn(2+) (in a residue 1-80 fragment) does not prevent interaction with SigW, nor does it change the overall conformation of RsiW, although a disulfide bond can form between Cys-3 and Cys-37 (PubMed:28319136).
Without Ni(II)-pyridinium-3,5-bisthiocarboxylate mononucleotide acting as a cofactor, this protein's function is compromised.
Was originally shown to use Ni(2+) as a cofactor (PubMed:24710389), but in fact, the cofactor is a (SCS)Ni complex, a nicotinic acid mononucleotide derivative that is covalently attached to Lys-184 and forms a tridentate pincer complex that coordinates nickel through one metal-carbon and two metal-sulfur bonds (By similarity).
Without Mo-molybdopterin cytosine dinucleotide acting as a cofactor, this protein's function is compromised.
Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) per subunit.
Binds 1 Co(2+) ion.
Divalent metal cation. Has preference for nickel ions for the HMG aldolase activity. Has preference for cobalt and zinc ions for the OAA decarboxylase activity.
Divalent metal cations such as Mg(2+), Mn(2+) or Ca(2+).
Binds 1 Mn(2+) or Co(2+) ion per subunit.
Binds 1 Mg(2+) ion per monomer; in the crystal structure only 1 toxin is bound to Mg(2+).
The zinc ion seen in the crystal structure is located far away from the active site and likely plays a structural role. However, it seems important for enzyme activity since the mutation of one of its coordination residues causes a high decrease in activity.
Binds 1 pyridoxal phosphate per homodimer. This is unusual in the SHMT family, that normally contains 1 pyridoxal phosphate per subunit.
Has an absolute requirement of bivalent metal ions Mg(2+) or Mn(2+).
Binds 1 [4Fe-4S] cluster (PubMed:29848660). In the presence of oxygen, the [4Fe-4S] cluster may be converted to [2Fe-2S] (PubMed:29848660).
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the active site region by the zng1 zinc chaperone.
May bind 1 [2Fe-2S] cluster per subunit.
May bind 3 [4Fe-4S] cluster per subunit.
Binds 1 Mn(2+) ion per subunit (PubMed:25871919). However, the sequence similarity to CV_1693 from C.violaceum tends to indicate a trinuclear metal center.
FAD cannot be replaced by FMN or riboflavin.
Binds 1 [3Fe-4S] cluster in its tetrameric form.
Binds 1 [4Fe-4S] cluster in its dimeric form.
Binds 4 copper ions per subunit. The 4 copper centers adopt structures classified as type 1, type 2 and type 3.
Other divalent cations such as Zn(2+), Ni(2+), Ca(2+) and Co(2+) are not able to activate the enzyme.
Binds 7 [4Fe-4S] clusters.
Can use Mg(2+), Mn(2+), Ni(2+) or Co(2+).
Binds 1 FAD per subunit. The FAD cofactor does not cycle between oxidized and reduced forms and therefore does not have a typical redox role in the reaction; it plays a structural role essential for PyrE3 catalysis, to maintain the requisite geometry of the protein and position the 1,3-diene and dienophile groups through specific interactions with the substrate.
The cofactor is mostly bound to the substrate.
Binds 2 divalent metal cations (Ref.9). Shows activity with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (By similarity).
Has low activity with Co(2+) or Ni(2+).
Binds 3 [4Fe-4S] cluster per subunit.
Binds 2 manganese or magnesium ions per subunit (By similarity). Cobalt and nickel are less efficient (PubMed:17897734).
Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:17189640, PubMed:17785418). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (PubMed:17189640).
Fe-coproporphyrin III acts as both substrate and redox cofactor (Probable). Was originally thought to use heme as a cofactor (PubMed:23737523).
Binds 1 Fe(2+) ion per subunit. Can also bind Cu(2+) ions.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the Fe with a free coordination site of the Fe-S cluster may contribute to an enzymatic role.
Binds 1 copper ion in the interface between two trimers.
The copper metal center seems to be reduced from a Cu(II) to Cu(I) oxidation state prior to binding of dioxygen for catalysis.
Ca(2+) is required for its activity and/or stability.
Binds 1 [4Fe-4S] cluster per subunit. The cluster responds to both O(2) and NO. Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
To a lesser extent, can also use Mn(2+) or Co(2+).
No activity with Ni(2+), Co(2+) and Ca(2+).
Binds 2 magnesium ions per subunit. The first is coordinated via water, the second is coordinated to ATP but its significance is unclear.
The heterotrimer binds 1 Mg(2+)-Mn(2+) pair while the heterotetramer binds 2 pairs. Both metals are shared by the toxin-antitoxin pair.
Divalent metal cations. The effectiveness of the cations are Mn(2+) > Mg(2+) > Ca(2+) = Co(2+).
Has also activity with Mn(2+) (in vitro).
Binds 2 Mg(2+) per subunit.
Binds 1 heme group covalently per subunit.
Divalent metal cations. Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Divalent metal cations. Most likely Co(2+).
Binds at least 1 [4Fe-4S] cluster. This cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Probably binds two magnesium ions per subunit.
Binds up to 3 Ca(2+) cations per subunit.
The fourth ligand is a water molecule. Binds 1 Zn(2+) per monomer, in PDB:2FGY a second Zn(2+) is seen, but one of its ligands is an accidentally introduced mutation.
Binds 2 heme c groups covalently per subunit.
ATP is required for the deamidation and depupylation reactions but is not hydrolyzed during the reactions.
Divalent metal cations; Mg(2+) or Mn(2+). Acts as a 3'-5' exoribonuclease in presence of Mg(2+), while it has no 3'-5' exodeoxyribonuclease activity. Has both as a 3'-5' exoribonuclease and exodeoxyribonuclease activities in presence of Mn(2+).
Zn(2+) probably constitutes the cofactor in vivo. Excess zinc decreases the activity, possibly due to the binding of a second Zn(2+) in the active site. Mn(2+) and Co(2+) strongly increase activity.
There are 12-13 Fe atoms per alpha/beta/gamma unit of the FRH.
Divalent cations, Mg(2+) has higher activity than Mn(2+).
Divalent cations including magnesium and manganese.
Binds 1 FMN non-covalently.
Binds 1 zinc ion per subunit (By similarity).
Binds 2 Zn(2+) ions per subunit. Can also use Ni(2+), Co(2+) or Mn(2+).
Binds 1 heme b per subunit.
Probably binds 2 Mn(2+) per subunit.
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. The enzyme is active with cobalt, nickel, manganese and divalent iron ions.
Binds 1 Mg(2+) per subunit, coordinated entirely by the nucleotide and ordered water molecules.
Zinc. May bind iron when zinc levels are limiting.
Divalent metal cations.
Mg(2+) is directly coordinated by Glu-197 and Asp-249 as well as indirectly coordinated through 2 water molecules by Asp-251 (PubMed:10545127).
The hydrogencarbonate anion plays the same catalytic role (proton acceptor) as the side-chain carboxylate group of the essential 'Asp-185' found in actinobacteria, archaea, bacteroidetes, and deltaproteobacteria.
Binds 2 divalent metal cations (By similarity). Shows activity with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (By similarity).
Binds 2 iron ions per subunit. During catalysis, PhnZ uses a mixed-valent Fe(2+)/Fe(3+) cofactor.
Binds 1 Mn(2+) ion per subunit. Can also use Co(2+) and Ni(2+) ions, albeit less efficiently than manganese ion.
Binds 1 zinc ion per subunit, to the LC (PubMed:1429690, PubMed:10932256, PubMed:17167418).
Divalent cations; Mn(2+) is slightly preferred over Mg(2+).
Without Co(3+) acting as a cofactor, this protein's function is compromised.
Binds 1 Co(3+) ion per subunit.
Binds 1 divalent metal cation per subunit. Activity is highest with Co(2+) > Mn(2+) > Zn(2+).
Binds 1 heme group per subunit. The heme group is called cytochrome b-557.
Binds 1 divalent metal cation per subunit. Can probably use ions such as Zn(2+), Mg(2+) or Co(2+).
Can also use Ni(2+), Mn(2+) and Zn(2+), to a lesser extent.
Binds 1 Mg(2+) ion per subunit (PubMed:17473010). Can also use Co(2+) ion to a lesser extent (PubMed:11329257).
Mn(2+) is the most effective activator, followed by Co(2+), Ca(2+), Mg(2+) and Ni(2+).
Fe-coproporphyrin III acts as both substrate and redox cofactor (PubMed:27758026). Was originally thought to use heme as a cofactor (PubMed:25602700).
Without Mo-molybdopterin guanine dinucleotide acting as a cofactor, this protein's function is compromised.
Binds 1 Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor per subunit.
Degradation of ssDNA requires Mn(2+), Co(2+) or Ni(2+); Mg(2+), Ca(2+) or Zn(2+) do not activate ssDNase activity (PubMed:27105119). Formation of cOA requires Mn(2+), Co(2+) or Zn(2+), Mg(2+) is not as efficient (PubMed:28663439).
Binds 3 [4Fe-4S] clusters per homodimer.
Without [Ni-4Fe-5S] cluster acting as a cofactor, this protein's function is compromised.
Binds 2 [Ni-4Fe-5S] clusters per homodimer.
Binds 1 zinc ion per subunit. The inability to bind a second zinc ion may explain its very poor exonuclease activity (PubMed:21893285).
Binds 1 Cu(+) ion.
Binds 1 Cu(2+) ion.
Magnesium is required for both helicase and nuclease activity; its relative concentration alters helicase speed and nuclease activity in a complicated fashion.
Magnesium is required for activity, even if it seems to interact primarily with the substrate.
Mg(2+), and possibly also Mn(2+).
Binds 1 protoheme IX center (heme b558).
Divalent metal cation. Requires Mn(2+), Co(2+) or Ni(2+).
Binds 2 Ca(2+) ions per subunit. One ion binds at a conserved binding site (GCXCG), whereas the second ion binds at a flexible site and may act as a supplemental electrophile as well as a backup.
Divalent cations in the following order of efficiency: cobalt, magnesium, and, to a lesser extent, nickel ions.
Binds 1 FAD. The FAD is in its reduced state.
Binds 1 F420 non-covalently per subunit. The F420 is in its oxidized state.
Mg(2+) is essential for the GTP-binding, but GDP-binding does not require a metal cofactor.
Binds 1 [4Fe-4S] cluster. The cluster is likely coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 zinc ion per subunit. It helps recognize and select the amino acid substrate, and thus has neither a purely catalytic or structural role (PubMed:10881191).
Binds 1 divalent metal cation per subunit. Fully active with Ca(2+), Mg(2+) or Zn(2+) ions. Active at 35% with Mn(2+) ion.
Binds up to 2 Ca(2+) per subunit.
Slightly more active with Mn(2+) than with Mg(2+).
Can also use magnesium, calcium and iron ions with lower efficiency.
Binds 2 heme b groups per subunit. Heme 1 is located at the cytoplasmic interface, heme 2 is located at the extracellular interface. Electrons are transferred from the extracellular to the cytoplasmic heme.
Binds 2 Mg(2+). Prefers Mg(2+), but can also use Mn(2+). In vitro, can also utilize other divalent cations such as Ca(2+).
Requires divalent cations for activity in the following order of efficiency: Mn(2+), Co(2+), Mg(2+) and Ni(2+) ions.
Binds 2 divalent metal cations (By similarity). Shows activity with Mn(2+), Co(2+) and Mg(2+) but shows no activity with Zn(2+) (PubMed:29752939).
Binds 1 [4Fe-4S] cluster, which is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Manganese or any other divalent metal ion.
Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Divalent metal cation. Highest activity with Co(2+), followed by Mg(2+), Mn(2+) or Ni(2+).
Although Mn(2+) can act as a cofactor, it is much less effective than Mg(2+).
Binds 8 zinc ions per octamer. Requires four zinc ions per octamer for full catalytic activity. Can bind up to 2 zinc ions per subunit.
May bind 2 [4Fe-4S] clusters.
Binds 1 pyridoxal 5'-phosphate per subunit.
Binds 1 magnesium ion per subunit. Can also use Zn(2+) as cofactor.
Binds 3 divalent metal cations (PubMed:23620482). Can use Mn(2+) with a lower efficiency than Zn(2+) ions (PubMed:23620482).
Binds 1 divalent metal cation per subunit (By similarity). Most active with Co(2+), Mg(2+) or Mn(2+). Has weaker activity with Fe(2+), Ni(2+) or Zn(2+) (PubMed:28854683).
Binds 1 FAD per subunit. FAD does not seem to be involved in catalysis but rather in the structural stabilization of the enzyme.
Reduced FMN (FMNH(2)). It can also use FAD, however FMN is the preferred cofactor.
Binds 1 thiamine pyrophosphate per subunit. During the reaction, the substrate forms a covalent intermediate with the cofactor.
Divalent metal ions. Magnesium seems to be the preferred ion.
Binds two Mg(2+) ions per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
C-terminally truncated SLFN14 endoribonuclease: Requires manganese and magnesium for its endoribonuclease activity.
Binds 1 zinc ion per subunit (for dihydroorotase activity).
Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:11893335). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (PubMed:11893335).
Divalent metal cations. Can use Mg(2+), Co(2+) and, to a lesser extent, Mn(2+) ions.
Binds 2 magnesium ions per subunit. One ion coordinates the alpha and beta phosphates of ATP, and the other coordinates the beta and gamma phosphates.
Can also use Ni(2+), Co(2+) and Fe(3+).
Can also use manganese or cobalt.
Can also use ammonium ions.
Divalent metal cation. Has preference for nickel and cobalt ions for the HMG aldolase activity. Has preference for zinc ions for the OAA decarboxylase activity.
Magnesium may play a role in formation and maintaining of proper enzyme conformation and multimerization.
Binds 1 Zn(2+) ion per subunit. At lower physiological Zn(2+) concentrations, Mg(2+) replaces Zn(2+). The nature of the bound ion affects the speed of the RNA degradation reaction and, to a limited extent, base selectivity.
Divalent metal cation. Highest activity with cobalt or manganese.
Divalent metal ions. Mg(2+), Co(2+), Mn(2+), Zn(2+) or Ca(2+).
Divalent metal cations. Zn(2+) is more efficient than Mg(2+).
Binds 3 heme c groups covalently per subunit.
Binds 2 Mg(2+).
Binds 1 Mg(2+) ion per subunit. Can also use other divalent metal cations as Mn(2+), Co(2+) and Zn(2+).
Probably binds two or three Mg(2+) ions per subunit.
Also accepts various divalent metal ions.
Divalent cation. Prefers Mg(2+), Mn(2+) or Co(2+).
Catalytic activity is higher with Mg(2+) (By similarity). According to PubMed:7998949 the cofactor is Mn(2+), while Mg(2+) is much less effective.
Binds 1 Zn(2+) ion per subunit (PubMed:15381710, PubMed:15826652, PubMed:19128030, PubMed:24314009). Fully functional with a mononuclear metal center. Does not require a second metal for activity, although the conservation of the second metal-binding site during evolution leaves open the possibility that a second ion might bind in vivo (PubMed:24314009).
Binds 2 FAD per tetramer.
Requires divalent cations for activity.
Weak activity with Fe(2+), Co(2+) and Zn(2+), but no activity with Ca(2+), Mg(2+) or Cu(2+).
Binds 1 zinc ion per subunit. Zinc is required for binding of the SecB chaperone to the extreme C-terminus of SecA.
Binds 1 [4Fe-4S] cluster. The cluster does not appear to play a role in catalysis, but is probably involved in DNA-binding and proper positioning of the enzyme along the DNA strand.
Binds one Mg(2+) per dimer. Can also use other divalent cations.
Binds 1 divalent metal cation per subunit. Seems able to use Mg(2+), Mn(2+) or Co(2+).
Binds 1 Mn(2+) per subunit (PubMed:23671667, PubMed:33763291). Can also use Mg(2+), with lower efficiency (PubMed:33763291).
Binds 1 K(+) per subunit.
Binds tightly a transition metal ion; prefers Co(2+) over Mn(2+).
Mg(2+) ions are required for optimal catalytic activity.
Binds 3 [4Fe-4S] clusters (PubMed:20218986). The first cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Can also use Co(2+) or Ca(2+) in vitro.
Binds 2 Mg(2+) ions per subunit (PubMed:25787157). Mg(2+) is required for catalysis and for stabilizing the dimer (PubMed:25787157). Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformation (PubMed:25787157). Inhibited by high levels of Mg(2+) (By similarity).
Adopts alpha-helical conformations in the presence of divalent cations and is unstructured in the absence of divalent cations.
Probably binds 2 Mn(2+) per subunit; only 1 is seen in the structure (PubMed:15800637) (By similarity). Mn(2+) is the preferred cation for cleavage, Co(2+) can be used but not Mg(2+), Ca(2+), Cu(2+), Fe(2+) or Ni(2+) (PubMed:25925567).
Divalent metal cations. Has optimal activity with Mg(2+).
Binds 2 Zn(2+) ions per homotetramer.
Binds 2 divalent metal cations per subunit. Can use cobalt, and to a lesser extent, nickel, manganese or copper.
Binds 1 Mg(2+) ion per subunit. Is also active with manganese ions (in vitro).
Divalent metal cations. Mn(2+) is 4-fold better than Mg(2+).
Mg(2+) cannot be replaced by Mn(2+).
Binds 1 Fe(2+) per subunit.
Binds 1 Mn(2+) ion per subunit. Can also use Co(2+) ion.
Divalent metal cations. Calcium or manganese or magnesium.
Can also use Mn(2+) or Co(2+), with lower efficiency.
Binds 1 zinc ion per subunit (PubMed:9405410, PubMed:11939797). Zinc plays a key role in activating an organic thiol substrate for nucleophilic attack on an alkyl-donating substrate (PubMed:11939797).
The 3Fe-4S cluster is redox-responsive, binds 1 cluster per monomer.
Binds 1 [4Fe-4S] cluster per subunit. [4Fe-4S]-binding affects RNA-binding activity, thereby inhibiting activity of the protein.
Manganese or magnesium. Has higher activity with manganese.
Binds 1 [4Fe-4S] cluster. The [4Fe-4S] cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Probably binds 2 heme groups via the 2 magnetochrome (MCR) motifs.
Manganese or cobalt are requested for FAD-AMP lyase activity.
Protospacer integration in vitro also occurs with Mn(2+) and also requires low concentrations of KCl (PubMed:25707795). The transesterification function works equally well with Mg(2+), Mn(2+) or Co(2+) in vitro (PubMed:26284603).
Binds 1 manganese ion per subunit. Can also use Fe(2+) and Co(2+). The unusual metal binding site is heavily hydrated, coordinated with an aspartate side chain and five water molecules, and likely plays a role in anchoring the PsiMP phosphate.
Can also use magnesium with lower efficiency.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine, the other is coordinated via 3 cysteines and maybe direct contact with the SboA precursor.
Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit, that serves as photoantenna.
Binds 3 [4Fe-4S] clusters per homodimer. Contains two stable clusters in the N-termini and one labile, bridging cluster between subunits of the homodimer.
Binds 1 Mg(2+) ion per monomer. Mg(2+) is important for dimerization.
The cofactor facilitates a conformational change critical to the transport cycle. The binding of Ca2+ from extracellular fluid activates the transporter by triggering a conformational change that enables the transition from the open outward to open inward states.
Magnesium. Fe(2+) or Cu(2+) ions are very less efficient as cofactors.
Binds two heme c groups per subunit. Heme 1 appears to be in the active site, whereas heme 2 probably functions in electron transfer.
Mg(2+) and, at a lesser extent, Mn(2+).
Mn(2+), Co(2+) and Mg(2+) enable equal cleavage, Zn(2+) is less active and Ni(2+) is essentially inactive.
Binds 3 Mn(2+) ions per subunit (PubMed:15530359). The third manganese ion is unlikely to be involved in catalysis but contributes instead to stabilize a flap segment, which is partially disordered in the absence of bound metal (PubMed:17961594).
Binds 1 divalent metal cation per subunit. Displays higher activity with Co(2+), however, Zn(2+) may be the physiological metal cofactor.
C-terminally truncated SLFN14 endoribonuclease requires manganese and magnesium for its endoribonuclease activity.
Binds 1 [4Fe-4S] cluster. The cluster has a structural role.
Binds 4 to 6 Zn(2+) ions.
Manganese. Mn(2+) can be replaced by Mg(2+).
Endoribonuclease function is magnesium-dependent.
Binds 2 [4Fe-4S] clusters (PubMed:21103360) (By similarity). The two centers are coupled but must possess different redox potentials (PubMed:21103360).
Binds one FMN non-covalently per monomer.
Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. All three [Fe-S] clusters are required for MftC modification of MftA.
Binds 2 [4Fe-4S] clusters (PubMed:24854437). One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable).
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-SPAC806.02c heterotetramer.
Requires a divalent metal cation such as Mn(2+), Mg(2+), or Ca(2+).
Highest activities are measured with Mn(2+). Can also utilize Co(2+).
Binds 1 divalent metal cation per subunit. Manganese, iron, cobalt or nickel enhance activity.
Binds 1 NAD(+) per subunit. Is only active with NAD(+), not NADH.
Binds 1 [4Fe-4S] cluster per subunit. This [4Fe-4S] cluster is referred to as N2.
Binds 1 Cu(+) ion per subunit.
Binds 1 Mo-molybdopterin cytosine dinucleotide (Mo-MCD) cofactor per subunit.
Mg(2+) is required for RNase activity (PubMed:22561375).
Binds 1 zinc ion per subunit (PubMed:9548961, PubMed:10769139, PubMed:11732895, PubMed:11732896). Also able to use cobalt and manganese ions, but less efficiently (PubMed:10769139).
Requires a divalent metal cation for DSD activity, with a preference for Co(2+) but can also use Ni(2+), Mn(2+) and Mg(2+).
Mn(2+) ion stimulates activity.
Probably binds 2 metal cations. In vitro during a short incubation, Mn(2+) is most efficient on linear or supercoiled dsDNA, nicks but only poorly digests dsDNA with Co(2+), Ni(2+) or Zn(2+). When purified from E.coli Ca(2+) and Mg(2+) are the most abundant metals.
The crystal structure with reduced Cu(1+) has also been determined (PubMed:10320332).
Binds 1 divalent metal ion per subunit.
Co(2+), Mn(2+) or Ni(2+).
Binds 2 Mg(2+) (PubMed:27284197). Prefers Mg(2+), but can also use Mn(2+) (PubMed:27284197). In vitro, can also utilize other divalent cations such as Ca(2+) (PubMed:27284197).
Binds 8 Ca(2+) ions per subunit.
Binds 11-14 calcium ions per subunit.
Shows highest activity in vitro with Co(2+), Mn(2+) and Ni(2+).
Mg(2+) is required for RNase activity.
Unlike other alpha-(1,3)-fucosyltransferases, appears not to require a divalent metal cation as cofactor.
In the presence of Zn(2+) ions, activity is 13% of maximum, in the presence of Mn(2+), Cu(2+), Fe(2+) or Co(2+) ions, activity is very low. In the absence of metal ions, there is no activity.
Binds 1 [2Fe-2S] cluster per subunit (By similarity). Binds to divalent metal cations (PubMed:12606038).
Binds two Mg(2+), but the interaction with the protein is mostly indirect.
Binds 2 [Ni-4Fe-4S] clusters per homodimer.
Binds 1 Fe(2+) ion per subunit. Since MptB requires Fe2(+) for activity, the Fe(2+) ion likely has a catalytic role. The enzyme is also active under high concentrations of Mn(2+) in vitro.
Binds 1 Zn(2+) ion per subunit. The Zn(2+) ion is proposed to have a structural role.
Binds two metal ions per subunit. Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals: site 1 is occupied by Zn(2+), Mn(2+), Mg(2+) or Co(2+), while the tight binding site 2 can be occupied by only Zn(2+) or Co(2+) (PubMed:16519517). One Zn(2+) ion is tightly bound to site 2 and essential for enzyme activity in vivo, while site 1 can be occupied by different metals to give different enzymatic activities (PubMed:16519517). Mn(2+) is required for Cys-Gly hydrolysis activity (PubMed:16519517). A third metal binding site may serve a structural role, possibly stabilizing part of the interface between the N-terminal and the catalytic domain (PubMed:7619821).
Magnesium. It could be replaced to some extent by nickel, manganese or cobalt.
Binds 1 heme (probably heme b) per subunit, probably hexa-coordinated, which inhibits PDE and ATPase. The Fe(2+) binds CN(-), CO and NO.
ATPase activity (residues 84-303) prefers Mg(2+) over Mn(2+).
For phosphodiesterase activity (residues 84-695), probably binds 2 Mn(2+) per subunit, can also use Co(2+), Mg(2+) or Ni(2+).
Maximal DNA relaxation at 5.0 mM MgCl(2).
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid.
Binds 1 sodium ion per subunit. The sodium ion has a structural role.
Requires the presence of a divalent metal cation for activity. Can use magnesium, manganese or cobalt.
Binds 1 Fe(2+) cation per subunit. Ni(2+) and Zn(2+) can be used to a lesser extent.
Binds 1 Mg(2+) per trimer.
Binds 16-17 chlorophyll a molecules per subunit.
Fe-coproporphyrin III acts as both substrate and redox cofactor (By similarity). Was originally thought to use heme as a cofactor (PubMed:25908396).
Requires divalent metal ions, preferentially magnesium, for activity (Probable). Binds 2 divalent metal cations per subunit (PubMed:12904291, PubMed:15213409). Zinc and calcium, which are present in the crystals do not support the enzymatic reaction.
Without tungstopterin acting as a cofactor, this protein's function is compromised.
Binds 1 Mo-molybdopterin (Mo-MPT) or 1 tungstopterin cofactor per subunit.
Binds a di-iron center symmetrically between each dimer. Fe(2+), Zn(2+) and Co(2+) but not Fe(3+), Ca(2+), Mg(2+) or Mn(2+) induce protein oligomerization.
Binds 1 Ca cation symmetrically between each dimer in what is called the entry site; in vivo this may be an Fe cation.
Mg(2+). Mg(2+) can partially be replaced by Mn(2+) and Fe(2+).
Binds 3 zinc per trimer.
Divalent metal ions. Required for self-glucosylation. Manganese is the most effective.
Without sulfate acting as a cofactor, this protein's function is compromised.
Binds 1 sulfate ion per subunit.
Binds 1 2Fe-2S cluster per subunit.
Does not require Ca(2+) or any other cation for activity.
Binds 3 Mg(2+) ions per subunit. Can also use Mn(2+) and Fe(3+) but less efficiently, and other divalent cations such as Zn(2+), Fe(2+), Co(2+), Cu(2+) and Ni(2+) are nearly completely inefficient as cofactors.
Requires divalent cations for activity. Mg(2+) gives the maximal activity, but the enzyme can also use Ca(2+), Mn(2+), Fe(2+) or Co(2+) ions, but not Zn(2+) or Cu(2+) ions.
Can also bind other divalent metal ions with lower efficiency (PubMed:22183084). Calcium ion binding contributes to the thermostability of the protein (PubMed:22183084).
Binds 1 divalent metal ion per subunit. Mn(2+) is the most efficient metal, but can also use Co(2+), Ni(2+) and Fe(2+), and to a lesser extent Mg(2+). Cannot use Zn(2+).
Binds 3 divalent metal cations (PubMed:23620482). Uses Ca(2+) ions with ssDNA as substrate (PubMed:23620482). Can also use Mn(2+) with lower efficiency with ssDNA and dsDNA as substrates (PubMed:23620482).
Binds 1 zinc ion per subunit. Is able to bind nickel instead of zinc.
Divalent metal cations. The best activity is observed with Co(2+), where the activity is 4 and 2.5 times greater than that with Mg(2+) and Mn(2+), respectively.
Binds 1 Zn(2+) per subunit, which may stabilize the HNH Cas9 architecture.
Dependent on a divalent cation for ethanol oxidation, among which Mn(2+) is optimal. Compared with the oxidation reaction, displays about 30% acetaldehyde reduction in the absence of divalent cation. Shows maximal reduction activity in the presence of Fe(2+).
Uses manganese ion preferentially to magnesium ion.
Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per subunit.
Binds 1 Fe(2+) ion per subunit (PubMed:12450410, PubMed:25760618). In vitro can also use Co(2+) or Mn(2+) (PubMed:12450410).
Divalent metal ions. Mg(2+) or Mn(2+).
Binds 1 divalent metal cation per subunit. Ni(2+) ion is seen in the structure.
Binds 1 zinc ion per subunit (PubMed:25559274). Can also use Cd(2+), Ni(2+) or Cu(2+) (PubMed:16475788, PubMed:17128965).
Mg(2+). Exhibits no peptide cleavage activity without Mg(2+), regardless of the presence or the absence of ATP. Can also use other divalent cations such as Ni(2+), Ca(2+), Mn(2+) and Co(2+).
Binds 2 Zn(2+) ions per homotetramer. Zinc ions are bound between subunits and are essential for homotetramerization and catalytic activity, but not for RNA binding. In the absence of zinc, the protein dissociates into inactive dimers.
Chloride.
Does not seem to have metal cofactors; no metal ions were found via inductively coupled plasma atomic emission spectroscopy, and the residues that bind metal in homologs are not conserved.
Binds 1 divalent metal ion per subunit. Mn(2+) is the most efficient metal, but to a lesser extent, can also use Co(2+), Ca(2+), Fe(2+), Mg(2+), Sr(2+), and Ni(2+). Cannot use Zn(2+), Cu(2+) or Cr(2+).
A flavin ligand is bound near the 3-fold axis channel; FMN is consistent with the observed density, absorbance data and mass spectrometry.
Binds 2 Fe(2+) ions per subunit (PubMed:18678932). Active in the presence of various divalent cations such as Fe(2+), Zn(2+), Cd(2+), Co(2+) and Mn(2+) (PubMed:17306828, PubMed:17630782, PubMed:18535849, PubMed:18678932, PubMed:18831553). Fe(2+) is probably the native metal ion (PubMed:18678932).
Glutathione is required for the MAAI activity.
Binds 2 manganese or magnesium ions per subunit.
Binds 1 [4Fe-4S] cluster. The iron-sulfur cluster is essential for protein stability and helicase activity.
Autophosphorylates in the presence of Mg(2+) and/or Ca(2+), but only Mg(2+) ions promote phosphotransfer to MtrA.
Isoform 1 binds 3 zinc ions. Isoform 2 binds 2 zinc ions.
Binds 2 heme groups per subunit. One heme group is bound covalently by a single cysteine link, the other one non-covalently.
Heme-binding is redox-active and coordinates various ligands such as imidazole, dimethyl sulfide, and carbon monoxide depending on the redox state. The redox state of the heme cofactor influences on autophosphorylation activity: while reduced protein does not autophosphorylate, oxidized protein promotes autophosphorylation signal.
Besides the tightly bound Zn(2+) ion, TRZ1 requires additional Ca(2+), Mn(2+) or Mg(2+) for pre-tRNA processing, while bpNPP hydrolysis occurs without addition of metal ions but is stimulated 2- to 3-fold when free Mn(2+) or Zn(2+) ions are added.
Binds 1 [4Fe-4S] cluster per subunit. This cluster is stable to O(2) but very reactive to nitric oxide (NO). Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit.
Can also use Mg(2+), Ca(2+) and Zn(2+), with lower efficiency.
Binds 1 FAD per subunit, non-covalently bound to the BLUF domain.
Binds 1 Mg(2+) per subunit. Is also active with Mn(2+). Mn(2+)-activated enyzme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over. Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues.
Binds 4 copper ions per subunit.
Zn(2+) probably constitutes the cofactor in vivo.
Binds 1 Mg(2+) ion per dimer.
Magnesium may be the real cofactor in vivo.
Binds 2 divalent metal cations per subunit (PubMed:15087448). Can use a diiron cofactor for catalysis (PubMed:32967910). However, activity is much higher in vitro in the presence of both iron and manganese, which implicates a heterodinuclear iron/manganese cofactor (PubMed:36122239).
Binds 1 heme b (iron(II)-protoporphyrin IX) group covalently per monomer.
Binds 1 Mg(2+) ion per subunit. In contrast to other surE homologs, is essentially inactive with other divalent cations.
Binds 1 Mg(2+) ion per subunit (PubMed:25295175). Is also active with manganese ions (in vitro) (PubMed:11431477, PubMed:11447108).
Can use both pyridoxamine 5'-phosphate (PMP) and pyridoxal 5'-phosphate (PLP) as cofactors.
PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a' dimer, A0 is one or more divinylchlorophyll a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Binds 1 heme group per subunit; upon expression in E.coli it purifies predominantly in the Fe(2+)-oxy form, binding O(2) tightly even under anaerobic conditions.
Binds 2 copper ions per subunit (PubMed:19453274, PubMed:20204476). The two coppers forms a binuclear cluster (By similarity).
Binds 6 Cu(2+) ions per subunit. Decreased of the heat stability in the presence of metal ions (e.g. K(+), Ca(2+), Cu(2+), Sr(2+) and Mg(2+)).
Binds 1 FAD covalently per subunit (PubMed:24374335, PubMed:26644464, PubMed:10373108). Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE (PubMed:24374335, PubMed:26644464).
Binds 1 FAD per subunit (PubMed:4628374, PubMed:16095622). The FAD is covalently bound to the protein (PubMed:4628374, PubMed:5083098, PubMed:2680607, PubMed:2115879, PubMed:16095622).
Binds 2 divalent metal cations per subunit (PubMed:17727341, Ref.20). Site 2 has a preference for magnesium and/or manganese ions (By similarity).
Binds 3 Mg(2+) ions per subunit (PubMed:12906832). Activity is highest with Mn(2+). Can also use Zn(2+) or Co(2+), with lower efficiency (PubMed:27683242).
Maximal DNA relaxation at 5.0 mM MgCl(2) (PubMed:16313624).
Contains an active site Fe binuclear center, which is coordinated by Cys-503 and by non-protein ligands including 2 sulfur atoms, 1 water and 5 cyanide or carbon monoxide ligands.
Can also use Ni(2+), Co(2+) or Fe(2+), with lower efficiency.
Binds 2 Zn(2+) ions per subunit (PubMed:27435900).
Divalent metal ion. Manganese, iron, cobalt and nickel ions enhance activity whereas magnesium, zinc, calcium and strontium do not.
Endonuclease activity on target dsDNA requires Mg(2+) (PubMed:22745249). The RuvC-like nuclease domain should have 2 divalent cations, while the HNH domain should have 1. Crystals are often soaked in MgCl(2) or MnCl(2+).
At low magnesium concentrations there is no nuclease activity, but helicase activity is unaffected.
Can use Mg(2+) and Mn(2+) with equal efficiency in vitro, and to a lesser extent, Ni(2+).
Binds 2 divalent metal cation ions per subunit. Fe(2+), which is the most abundant metal ion found in the X-ray structure, may constitute the physiological cofactor.
Manganese. Cobalt, iron and magnesium can be used to a lesser extent.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (PubMed:23282011). The other is coordinated via 3 cysteines and maybe direct contact with the SkfA precursor (Probable).
Pre-crRNA processing is metal independent, while crRNA-guided target RNA cleavage is dependent on divalent metal (i.e. inhibited by EDTA) (PubMed:27669025).
Have significantly greater activity in the presence of Mn(2+) than Mg(2+).
Also liganded by DNA (PubMed:28319084). Cleavage probaby requires 2 divalent metal cations (By similarity).
Mg(2+) is required for RNase activity (PubMed:19322177).
Binds 1 zinc ion per subunit (PubMed:1429690, PubMed:11700044, PubMed:15592454, PubMed:19351593, PubMed:22363010).
The FAD is tightly bound.
Binds 2 magnesium ions per subunit. A third magnesium ion may be bound between subunits.
Binds 2 zinc divalent cations per subunit.
Mg(2+) is essential for activity. However, Mn(2+) is able to functionally replace Mg(2+) with a 50% reduced efficiency, whereas no MCD is produced with other divalent cations like Co(2+) or Ni(2+).
Binds 3 Ca(2+) ions per subunit. The calcium ions probably have a structural role.
Binds 1 FAD per subunit, which helps bind the antibiotic substrate.
Divalent metal cation. Requires divalent metal cation for binding of dermatan sulfate substrate, whereas it is not necessary for the binding of chondroitin sulfate substrates. Prefers Ca(2+) or Mg(2+), binding 1 ion per subunit.
Has a very strong preference for NAD(+) over NADP(+).
Also has weak activity in the presence of Mg(2+) or Ca(2+) ions.
Magnesium. It can also use divalent cations such as manganese, calcium, zinc, iron, cobalt and copper.
Binds 1 Mg(2+) per subunit (PubMed:23722159). Is also active with Mn(2+). Mn(2+)-activated enyzme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over. Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues (PubMed:23722159) (By similarity).
Binds 1 coenzyme F430 non-covalently per MCR heterotrimeric complex. Coenzyme F430 is a yellow nickel porphinoid. Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced, probably to the Ni(I) oxidation state.
Binds 1 [Ni-Fe-S] cluster per subunit.
Binds 2 [4Fe-4S] clusters per homodimer.
Binds 3 Mg(2+) ions.
Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery to the Rieske protein is mediated by components of the iron sulfur (Fe-S) cluster assembly machinery that reside in the mitochondrial matrix (including HSC20 and LYRM7).
The heme is bound between the two transmembrane subunits CybS and CybL.
Cannot use Mg(2+) as a cofactor.
The binding sites for NAD(+) are contained in the regulatory subunit DHSp.
Mn(2+) and Fe(2+) serve as a cofactor, Mg(2+) is a very poor cofactor (Ref.2). Binds 2 Mn(2+) per monomer, with unusually long metal coordination distances so that neither is tightly bound (PubMed:19706507).
Binds 2 divalent metal cations per subunit (PubMed:15260978, PubMed:15576036). Site 2 has a preference for magnesium and/or manganese ions (By similarity).
Shows an absolute requirement for Mg(2+) for activity. Mg(2+) cannot be replaced by Ca(2+), Mn(2+) or Zn(2+).
Without phosphate acting as a cofactor, this protein's function is compromised.
Shows an absolute requirement for inorganic phosphate for activity. The function of the phosphate may involve stabilizing the protein conformation and/or initiating protein aggregation.
Contains a nonheme dinuclear iron cluster that stabilizes a peroxo intermediate.
Ca(2+) or Mn(2+). Mg(2+) can be used to a lesser extent.
tDNA cleavage prefers Mn(2+) over Mg(2+) (PubMed:27035975). Cleavage probaby requires 2 divalent metal cations (By similarity).
Binds either 1 Fe or Ni cation per monomer (PubMed:26858196). Iron-binding promotes an acireductone dioxygenase reaction producing 2-keto-4-methylthiobutyrate, while nickel-binding promotes an acireductone dioxygenase reaction producing 3-(methylsulfanyl)propanoate (PubMed:26858196).
Binds 1 Zn(2+) ion per subunit; 2 are expected compared to other E.coli strains.
Some evidence supports a zinc cofactor.
Appears to contain about 1 [4Fe-4S] cluster per heterodimer FldBC.
No flavin coud be detected in the FldABC complex, and the addition of FAD, FMN or riboflavin to the dehydratase do not increase enzymatic activity.
Binds 1 zinc ion per subunit. The zinc ion is necessary for interaction with host MHC class II molecules.
Possesses two zinc-binding sites. The zinc ion is necessary for the toxin interaction with MHC class II.
Binds 2 Mg(2+) ion per subunit. Mn(2+) reduces cleavage sequence specificity (PubMed:8001122, PubMed:7638215). Cations are not required for DNA-binding (PubMed:8195150).
Binds 2 [4Fe-4S] clusters per subunit. The [4Fe-4S] clusters are referred to as N6a and N6b.
Binds 1 FAD per heterodimer.
Binds 1 Mg(2+) ion per subunit (By similarity). Can also use Mn(2+) (PubMed:25037224, PubMed:25521849).
Binds 3 manganese or magnesium ions per subunit.
Binds 2 heme groups via the 2 magnetochrome (MCR) motifs.
Divalent cations stabilize the toxin the in alpha-helix conformation. Zinc also stabilizes the alpha-helical conformation.
Mg(2+) contributes to binding the 5'-end of the gRNA.
Binds 2 [4Fe-4S] clusters (By similarity). The two centers are coupled but must possess different redox potentials (By similarity).
Binds 2 Fe(2+) ions per subunit. Can also use Mn(2+), with lower efficiency.
PSI electron transfer chain: 5 divinyl chlorophyll a, 1 divinyl chlorophyll a', 2 phylloquinones and 3 4Fe-4S clusters. PSI core antenna: 90 divinyl chlorophyll a, 22 carotenoids, 3 phospholipids and 1 galactolipid. P700 is a divinyl chlorophyll a/divinyl chlorophyll a' dimer, A0 is one or more chlorophyll divinyl a, A1 is one or both phylloquinones and FX is a shared 4Fe-4S iron-sulfur center.
Binds 2 heme groups. One heme group is bound covalently by a single cysteine link, the other one non-covalently.
Mg(2+) and Mn(2+) are more tightly associated with the active site motifs (D(D/E)XX(D/E) and NSE) and thus lead to more efficient removal of PPi.
Divalent metal cation. Can use Mn(2+) or, to a lower extent, Mg(2+) or Zn(2+). Half-maximal activation occurs between 10 and 100 uM of Mn(2+) whereas maximal activation occurs with 10 mM of Zn(2+) or Mg(2+).
Shows highest activity in vitro with Co(2+) and Ni(2+).
Binds 1 [4Fe-4S] cluster per subunit (PubMed:17609386). Following nitrosylation of the [4Fe-4S] cluster binds 1 [4Fe-8(NO)] cluster per subunit (PubMed:17609386).
Mg(2+). The phosphatase activity is also stimulated by cobalt ions, whereas baryum, zinc, and manganese ions are less effective stimulators.
Binds 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable). All three [Fe-S] clusters are required for MftC modification of MftA (By similarity).
Binds 2 coenzyme F430 non-covalently per MCR complex. Coenzyme F430 is a yellow nickel porphinoid (By similarity). Methyl-coenzyme-M reductase is activated when the enzyme-bound coenzyme F430 is reduced to the Ni(I) oxidation state (By similarity).
Divalent cations, Mg(2+) and Zn(2+) are best.
Binds 2 Mg(2+) ions per subunit. Required for catalysis and for stabilizing the dimer.
Binds 2 zinc ions per subunit. After heterologous expression, a stoichiometry of 1 zinc ion per subunit is observed.
Zn(2+) is involved in coenzyme M activation: in the absence of coenzyme M, zinc is coordinated by a single sulfur ligand and three oxygen or nitrogen ligands. In the presence of coenzyme M, one oxygen/nitrogen-ligand is replaced by sulfur, probably due to ligation of the thiol group of coenzyme M.
Binds 1 divalent metal cation per subunit. Co(2+) is the preferred cofactor.
Probably binds 2 heme groups via the magnetochrome (MCR) motifs.
Binds 2 heme groups via the magnetochrome (MCR) motifs.
Mg(2+) is the most effective ion, but it can be replaced with Co(2+), Ni(2+), Zn(2+) or Mn(2+).
Optimal activity at 0.5-1 mM CoCl(2), also functions with Mn(2+), for a construct missing residues 1-80.
Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.
Binds 1 Mg(2+) ion per subunit. Can also use Mn(2+), Co(2+) and Zn(2+) to a lesser extent.
Divalent metal cations. Mg(2+) or Ca(2+).
Binds 2 Zn(2+) ions per subunit. Contains one structural ion and one catalytic ion that seems to be less tightly bound at the site (PubMed:16233775). Zn(2+) can be replaced by Mn(2+) or Co(2+) to some extent (PubMed:15902509).
Can use both zinc and magnesium that is complexed with ATP. However, magnesium seems to be the preferred metal used under physiological conditions.
Binds 1 zinc ion per subunit. Only 1 ligand appears to be Cys, the other are thought to be His and either backbone amides or solvent (PubMed:22196016).
Binds 1 Mn(2+) ion per subunit. Although a Mg(2+) ion is seen in the structure, galacturonidase activity was shown using manganese (PubMed:23416295).
Binds no magnesium or manganese ion per subunit.
Divalent metal cations. Prefers Ca(2+) or Mg(2+) which have a synergistic effect on activation.
Binds 1 mole of FAD per mole of enzyme. Also able to use FMN, but the activity is less than that obtained with FAD.
Mn(2+) allows activity only at low concentrations. In the presence of low concentrations of Co(2+) or Ni(2+), activity could be measured, but at concentrations above 0.2 mM, strong inhibition is observed.
Does not use FAD as a cofactor.
Binds Mg(2+), Co(2+) or Mn(2+).
Binds 1 Mg(2+) per subunit, in one structure a second Mg(2+) was seen.
Binds Mg(2+) or Mn(2+). Maximal rates of activity with 1 to 4 mM Mg(2+) and only one third of activity with Mn(2+). No activity with Zn(2+) or Ca(2+).
Binds 1 NADP(+) per subunit. The NADP(+) cannot dissociate.
Magnesium. Can also use other divalent cations like manganese or calcium.
Divalent cation. Mg(2+) is preferred. Has Holliday junction resolvase activity solely in the presence of Mn(2+).
Binds 2 magnesium ions per monomer. Can also use manganese and iron.
Binds 1 sodium ion per monomer. Can also use potassium.
Binds 1 Mg(2+) ion per subunit. Ca(2+) may be able to substitute. 2 Ca(2+) ions are seen in the crystal structure; one of the two occupies the same site as Mg(2+) in other family members.
Binds 3 divalent metal cations (PubMed:23620482, Ref.7, PubMed:25157844). Use Mn(2+) and Ca(2+) as cofactors with ssDNA as substrate in basic conditions (pH 8) (PubMed:23620482). Can use Zn(2+) with lower efficiency with dsDNA and ssDNA as substrates in acidic conditions (pH 5.5) (PubMed:23620482, Ref.7, PubMed:25157844).
Binds 3 [4Fe-4S] clusters per heteropentamers.
Binds 8 heme groups covalently per monomer.
Manganese or magnesium. Required for optimal RNA cleavage rates.
Divalent metal cations; Mg(2+) or Mn(2+).
Binds 1 Fe(3+) ion per subunit. Electron spin resonance clearly indicates the presence of Fe(3+) (PubMed:16227621).
Binds 1 Fe(2+) or Zn(2+) ion per subunit. Electron spin resonance indicates the presence of either Fe(2+) or Zn(2+), while X-ray crystallography shows the presence of Zn(2+). Mn(2+) is not a cofactor (PubMed:16227621).
Divalent metal cations. Probably Zn(2+).
Both strand exchange and nuclease activities require magnesium, for the strand exchange activity, calcium can replace magnesium when the linear ds-DNA has been first resected with an exogenous endonuclease.
Binds 1 Mg(2+) ion per subunit. Can also use Co(2+), Zn(2+), Ni(2+) and Ca(2+) to a lesser extent.
Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+) (PubMed:12051843, PubMed:18642932).
Binds one K(+) per subunit which interacts with the alpha-phosphate of ATP analog and stimulates ATPase activity of the N-terminal fragment; Na(+) or water bind less well (PubMed:25849408).
Binds one Na(+) per subunit, with 4 ligands provided by water; may be able to bind K(+), the functional significance of this ion is unclear (PubMed:25849408).
Binds 2 manganese ions per subunit. Mn(2+) is inhibitory below pH 8 and activating above pH 8 (PubMed:24892992).
Does not require any standard metal (Mg(2+), Mn2(+), Ca(2+)).
Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Requires divalent cations for activity in the following order of efficiency: Mn(2+), Co(2+) and Mg(2+) ions.
Binds about 5 Ca(2+) per subunit (Probable). The metallopeptidase domain binds 1 Ca(2+), while each CDB binds 2 (Probable).
Binds 1 catalytic Zn(2+) per subunit.
Divalent metal cations. Mn(2+) or Co(2+) can be used.
Decapping activity is higher in the presence of manganese than in Magnesium or cobalt.
Without cysteine tryptophylquinone residue acting as a cofactor, this protein's function is compromised.
Contains 1 cysteine tryptophylquinone per subunit.
Binds 1 divalent metal ion per subunit. Mn(2+) is the most efficient metal, but can also use Co(2+), Ca(2+) and Mg(2+).
In the presence of oxygen, the A site-bound [2Fe-2S] cluster is labile and the B site-bound [4Fe-4S] cluster is readily converted into a [2Fe-2S] cluster, a reason why recombinant protein is often isolated with a single [2Fe-2S] cluster.
Mg(2+) or Mn(2+) required for ssDNA cleavage activity.
Binds 1 [4Fe-4S] cluster per subunit. It may be important for protein stability, since mutation of the Cys that binds the cofactor leads to a colorless, insoluble protein.
Binds 1 Zn(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium (By similarity). Tightly binds zinc (By similarity).
Binds 1 Mg(2+) ion per subunit. Binds 2 divalent metal cations per subunit: site 1 preferentially binds zinc, while site 2 has a preference for magnesium (By similarity). Binds magnesium less tightly than zinc (By similarity).
Binds 1 [4Fe-4S] cluster per subunit. The [4Fe-4S] cluster requires a potential lower than -600 mV for reduction.
Divalent metal cation. Highest activity with Mn(2+) followed by Mg(2+) and Co(2+).
Zinc. Can also use cobalt(II) with lower efficiency, but not copper(II), nickel(II) and manganese(II).
Magnesium. Can also use manganese or zinc.
Mg(2+) required for DNA supercoiling, DNA relaxation, DNA cleavage and DNA decatenation, Mn(2+) substitutes for relaxation but not supercoiling or cleavage activity (PubMed:16876125). Ca(2+) does not substitute for supercoiling activity (PubMed:22844097).
Has no RNase activity in the presence of Mg(2+), Ca(2+) or Zn(2+).
Binds 2 Zn(2+) ions per subunit (PubMed:27349982, PubMed:27725636).
Binds 2 Mg(2+) per monomer.
Binds 1 Zn(2+) ion per subunit. It is not clear if Zn(2+) or Mg(2+) is physiologically important.
The physiological metal is unknown.
Divalent metal ion.
Divalent cation. Ca(2+) and Mg(2+) have both been seen in crystal structures. Optimal DNA-binding requires Ca(2+).
Removal of zinc reduces the enzymatic activity by about 2-fold.
Binds two Mg(2+) ions per subunit.
Binds 1 spin-admixed [4Fe-4S] cluster.
Fe-coproporphyrin III acts as both substrate and redox cofactor (By similarity). Was originally thought to use heme as a cofactor (PubMed:20543190).
Binds 3 [4Fe-4S] cluster.
Zinc or iron.
Less efficient with Mn(2+).
Binds 1 Mg(2+) ion per subunit in the absence of substrate. Requires millimolar levels of Mg(2+) for maximal activity. Has low activity at micromolar concentrations of Mn(2+) and is inhibited at higher Mn(2+) levels. Can bind a second metal ion at a regulatory site, or after substrate binding.
Binds 1 FAD non-covalently per subunit.
Mg(2+). Mn(2+) is seen in the crystal structure; there are 2 Mn(2+) ions in the ATP-bound crystal and 1 Mn(2+) in the ADP-bound crystal.
In vitro glycosyltransferase activity is metal-independent.
Binds 1 Fe(2+) or Fe(3+) and 1 Zn(2+) ion per subunit, catalysis is optimal with 1 Fe and 1 Zn. Electron spin resonance indicates the presence of a mixture of protein molecules that contain either Fe(2+) or Fe(3+) and Zn(2+). Mn(2+) is not a cofactor (PubMed:19834746).
Zn(2+) is of critical importance for the stability of the enzyme.
PPPase is active in the presence of Mg(2+) ions, while no activity is observed in the presence of manganese ions.
ATPase occurs in the presence of Mg(2+) ions as well as Mn(2+) and Co(2+) ions.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The two iron atoms in each cluster are connected via a penta-sulfide bridge.
The corrinoid is probably a cobalamin.
Other ligands are provided by nucleic acid (PubMed:15800628, PubMed:15800629, PubMed:19187762).
Magnesium. Can also use other divalent metal cations as manganese and cobalt.
Divalent metal cations. Has highest activity with Mn(2+), followed by Zn(2+) and Co(2+).
Binds 10 calcium ions. The calcium may have a structural role.
Binds 1 divalent metal cation, Zn(2+), Co(2+) or Fe(2+).
Crystallized with and without Mg-ATP.
Binds 2 Zn(2+) ions per subunit. Mn(2+) and Co(2+) can substitute for zinc in reconstitution experiments.
Binds 2 Ca(2+) per subunit.
Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit. The oxidation state of Mo is +5. Is inactive in the presence of the tungsten-substituted form (W-MPT) of the cofactor.
Also able to use Mg(2+), Co(2+) and Ca(2+).
Requires Mg(2+), that can be substituted by Mn(2+).
Binds 2 Ca(2+) per subunit, this may not be the physiological cation.
Binds 4 Mn(2+) per subunit.
Binds 1 heme b (iron(II)-protoporphyrin IX) group per heterodimer.
Binds 1 nickel ion per mole of protein.
Binds 1 FAD per subunit. The role of this cofactor is not clear considering that the reaction does not involve redox chemistry. However, after removal of the FAD no AHAS activity can be detected (PubMed:9581571), indicating that the cofactor is essential. The large subunit alone does not bind FAD, and FAD is not necessary for association of the subunits.
Binds 1 Mg(2+) ion per subunit. Is not necessary for subunit association.
Binds 1 thiamine pyrophosphate per subunit. Is not necessary for subunit association.
Can also use Mg(2+).
Strict requirement of divalent metal cation. The highest activity is observed with combination of Mg(2+) and Mn(2+), followed by Mg(2+) > Mn(2+) > Co(2+). No activity detected with Ca(2+), Cu(2+) or Zn(2+).
Mg(2+). Other divalent cations can also be used.
Magnesium. Can also use Ca(2+), but less efficiently.
The heme b is bound between the two transmembrane cytochrome b560 subunits.
Binds 2 manganese ions per subunit. Can also use other divalent cation, with lower efficiency (PubMed:4990470).
Binds 1 iron-sulfur cluster per subunit. A study found 40-50% as [2Fe-2S] clusters, 15-25% as [4Fe-4S] clusters and the rest as paramagnetic iron.
Binds 4 magnesium or manganese ions per subunit.
Binds 1 Ca(2+) cation per subunit. Seen in 1 crystal structure, it is not clear if it is physiologically important.
Binds 2 Mg(2+) ions. Can also use Co(2+) and Mn(2+)ions.
Binds 1 cobalt ion per subunit (By similarity). Can also use Ni(2+) (PubMed:31950558).
Binds 6 phosphopantetheines covalently.
Binds 2 heme b (iron(II)-protoporphyrin IX) groups per subunit.
Calcium 4 is only bound to 1 residue in this protein.
Binds 1 Fe (3+) cation per subunit.
Activity is higher with Mg(2+).
Divalent metal cations. Has a preference for Mn(2+).
NAD is required for efficient interaction with E1A. Cofactor binding induces a conformation change.
Binds 1 Mg(2+) or Mn(2+) per subunit (PubMed:27744351). The type of divalent cation used by the enzyme affects the nucleotide specificity; Mg(2+) induces predominantly uridine (U) incorporation while Mn(2+) induces also substantial incorporation of both adenine (A) and cytosine (C) (By similarity).
The Zn(2+) ion may play a catalytic role.
Binds 2 heme groups per subunit. Heme 1, called the proximal or heme Bp in, is located at the cytoplasmic interface, heme 2, called the distal or heme Bd, is located at the periplasmic interface. Electrons are transferred from the periplasmic to the cytoplasmic heme.
Requires the presence of Mg(2+) to exhibit tRNA ligase activity.
Binds 2 [2Fe-2S] centers.
Divalent cations; Ca(2+) better than Mg(2+).
Endonuclease activity on target DNA requires Mg(2+).
Binds 1 zinc ion per subunit (PubMed:12166515, PubMed:19196988, PubMed:21366301, PubMed:21844374, PubMed:23897806, PubMed:23713488, PubMed:25299353, PubMed:26406322, PubMed:25645579, PubMed:26807544, Ref.21, PubMed:30537832, PubMed:32182520, Ref.24). Also, can use Mn(2+), Mg(2+) and Co(2+) with less efficiency (PubMed:12166515).
Binds 2 [4Fe-4S] cluster. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Binds 1 zinc ion per subunit. Can also be activated by other divalent cations such as iron, cobalt, or nickel.
Binds 1 Mg(2+) ion per subunit. Can also use divalent metal ions such as Co(2+), Mn(2+) and Ni(2+).
Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-metalloproteases under physiological conditions, and the catalytically relevant metal-binding site has been assigned to the histidine-containing high-affinity site. Also manganese has been proposed to be the physiological cofactor for human METAP2.
ssDNase activity requires Mg(2+), ssRNase activity does not require cations.
Requires a divalent metal cation for activity. Likely has a bi-nuclear metal center. Has the highest enzyme activity with Ca(2+), followed by Mg(2+).
Binds 1 heme group per subunit (PubMed:16477023, PubMed:25313323). In the active form, the heme iron is in its ferrous state Fe(+2). The catalytic cycle does not alter the oxidation state of the heme, but IDO1 is prone to autoxidation (PubMed:16574111).
Requires a divalent cation; Mg(2+) > Mn(2+) > Co(2+). Structures with 1 Mg(2+), or 1 or 2 Mn(2+) were determined; the authors conclude 2 metal ions are required for activity.
Binds 2 Mg(2+) ions per subunit. Each Mg(2+) binds only one residue (His-136 and Asp-175, respectively) of this protein, however the magnesium ions also bind substrates and water molecules to complete their coordination spheres (PubMed:2169413, PubMed:11790837). Can also use Mn(2+) and Cd(2+) ions, but the activity is less than that obtained with Mg(2+) ions (PubMed:2169413, PubMed:11790837).
Can act both with Mn(2+) and Mg(2+) as cofactor in vitro, but Mn(2+) is the preferred cofactor in vivo (PubMed:25255211, PubMed:25746449, PubMed:27989484, PubMed:30889508, PubMed:30633872). The polymerase activity incorporates correct dNTPs with much higher efficiency with Mn(2+) than with Mg(2+) (PubMed:25255211, PubMed:30889508). The fidelity is slightly more accurate when Mg(2+) is the cofactor compared to Mn(2+) (PubMed:25255211, PubMed:30889508). In the presence of Mn(2+), a conformational transition step from non-productive to productive PRIMPOL:DNA complexes limits the enzymatic turnover, whereas in the presence of Mg(2+), the chemical step becomes rate limiting (PubMed:30633872).
Cannot use Mn(2+) or Zn(2+).
Stoichiometry of heme binding is 2 PduOC:1 heme; the binding pocket is formed by a PduOC dimer. Full-length PduO also binds heme.
Mn(2+) and Co(2+) are almost as active as Mg(2+) for adenosylcobalamin synthesis.
Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-138-Cys-139 and the plane of Trp-266.
Binds 3 Mn(2+) per subunit (PubMed:24374628) (Probable). Target RNA cleavage occurs in the presence of Mn(2+) (PubMed:18754009, PubMed:19812667). Prefers Mn(2+) over Mg(2+) for tDNA cleavage (PubMed:24531762). tDNA cleavage occurs in the presence of Mn(2+) or Mg(2+) with a slight preference for Mn(2+), no cleavage occurs in the presence of Ca(2+) (PubMed:19812667, PubMed:24374628).
Translesion synthesis across abasic sites is more efficient with Mn(2+) compared to Mg(2+), replication of undamaged template is more efficient with Mg(2+).
Divalent metal cations, Mg(2+) or Ca(2+).
Binds 1 protoheme IX center (heme b595) per heterodimer, in conjunction with CydA.
Binds 1 zinc ion per subunit. The zinc is involved in both translation regulation via mRNA-binding and catalysis.
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. The second cluster is proposed to be involved in the electron-transfer mechanism for the catalytic cycle.
Binds 1 zinc ion per subunit (PubMed:19543288).
Divalent metal cations. Mg(2+), Mn(2+) or Co(2+) can be used.
Magnesium, but can also use calcium, manganese, nickel or zinc ions.
Crystallized with Mn(2+) to trap in the pre-reaction state.
Activity is highest with Mg(2+). Can also use Zn(2+), Co(2+), Mn(2+) and Ni(2+).
Binds two heme c groups per subunit.
Binds 2 calcium ions per subunit (PubMed:6609921, PubMed:9283074, PubMed:16880540). Calcium is inhibitory at high concentrations.
The substrate is directly bound to the heme iron.
Calcium may act as a cofactor.
Binds 2 metal ions per subunit. Manganese or magnesium.
Binds 2 Zn(2+) ions per subunit (PubMed:17362992). Also able to bind Mn(2+) (PubMed:25020232).
Binds 1 heme c group covalently per monomer.
Binds 1 heme group per subunit. The Fe(2+) state binds O(2) and CO while the Fe(3+) state can bind CN(-) and imidazole.
Requires a divalent metal cation. Activity is highest in the presence of Mn(2+), followed by Co(2+) and Ni(2+). Mg(2+) and Ca(2+) are poor metal cofactors. No activity with Cd(2+), Zn(2+) or Cu(2+).
Binds 2 Zn(2+) ions per subunit (By similarity). In vitro, shows higher activity with Co(2+), Mg(2+), Ni(2+) and Mn(2+) than with Zn(2+) (PubMed:20676924).
Binds 2 iron ions per subunit. During catalysis, TmpB uses a mixed-valent Fe(2+)/Fe(3+) cofactor.
The C-terminal 70 residues (positions 90-160) when overexpressed in E.coli bind Fe (PubMed:20870711). Might bind an [Fe-S] cluster in vivo (Probable).
Binds 2 Zn(2+) ions per 7S complex. The Zn(2+) ions are bound at the alpha-gamma interfaces.
Binds 2 divalent metal ions per subunit. Most effective are nickel and manganese.
Able to bind Fe(2+), but has only very weak PDE activity.
Metal-ion independent.
Optimal binding to GTP occurs between 5-10 mM Mg(2+), binding to GDP is inhibited at > 1 mM Mg(2+).
Probably binds 2 divalent metal cations per N-terminal polymerase domain. Mn(2+) is more effective than Mg(2+) for DNA polymerase activity.
Probably binds 3 Mn(2+) ions per C-terminal exonuclease domain. Mg(2+) cannot replace Mn(2+) for 3'-5' exonuclease activity.
Binds 2 FMN prosthetic groups per subunit. 1 FMN is bound covalently, while the other is non-covalent.
Binds 1 PQQ group non-covalently per subunit (PubMed:7730276). PQQ is inserted between disulfide Cys-139-Cys-140 and the plane of Trp-282 (By similarity).
Binds 2 divalent metal ions. Zinc, magnesium or manganese.
May also use Ca(2+). The enzyme has substantial activity without divalent cations.
Binds 1 magnesium ion per subunit. This ion is coordinated by a threonine and an asparagine, and by the alpha- and beta-phosphates of CDP.
Zn(2+) is the most effective divalent metal cation in vitro, followed by Co(2+), Mn(2+) and Mg(2+).
Less active with Ca(2+) or Co(2+). Not active with Cu(2+), Zn(2+), Sr(2+) or Ni(2+).
Glutathione seems to stabilize the enzyme, which loses activity rapidly in the absence of this compound.
Binds 2 heme c groups per subunit. Each heme is also bound by the other subunit.
Binds 1 iron-sulfur cluster per subunit, probably [2Fe-2S] cluster.
Activity is maximal in the presence of Mg(2+). The use of Mn(2+) or Co(2+) decreases ligase activity.
The 3Fe-4S cluster is redox-responsive, binds 1 cluster per monomer. It is coordinated by Cys-19 and other non-Cys residues.
Does not require metal ions for activity.
Mg(2+). Can also accept Mn(2+). The Mg(2+) is bound between two conserved protein residues and the ATP phosphate groups.
Binds 1 Mn(2+) ion per subunit. Can also use Zn(2+), Cu(2+) and Mg(2+) ions.
Binds 1 zinc ion per subunit (PubMed:9783750, PubMed:17173035, PubMed:21434688).
Binds 2 manganese ions per subunit. Mn(2+) is inhibitory below pH 8 and activating above pH 8 (By similarity).
Mn(2+) or Mg(2+) or Ca(2+). ATPase and nuclease activities are dependent on divalent cations, for ATPase Mn(2+) is marginally preferred over Mg(2+) or Ca(2+).
Mn(2+) works as well as Mg(2+), Co(2+), Ni(2+) and Zn(2+) work less well (PubMed:33290744). Bind 2 Mg(2+) per subunit (By similarity).
Mg(2+) is required for dsDNA cleavage.
Requires Mg(2+) for membrane fusion.
Binds 3 [4Fe-4S] clusters. Cluster 1 is referred to as proximal, cluster 2 as distal, cluster 3 as medial.
Cleavage is more efficient in Mn(2+), has weak cleavage activity with Mg(2+) (PubMed:32013676). Cleavage probaby requires 2 divalent metal cations (By similarity).
Binds more tightly in the presence of chorismate.
The heme b is bound between the two transmembrane subunits CybS and CybL.
Partial activity is seen with Co(2+), Ni(2+), Mn(2+), Zn(2+) and Fe(2+); in the presence of Mg(2+) these cations inhibit.
Binds 2 heme groups.
Mg(2+). Both Mn(2+) and Ca(2+) can substitute Mg(2+) ion in the autophosphorylation reaction but not for phosphate transfer to DevR (DosR) (PubMed:15135056). In another study Mn(2+) and Ca(2+) substitute poorly for autophosphorylation (PubMed:17600145). In another study Mg(2+) or Mn(2+) are required for transfer, but Ca(2+) does not substitute as well (PubMed:28977726).
Binds 1 heme group per monomer (PubMed:15135056, PubMed:17600145, PubMed:18980385). Half-life of Fe(2+) DosT is over 60 hours in air (PubMed:17600145).
Binds 2 heme c groups covalently. Heme 1 is low-potential (-330 mV) with 2 His axial ligands and functions in the peroxidase reaction, while heme 2 is high potential (+320 mV) with His and Met axial ligands and functions to feed electrons from electron-shuttle proteins such as cytochrome c and azurin.
Binds 1 nickel ion per subunit. In the homodimer, two nickel ions are bound between subunits. Is not active with zinc ions.
May bind 1 Zn(2+) cofactor that does not appear in the structures.
Binds 2 iron ions per subunit. The catalytic dinuclear iron-binding site within each subunit is known as the ferroxidase center. In BFR, the ferroxidase center appears to function as a true di-iron catalytic cofactor, rather than as a pore for the transfer of iron into the central cavity, as found for eukaryotic ferritins.
Divalent metal cations. Mn(2+) is better for the L-fucokinase activity, while Mg(2+) is preferred for the GDP-fucose pyrophosphorylase activity.
Binds 1 protoheme IX center (heme b595, originally called cytochrome a1) per heterodimer, in conjunction with CydB.
Binds 1 zinc ion per subunit. Not sensitive to EDTA and not significantly stimulated by cations such as Ca(2+), Co(2+), Mn(2+), Ni(2+) or Zn(2+) (PubMed:16460512).
Divalent metal cations. Mg(2+), Ca(2+) or Mn(2+) ions for farnesene synthase activity.
Binds 1 Zn(2+) per subunit. Zinc is not required for SigR-binding, but is required for anti-sigma factor activity. Zinc-binding renders RsrA relatively resistant to oxidation.
Binds 3 Mg(2+) per subunit.
Binds 1 zinc ion per subunit. Does not contain structural calcium, which is often associated with other metalloproteases.
Divalent metal cations such as Mg(2+) and Mn(2+) ions at 5 mM.
Can also use Mn(2+) ions as cofactors with a lower efficiency.
Binds 2 Calcium ions per subunit.
Binds 2 Zn(2+) ions per subunit. These two catalytic ions are both involved in the stabilization of the tetrahedral intermediate and in the activation of the catalytic water molecule.
Cannot use Mg(2+), Ca(2+), Ni(2+) or Co(2+) instead of Mn(2+) as cofactor.
Zinc, although calcium also allows some activity.
Possesses phosphatase activity in presence of Mn(2+), Co(2+), Ni(2+) or Zn(2+). No phosphatase activity in presence Ca(2+).
Binds 2 Zn(2+) ions per subunit (By similarity). Zn(2+) can be replaced by Cu(2+), Co(2+), Ca(2+) or Mn(2+) to some extent (PubMed:19307254).
Binds 1 zinc ion per subunit; the homodimer seems not to bind zinc. The zinc is probably not catalytic (PubMed:16087889). Another report suggests the zinc is catalytic (PubMed:16374837).
Divalent metal cations, preferably Mg(2+). While only 1 Mg(2+) is detected by crystallography, other evidence indicates there may be more than 1 metal necessary for catalysis. Binding of the second metal my be promoted by substrate binding.
Binds 1 zinc ion per subunit (PubMed:11866529). In a number of structures (e.g. 4Y4O, 5FDV) a 4Fe-4S cluster is seen in place of the zinc cofactor (PubMed:25775268, PubMed:26792896).
Binds 1 heme c group covalently per subunit (PubMed:11478889).
Binds 1 PQQ group per subunit (PubMed:3521592, PubMed:11714714). PQQ is inserted between disulfide Cys-147-Cys-148 and the plane of Trp-276 (PubMed:11714714).
Binds 2 divalent metal cations per subunit (PubMed:19350606). Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions (PubMed:19350606).
Was shown to bind 1 [3Fe-4S] cluster (PubMed:24188825). However, it initially contains a [4Fe-4S] cluster which easily degrades into a [3Fe-4S] form in the presence of oxygen (Probable).
Binds 2 magnesium ions per subunit. Can also use manganese as divalent cation, however calcium and zinc ions are much less effective.
No cofactors were found to be necessary.
Binds 2 Zn(2+) ions per subunit. Contains one structural ion and one catalytic ion that may be less tightly bound at the site.
Binds 2 metal cations (PubMed:22387043). The role of the metal cation is unclear (PubMed:22387043).
Mg(2+) is preferred for polyP utilization and Mn(2+) is preferred for polyP synthesis.
Binds 2 Zn(2+) ion per monomer.
Binds 2 heme b groups non-covalently. Heme 1 (or bL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or bH or b566) is high-potential and absorbs at about 566 nm.
Binds 1 heme c group covalently. Heme 3 is covalently bound to cytochrome c1.
Tetrahydrobiopterin (H4B). Can also use tetrahydrofolate (THF) in place of tetrahydrobiopterin (H4B) but binds THF with much lower affinity than H4B.
Binds 1 Fe(3+) or Zn(2+) ion per subunit.
Probably binds 2-3 heme groups via the 3 magnetochrome (MCR) motifs.
Binds 1 Mg(2+) ion per monomer. The Mg(2+) ion binds to water and substrates.
Shows an absolute requirement for inorganic phosphate for activity. The function of the phosphate may involve stabilizing the protein conformation and/or initiating protein aggregation. Unlike the threhalase ortholog in M.smegmatis, does not require Mg(2+) for activity.
Bind 1 Zn(2+) per monomer.
Mn(2+) supports cleavage of all guide:target combinations, Mg(2+) only supports gRNA-directed cleavage (PubMed:36288702). Cleavage probaby requires 2 divalent metal cations (By similarity).
Binds 1 Fe(2+) ion per subunit. In contrast to some other SORs, does not bind a second iron ion.
No activity with Mn(2+) or Ca(2+).
Synthesis of cA6 requires Mg(2+).
May bind up to 3 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Mg(2+). Mn(2+) can replace Mg(2+) as the divalent metal. The role of the metal is to bind 5-phosphoribose 1-diphosphate and form a Mg-5-phosphoribose 1-diphosphate complex which then serves as substrate for OPRTase.
Binds about 6 Ca(2+) per subunit (Probable). The metallopeptidase and PKD domains bind 1 Ca(2+), while CDB binds 2 (Probable).
Binds 2 Mg(2+) ions per subunit. A third Mg(2+) ion binds between the 2 farnesyl diphosphate (FPP).
Most active with magnesium.
Binds 2 magnesium ions per monomer. The first magnesium ion is required for catalysis. The second functions as an allosteric activator.
Binds up to 3 divalent cations (Ca(2+) or Mg(2+)); their binding site probably overlaps with that of cationic antimicrobial peptides that induce the operon.
Binds 1 NAD(+) pers subunit.
Can also use Mg(2+) and Ca(2+), with lower efficiency.
Can also use Ni(2+), Mn(2+) and Zn(2+), to a lower extent.
Without Pb(2+) acting as a cofactor, this protein's function is compromised.
Divalent metal cation. Mn(2+), Ni(2+), and Pb(2+) enhance the enzyme activity.
Binds 1 or 2 zinc ions per subunit.
A divalent cation Ca(2+), Mg(2+) or Mn(2+).
Binds 1 FMN non-covalently per subunit.
Binds 1 divalent metal cation per subunit. The highest efficient metals are Zn(2+) and Co(2+), followed by Mn(2+), Cd(2+), Fe(2+) and Ni(2+).
Binds 1 [2Fe-2S] cluster per subunit. The redox potential of the [2Fe-2S] cluster is -254 mv.
Binds 1 heme group.
Binds 3 Ca(2+) ions per subunit. Two of the Ca(2+) ions are bound to the C2 domain.
Binds 3 divalent metal cations per subunit. Can use either Mg(2+) or Mn(2+).
Binds 1 zinc ion per subunit. Cobalt, nickel and manganese ions can also function as cofactors.
Binds 1 Mg(2+) ion per subunit (PubMed:11124906). Can also use Ca(2+) ion to a lesser extent (PubMed:11118459).
Requires a divalent metal ion for activity. In vitro, exhibits a preference for Ni(2+) followed by Mn(2+) and very poor activity with Mg(2+). However, it is unclear what the physiologically relevant metal ion is.
Rapid, sequence-specific cleavage at physiological concentrations of Mg(2+) (4-5 mM) or Mn(2+) (15 uM). In presence of >20 uM Mn(2+) has rapid non-specific cleavage activity.
Binds 2 manganese ions per subunit (Probable). May also use Mg(2+) and Zn(2+) (Probable).
Binds 2 Mg(2+) ions per subunit (Potential). Can also use Mn(2+) ions (PubMed:4306285).
Can use either Fe(2+) or Zn(2+). The metal cofactor can switch between Fe(2+) and Zn(2+) in response to metal availability. Metal switching may be important for regulating the LpxC activity upon changes in environmental conditions. Has a significantly higher affinity for Zn(2+), but exhibits higher activity with Fe(2+) (PubMed:20136146, PubMed:20709752). Can also use Co(2+), Ni(2+) and, to a lesser extent, Mn(2+) (PubMed:10026271).
Binds 2 Zn(2+) ions per subunit (PubMed:19408962, PubMed:20133789, PubMed:21844374, PubMed:23713488, PubMed:25299353, PubMed:25645579, PubMed:35691342). Two metal binding sites with different affinities are located in the enzyme active site and can be occupied in vitro by different metals (PubMed:19408962). Site 1 binds metal with low affinity and can be occupied by Zn(2+), Mn(2+), Co(2+) or Mg(2+) (PubMed:19408962). While Zn(2+) has the highest affinity for site 1, catalytic activity is the highest with Mn(2+) or Co(2+) and less with Mg(2+) (PubMed:19408962, PubMed:33303633). Site 2 binds tightly to the metal ion and can be occupied only by Zn(2+) or Co(2+) (PubMed:19408962). A third metal binding site is also present in an inactive conformation of the hexamer; in this conformation only the metal binding sites 1 and 3 are occupied (PubMed:35691342).
Binds 1 zinc ion per subunit. Can also use manganese, copper and magnesium ions.
Monovalent cations. Strong preference for ammonium over potassium.
Binds 3 Fe(2+) ions per subunit (PubMed:33468680). Two Fe(2+) bind the HO-like central domain and one Fe(2+) binds the C-terminal cupin domain (PubMed:33468680).
Can also use, to a lesser extent, Mg(2+) and Zn(2+).
Binds 2 calcium ions per monomer.
Active in the presence of Mn(2+) or Ni(2+) ions. No activity detected with Zn(2+) or Co(2+).
Mg(2+) is the most effective ion.
10 uM Mn(2+) or 10 mM Mg(2+) are equally active in vitro.
Binds 1 Zn(2+) ion1 per subunit.
May bind up to 2 Ca(2+) per subunit, Ca(2+) does not substitute for supercoiling activity, but is required for relaxation, probably by an interaction with this subunit (PubMed:22844097). This subunit has altered protease sensitivity in the presence of Ca(2+), which might reflect regulation (PubMed:22844097).
Binds 2 magnesium ions per subunit (By similarity). Is also active with manganese (in vitro) (PubMed:9874775).
Binds 1 zinc ion per subunit in the active site.
Binds 1 Zn(2+) per subunit, at the subunit interface.
May bind 2 [2Fe-2S] clusters per subunit.
May bind 4 [4Fe-4S] clusters per subunit.
Contains a catalytic Fe binuclear center (H-cluster), which is coordinated by Cys-486 and by non-protein ligands.
Binds Ca(2+).
Binds 2 magnesium ions per subunit (PubMed:25040695). Is also active with manganese (in vitro) (PubMed:12609998, PubMed:15659711, PubMed:24616449).
Requires Ca(2+) or Mg(2+) for catalytic activity and the maximum activity is achieved when both of these ion species are present.
Mn(2+) ions. Can also use Mg(2+) ions with a lower efficiency.
Binds 2 [4Fe-4S] cluster per subunit.
Binds 1 Mn(2+) ion per subunit. To a much lesser extent, can also use Co(2+) and Mg(2+) as cofactor, but not Zn(2+).
Binds 2 iron ions per homodimer.
Binds 2 FMN per homodimer. The occupancy is 1.3-1.9.
Binds 2 divalent cations per subunit, one with high affinity and the other with lower affinity. Zn(2+) and/or Co(2+) ions are used for desuccinylase activity. The form of DapE active as a peptidase contains Zn(2+) in the high-affinity site and Mn(2+) in the low-affinity site.
Binds 2 [4Fe-4S] clusters per dimer. The [4Fe-4S] cluster quickly oxidizes to a [2Fe-2S] form in the presence of oxygen.
Corrinoid.
Divalent metal cations; Co(2+), Mn(2+) or Mg(2+).
Binds 1 divalent metal cation per subunit. Mn(2+) is the most efficient metal cofactor, but can also use other divalent metal cations such as Ni(2+), Mg(2+), and, to a lesser extent, Co(2+) and Zn(2+), but not Ca(2+), Cu(2+), and Fe(2+).
Corresponds to iron 2 in the structure.
Corresponds to iron 1 in the structure.
For PI-TfuII intein endonuclease.
For PI-TfuI intein endonuclease.
Binds 1 heme b (iron(II)-protoporphyrin IX) covalently through ester linkages to hydroxylated methyl groups formed auto-catalytically with hydrogen peroxide at the heme C-1 and C-5 positions. The ester linkage to Asp-232 was observed in 30% of the chains.
Without cob(I)alamin acting as a cofactor, this protein's function is compromised.
Divalent metal ions. Optimum activity is obtained with Mn(2+).
Binds 2 zinc ions (PubMed:31978345). One zinc is catalytic and mediates binding to the substrate, while the second is probably structural (PubMed:31978345).
Binds 8 heme c groups per subunit. One of them is an atypical heme c (unusual heme c binding motif CXXXXCH). Catalysis takes place at heme-4, termed P460. The other c-type hemes mediate electron transfer to the external electron acceptor, which is a cytochrome c-type protein.
Mn(2+), Zn(2+), Cd(2+) and Co(2+) support activity to lesser extents.
Binds 1 [2Fe-2S] cluster per subunit. The [2Fe-2S] cluster 1 is referred to as N1b.
Binds 3 [4Fe-4S] clusters per subunit. The [4Fe-4S] clusters 2, 3, and 4 are referred to as N5, N4, and N7, respectively. The [4Fe-4S] cluster 4 is too far away from the main redox chain to participate in electron transfer but probably confers structural stability.
In vitro Co(2+) and Mn(2+) strongly activate condensation, Mg(2+), Cd(2+), Ni(2+) and Zn(2+) weakly activate.
Binds 2 divalent metal cations per subunit (PubMed:17727341). Site 2 has a preference for magnesium and/or manganese ions (By similarity).
Binds 3 Mn(2+); 2 Mn(2+) for polymerase/primase activity and 1 for ligase activity.
May bind 2 Mg(2+) ions.
Zn(2+). Although displays higher activity with Co(2+) than with Zn(2+) in vitro, bioavailability may well limit this enzyme to be zinc-dependent.
Binds 1 cobalt ion per subunit. Can also utilize Mn(2+) (in vitro). Is not active with zinc ions.
Divalent metal cation. Has the highest activity with Mn(2+) as cofactor. Can also use Cd(2+) at low concentrations (0.01-0.1 mM) or Co(2+), although with less efficiency. Mg(2+) and Ni(2+) are very poor metal cofactors.
Can use Ca(2+), Mn(2+), and, to a lesser extent, Mg(2+).
Manganese; magnesium does not support nuclease activity.
Binds 2 manganese ions per subunit. Other divalent cations, such as Mg(2+) or Ca(2+), cannot serve as cofactors.
Binds 3 Mg(2+) ions per subunit. To a lesser extent, can also use Mn(2+) instead of Mg(2+). Cannot use Fe(2+), Co(2+), Zn(2+), Ni(2+), or Cu(2+).
Does not require metal ions for catalytic activity.
Binds one cofactor per subunit.
None. Contrary to most other dioxygenases, this enzyme does not require a cofactor for catalysis.
Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells. Required for glucosyltransferase activity.
Binds 1 zinc ion per subunit. At high pH manganese can replace zinc.
Binds 2 manganese ions per subunit (PubMed:26095028, PubMed:27717128). Substrate binding triggers a switch in the coordination state of the Mn(2+) active site between six- and five-coordinate species; this switch is critical to prime the active site for catalysis, by facilitating the formation of a high-energy imidazolate intermediate (PubMed:26095028).
Binds 2 metal cations per subunit. Site 1 may preferentially bind Fe(3+) ions, while site 2 may have a preference for Fe(2+) ions.
Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-134-Cys-135 and the plane of Trp-277.
Divalent metal cations. Exopolyphosphatase activity is predominant in the presence of Co(2+), while endopolyphosphatase activity is predominant in the presence of Mg(2+) (PubMed:25742176, PubMed:8900207). Co(2+) is more effective than Mn(2+) for dATP phosphohydrolase activity (Ref.16). The yeast vacuole plays an important role in Zn(2+) storing and sequestering. Therefore, the changes in Zn(2+) concentration may regulate the enzyme's activity (Probable).
Can use Co(2+) or Mn(2+) as cofactor, but Mg(2+) and Ni(2+) cannot support enzymatic activity.
Was originally shown to use Ni(2+) as a cofactor (PubMed:24710389), but in fact, the cofactor is a (SCS)Ni pincer complex, a nicotinic acid mononucleotide derivative that is covalently attached to Lys-184 and forms a tridentate pincer complex that coordinates nickel through one metal-carbon and two metal-sulfur bonds (PubMed:26138974, PubMed:27114550).
Binds 1 Ni(2+) ion per monomer; it is not certain this is the physiological metal.
Requires a divalent metal cation for activity. Likely has a bi-nuclear metal center. Has the highest enzyme activity with Mn(2+), and when incubated with Ni(2+), its activity is about 60% lower than that observed with Mn(2+).
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. A second auxiliary cluster is also in contact with the substrate and is proposed to facilitate the loss of the second electron in the oxidation.
Binds 1 Mg(2+) per subunit, in some structures a second Mg(2+) is also seen.
Binds 1 Zn(2+) ion per subunit (PubMed:27571750, PubMed:31308519). Zn(2+) is required for autocatalytic cleavage (PubMed:27571750).
Has higher activity with Mn(2+), but most likely uses Mg(2+) in host cells (PubMed:16054646, PubMed:28433497). Mn(2+) or Mg(2+) are required for glucosyltransferase activity (PubMed:27089365).
Binds 1 FAD per subunit; it is seen bound in two conformations.
Replacement of Mg(2+) by Mn(2+) restores only 10% of the activity.
Not stimulated by Ca(2+), Mn(2+) and Ni(2+).
Binds 1 copper ion per subunit. Can also use zinc ion as cofactor (By similarity).
Binds 1 iron-sulfur cluster per subunit. As the iron-sulfur cluster is unstable, it is not clear from the contradictory experimental evidence whether it is 2Fe-2S, 4Fe-4S or something intermediate. Nor is it clear which other residues besides Cys-53 and Cys-56 are involved in metal binding (PubMed:22937074).
Mg(2+). Mn(2+) can substitute for Mg(2+) for PAP phosphatase and IMPase activities, but is less efficient (50%-60% of the activity observed with Mg(2+)).
Binds 1 divalent metal cation per subunit. Maximum activity is obtained with Mg(2+). Activity with Mn(2+) or Ni(2+) makes up 60-75% of the maximum rate.
Binds 2 Zn(2+) ions per subunit. One of the Zn(2+) is essential for catalytic activity while the other has a structural function.
Binds 2 Fe(2+) ions per APD complex. The iron ions are bound to the beta subunit.
Binds 1 Mg(2+) ion per subunit (PubMed:23517223). Zn(2+) can substitute, but yields a catalytically inactive enzyme (PubMed:14725765, PubMed:16880541, PubMed:16595672).
Magnesium. Co(2+) and Fe(2+) can replace Mg(2+) but lead to a partial activity (30%), and Mn(2+) leads to a partial activity of 13%.
Binds 1 divalent metal cation ion per homodimer with both subunits providing Cys ligands; Fe(2+) gives most activity and is possibly the physiological cofactor.
Binds 1 Mg(2+) ion per subunit. Can bind other divalent cations such as Mn(2+), Fe(2+) and Co(2+).
Binds 1 [4Fe-4S] cluster (PubMed:16420352). The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (PubMed:16420352). The cluster is required for structural integrity of the elongator complex, while it is not required for catalytic activity (PubMed:18986986).
Flavinylated by SdhE, flavinylation occurs at a low level in the absence of SdhE.
Binds 0.5 mol of zinc/mol protein, probably 1 zinc per dimer.
Binds 1 3'-hydroxyechinenone molecule per subunit.
Divalent metal cation. Has the highest activity with Co(2+) as cofactor, followed by Ni(2+) and Mn(2+). Mg(2+) and Ca(2+) are very poor metal cofactors.
ssRNA target cleavage requires Mg(2+), weak target cleavage is seen with Mn(2+) and Ca(2+).
Binds 1 Zn(2+) or 1 Ni(2+) ion per dimer or tetramer.
Binds 3 Mn(2+) ions per subunit (By similarity). The third manganese ion is unlikely to be involved in catalysis but contributes instead to stabilize a flap segment, which is partially disordered in the absence of bound metal (By similarity).
Recombinant protein contains about 1.7 mole of iron per mole of protein.
Divalent metal cations. Ca(2+), Mg(2+) or Mn(2+).
Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable).
Binds 1 divalent metal cation per subunit. Fully active with Mg(2+). Active at 80% with Mn(2+) or Co(2+) ions. Active at less than 10% with Ca(2+) or Zn(2+) ions.
Binds 1 heme per molecule.
PncA contains Mn(2+) and Fe(2+) in a molecular ratio of 1:1. PncA has only one metal center. It is believed that PncA binds iron in the natural state, although both metals can support enzymatic activity.
Binds 4 [4Fe-4S] clusters per heterotetramer. Contains two stable clusters in the N-termini of nbp35 and two labile, bridging clusters between subunits of the nbp35-SJAG_02895 heterotetramer.
Mn(2+) is a poor substitute for Mg(2+) (PubMed:32085896). Binds 2 Mg(2+) ion per subunit.
Binds 2 Mg(2+) ion per subunit (By similarity). Mn(2+) is a poor substitute for Mg(2+) (PubMed:32085896).
Reaction requires Mg(2+).
Divalent metal cations. Zn(2+) is the most effective cation for catalysis.
No activity is detected with Mn(2+).
Binds 3 [4Fe-4S] clusters (PubMed:23477283, PubMed:23650368). The first cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (PubMed:23650368). The two auxiliary clusters may create a conduit for electrons to travel from the buried substrate to the protein surface (PubMed:23650368).
Addition of FAD increases DBTO2 production in cell lysates.
Reduced flavin is provided by flavin reductase DszD; in vitro NADPH and FAD are not substrates.
In vitro, optimal manganese concentration is in the range of 5-10 mM.
Appears to bind only one FMN molecule per homodimer.
Mn(2+) is probably the active metal ion. Other metals such as Zn(2+), Ca(2+) and Fe(2+) can also act as cofactors.
Mg(2+) is required for maximal activity.
Mg(2+) is the preferred cation, followed by Mn(2+) and Co(2+).
Might bind 1 zinc ion.
Shows highest activity with Mn(2+) and Fe(2+).
Binds 1 Mn(2+) or Fe(2+) ion per subunit.
FAD enhances the epoxidase activity while other flavins such as FMN or riboflavin are without effects.
Binds 2 [4Fe-4S] clusters (PubMed:16878993). One cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (Probable).
Might bind an [Fe-S] cluster in vivo.
1 pyridoxal phosphate per subunit.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster of the oxygen-evolving complex (OEC). There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls, carotenoids and specific lipids.
Divalent metal ion. Manganese, cobalt and nickel ions enhance activity whereas magnesium, calcium, strontium and zinc ions do not.
Requires divalent metal cations for activity. Prefers Mg(2+), Mn(2+) or Co(2+). Is inactive with Zn(2+), Ni(2+) and Fe(2+).
Cleavage of dsDNA requires Mg(2+) (PubMed:26422227, PubMed:28562584). Another report shows DNA cleavage occurs equally well in the presence of Ca(2+) or Mg(2+) (PubMed:27096362). Processing of pre-crRNA requires a divalent cation, preferably Mg(2+) which is bound by the crRNA (PubMed:26593719, PubMed:28431230).
Binds up to 2 Zn(2+) ions per subunit.
Cannot be substituted by Mn(2+) or Zn(2+).
Binds 6,7-dimethyl-8-ribityllumazine (DMRL) as antenna chromophore.
Binds 2 Zn(2+) ions per subunit. The average amount of Zn(2+) bound at physiological metal concentrations will be lower than stoichiometric.
Can also use Mn(2+) or Co(2+) with reduced efficiency. K(+) simulates the degradative reaction.
Binds 1 Mg(2+) per subunit (PubMed:23647843). Is also active with Mn(2+) (PubMed:23647843, PubMed:32814054). Mn(2+)-activated enyzme forms an inverted pppGp(2'-5')A intermediate, suggesting a non-canonical but accelerated 2',3'-cGAMP cyclization without substrate flip-over (PubMed:32814054). Mn(2+) ions are coordinated by triphosphate moiety of the inverted substrate, independent of the catalytic triad residues (PubMed:32814054).
Binds 10 calcium ions (PubMed:16682770, PubMed:17449691, PubMed:19193638). The calcium may have a structural role. Requires calcium or manganese for activity (PubMed:16682770, PubMed:17449691).
No activity in the presence of Ca(2+) or Zn(2+).
Contains a mononuclear Cu(II) center.
NAD kinase and pNPPase show maximum activities at 50 and 20 mM magnesium, respectively.
Requires a divalent cation; Co(2+) > Mn(2+) >Zn(2+) > Mg(2+).
Binds 2 divalent metal cations per subunit (PubMed:938681). Can use cobalt, zinc, and possibly also magnesium ions.
Required to stimulate the ATPase activity of DnaK.
Binds 1 zinc ion per subunit. Can also utilize cobalt ions, but contains bound zinc when purified after heterologous expression in E.coli.
Binds 1 zinc ion per subunit. This zinc stabilizes the protein.
The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. There is also a Cl(-1) ion associated with D1 and D2, which is required for oxygen evolution (PubMed:19219048, PubMed:21367867). PSII binds additional chlorophylls, carotenoids and specific lipids.
Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+) ions seen in the 3D-structure.
Binds 2 Zn(2+) ions per subunit. Three distinct zinc binding-sites were identified in the crystal structure, but the exact biological function of the third site remains to be determined. It could be an artifact of crystallization.
Upon overproduction is isolated with 1 Fe(2+) ion per monomer, a Ni(2+)-bound form is as active while a Zn(2+)-bound form is inactive (PubMed:9610360).
Mn(2+) is probably the active metal ion. Other metals such as Zn, Ca and Fe can also act as cofactors.
Endonucleolytic cleavage of target ssRNA by the Csm complex requires a divalent metal ion; Mg(2+) has the best activity in vitro, but Mn(2+), Ca(2+), Zn(2+), Ni(2+), and Co(2+) also support cleavage.
Binds 1 [4Fe-4S] cluster per subunit. The cluster is chelated by three Cys residues, the fourth Fe has a free coordination site that may bind a sulfur atom transferred from the persulfide of IscS. The [4Fe-4S] cluster is highly sensitive to oxygen and prone to decompose into the [2Fe-2S] form and further degraded forms.
Binds 2 manganese ions per subunit (By similarity). Can use zinc ions (PubMed:21209330) (PubMed:21209330).
Binds 2 manganese ions per subunit (By similarity). Mn(2+) is inhibitory below pH 8 and activating above pH 8 (PubMed:24892992).
Carboxypeptidase activity is stimulated by zinc (PubMed:7972112). Penicillin-binding is stimulated by zinc (PubMed:12196546).
Can also use Fe(2+), Cu(2+), Mn(2+), Zn(2+) and Ni(2+).
Manganese or any other divalent metal ion, except copper or zinc.
Binds 2 magnesium ions per monomer. Can also use manganese.
Does not require zinc.
Binds 1 divalent cation per subunit. Activity is maximal in the presence of Mg(2+), while Mn(2+) decreases the activity by 20%.
Divalent metal cations. Mg(2+).
Binds 1 Co(2+) ion per heterodimer.
Can use Mg(2+) and Co(2+) with equal efficiency in vitro, and to a lesser extent, Mn(2+), but not Ni(2+).
A monovalent cation. K(+) is most effective, followed by NH4(+) and Rb(+). Na(+), Li(+) and Cs(+) are ineffective.
Phosphatase activity is strongly promoted by several divalent cation ions but it is suggested that Mn(2+) and possibly Ni(2+) represent biologically relevant metal ion cofactors for damage-control phosphatase activity (PubMed:27322068).
The [2Fe-2S] cluster does not seem to be directly involved in catalysis (PubMed:27322068).
Binds 1 Fe-coproporphyrin III group per dimer.
Isoform 1 binds 3 Zn(2+) ions.
Isoform 2 binds 2 Zn(2+) ions.
Binds 1 Mg(2+) ion per subunit (PubMed:2118958, PubMed:8648644, PubMed:9092835). Ca(2+) can substitute but is not catalytically competent (PubMed:14596800, PubMed:9034362).
Divalent metal cations. Co(2+), Mg(2+) or Mn(2+) can be used.
Manganese and/or Cobalt or Copper. The ion enhances activity.
Binds 2 FMN per subunit. Each FMN has a myristate attached. This flavin-fatty acid linkage is probably the result of an enzyme-catalyzed reaction, most likely the bioluminescence reaction itself.
Binds 8 [4Fe-4S] clusters.
Cofactor affinity is increased in an IscS-IscU complex.
Can also use Mn(2+), Co(2+) and Ni(2+).
In vitro only Mn(2+) supports endonuclease activity; Mg(2+) inhibits binding to HJ DNA (PubMed:35744678). Another study shows Mn(2+) is the preferred cofactor but Mg(2+) does support cleavage (PubMed:36000732). Binds 2 Mn(2+) ion per subunit (By similarity).
Divalent metal cations. Probably Mg(2+).
Divalent metal cations. Zn(2+) >> Co(2+) > Mg(2+) > Mn(2+) > Ca(2+).
Crystallized in the absence of Mg(2+), the catalytic metal is not bound by the protein but probably by non-esterified oxygen atoms from ATP and/or ordered H(2)O (PubMed:11812124).
Contains a nonheme dinuclear iron cluster (PubMed:17679698, PubMed:23906247, PubMed:25453905). Contains three different forms of the dinuclear site: an hydroxo-bridged FeIII-OH-FeIII center, an oxo-bridged FeIII-O-FeIII center and an hydroxo-bridged FeII-OH-FeIII mixed-valent center (PubMed:17679698).
Binds 2 [2Fe-2S] cluster per subunit.
Binds 1 Ca(2+) ion per subunit. Can also use Co(2+) or Mn(2+).
Binds at least 1 Zn(2+) ion per subunit.
Binds 4 Cu cations per monomer (PubMed:11527384, PubMed:11867755, PubMed:12794077, PubMed:17217912, PubMed:17804014, PubMed:21903583, PubMed:24598746, PubMed:27380373, PubMed:30250139). Contains a mononuclear type 1 (T1) or 'blue' copper site, and a trinuclear copper center consisting of one type 2 (T2) or 'normal' copper site, and two type 3 (T3) or 'binuclear' copper sites (PubMed:11867755).
Binds 1 iron ion. Iron is essential for catalysis.
Binds metal ions, iron, manganese or zinc. The ion could be involved in the binding of substrate and/or the release of the product.
Binds 5 copper ions per monomer.
Mn(2+) ion. Can also use other divalent metal cations.
Mn(2+) supports cleavage of ss- and dsDNA, while Mg(2+) only supports digestion of dsDNA in vitro.
Although Co(2+) and Mn(2+) support eight- and fourfold higher catalytic efficiency than Mg(2+), respectively, Mg(2+) is likely the physiologically relevant catalytic divalent metal ion.
Binds 1 Mn(2+) ion per subunit. Can also use Co(2+), Ni(2+) and Mg(2+).
Binds 3 zinc ions per subunit. The zinc ions have a structural role (PubMed:24315485).
Both divalent cations appear to be equally efficient in an vitro reconstitution assay.
Binds 3 Mg(2+) ions per subunit. Can also accept Mn(2+) ions.
Divalent metal cations; Mg(2+) or Mn(2+) (PubMed:31127291). Acts as a 3'-5' exoribonuclease in presence of Mg(2+), while it has no 3'-5' exodeoxyribonuclease activity (PubMed:29335528, PubMed:31127291). Has both as a 3'-5' exoribonuclease and exodeoxyribonuclease activities in presence of Mn(2+) (PubMed:31127291).
Binds 1.0 Fe(2+) (PubMed:20087498) to 1.5 to 3.2 Fe(2+) per monomer (PubMed:21744456).
Can also use Co(2+).
Binds 1 cobalt ion per subunit (By similarity). Can also use Mn(2+) (PubMed:31950558).
Without Ba(2+) acting as a cofactor, this protein's function is compromised.
Divalent metal cation. Can use Mg(2+), or to a lesser extent, Mn(2+), Ca(2+) or Ba(2+).
Binds 2 heme groups per molecule.
Zn(2+) and Co(2+) are equally efficient in vitro, Fe(2+) is less efficient.
Binds 1 zinc ion per subunit (PubMed:29540745).
Binds 2 iron ions per dimer.
Can also use Mn(2+) and Co(2+) with lower efficiency.
Binds 6 heme c groups covalently per subunit.
Can use Mg(2+) and Ca(2+) with equal efficiency in vitro, and to a lesser extent, Co(2+).
Magnesium ions are not essential for catalysis.
Binds 1 zinc ion per dimer.
Requires a divalent metal cation for activity. Likely has a bi-nuclear metal center. Has the highest enzyme activity with Mn(2+).
Binds 2 divalent metal cations per subunit, which may be Mg(2+) or Mn(2+), and which are essential for catalysis.
Binds 5 calcium ions per subunit.
Binds 2 magnesium ions per subunit. Magnesium is probably occupied in place of calcium as excess magnesium is used in the experiments.
Does not require a divalent metal for activity (PubMed:23214453). The purified enzyme contains Zn(2+), but the addition of chelators does not diminish the catalytic activity of the enzyme, indicating that it does not require a divalent cation for substrate turnover (PubMed:23214453).
Binds 6 low-spin heme groups per subunit.
Other metal ions such as Mn(2+) and Zn(2+) can support activity, but at a much lower rate (PubMed:16239227). Three metal ions appear to be required for the activation of the enzyme and the substrate during the catalytic cycle (PubMed:26296329).
ATPase activity has a small preference for Mn(2+) over Mg(2+) or Ca(2+). Co(2+) and Zn(2+) are inactive.
Binds 1 divalent metal cation per subunit. Has the highest activity with Co(2+) and Mn(2+), but can also use Zn(2+), Fe(2+) and Mg(2+).
Binds 2 Zn(2+) ions or 1 Zn(2+) and 1 Mn(2+) per subunit. The Zn(2+) in the metal 1 binding site can be replaced with Mn(2+); however, the second zinc in metal binding site 2 is much more tightly bound and cannot be replaced. The enzyme with one zinc and one manganese ion is more active than that with two zinc ions.
ssDNase activity requires Mg(2+), ssRNase activity does not require cations. A second loosely associated metal ion is visible in the crystal structure.