Protein: PHQC_PENFE
Sequence: MSKTTEVKVVEVQLEDPLPGIVDASRFISGSPTEQRAFAVELVDSVRRCGFVKVINHGLSDELIDELFAWCQSSHVVQNERFFAIDPEQKLAVVNPPGPSPQRGWSCVGAEKASRLFSRGQTSLDLTDARRNQEHFDAGSPSDTKWPSRWPDEAVIPGFKAFLEDFYVRSHQAALLILEALEMGLNLPAGVLKSRCGGCASELRLNNYPEIDIEELRRGKISRIHPHADLGVITCLFQDGLGGLELEHRSHAGSFLPVPPGARSEMVVNISETFQLWTNNVITAGIHQVTVPPEMKTRTEGRISARRSCAFFLKANGDASVAPLPQFVTQERPAAYSEMTALDYHQKRLATAY
What is the function of this protein?
2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of paraherquamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2. 2. 2]diazaoctane core (PubMed:23213353).  The first steps in the biosynthesis of paraherquamide is the production of the beta-methyl-proline precursor from L-isoleucine (Probable).  They require oxidation of a terminally hydroxylated L-isoleucine to the corresponding aldehyde by enzymes which have still to be identified (Probable).  Spontaneous cyclization and dehydration would yield the 4-methyl pyrolline-5-carboxylic acid, which is then reduced by the pyrroline-5-carboxylate reductase phqD leading to the beta-methyl-proline precursor (Probable).  The next step of paraherquamide biosynthesis involves coupling of beta-methyl-proline and L-tryptophan by the bimodular NRPS phqB, to produce a monooxopiperazine intermediate (Probable).  The reductase (R) domain of phqB utilizes NADPH for hydride transfer to reduce the thioester bond of the T domain-tethered linear dipeptide to a hemithioaminal intermediate, which spontaneously cleaves the C-S bond to release the aldehyde product (PubMed:31548667).  This compound undergoes spontaneous cyclization and dehydration to give a dienamine which is reverse prenylated at C-2 by the reverse prenyltransferase phqJ (Probable).  The other prenyltransferase present in the cluster, phqI may be a redundant gene in the pathway (Probable).  During biosynthetic assembly, the key step to produce the polycyclic core is catalyzed by the bifunctional reductase and intramolecular [4+2] Diels-Alderase, phqE, resulting in formation of the [2. 2. 2] diazaoctane intermediate preparaherquamide (PubMed:31548667).  Following formation of preparaherquamide, an indole 2,3-epoxidation-initiated pinacol-like rearrangement is catalyzed by the phqK FAD-dependent monooxygenase (Probable).  The prenyltransferase phqA, the cytochrome P450 monooxygenase phqL, and the FAD-linked oxidoreductase phqH (or the cytochrome P450 monooxygenase phqM), are proposed to be involved in the formation of the pyran ring (Probable).  The FAD-dependent monooxygenase phqK is likely responsible for generation of the spiro-oxindole, and the N-methylation is likely mediated by the phqN methyltransferase leading to the isolable natural product paraherquamide F (Probable).  However, the order of these biosynthetic steps has still to be determined (Probable).  In late-stage paraherquamide biosynthesis, the third P450 monooxygenase, phqO, is probably responsible for the C-14 hydroxylation, transforming paraherquamide F to paraherquamide G, and paraherquamide E to the final product paraherquamide A (Probable).  The expansion from the 6-membered ring pyran (in paraherquamides F and G) to the 7-membered dioxepin ring (in paraherquamides A and E) represents a poorly understood but intriguing process that probably involves the 2-oxoglutarate-dependent dioxygenase phqC (Probable).  Finally, the remaining members of the paraherquamide cluster, including phqI as well as phqM (or phqH), do not have a clearly prescribed role and appear to be redundant (Probable).
What are the official names of this protein?
2-oxoglutarate-dependent dioxygenase phqC, Paraherquamide biosynthesis cluster protein C.
What is the protein family that this protein belongs to?
Belongs to the iron/ascorbate-dependent oxidoreductase family.