Protein: DMAW_CLAPU
Sequence: MSTAKDPGNGVYEILSLIFDFPSNEQRLWWHSTAPMFAAMLDNAGYNIHDQYRHLGIFKKHIIPFLGVYPTKDKERWLSILTRCGLPLELSLNCTDSVVRYTYEPINEVTGTEKDTFNTLAIMTSVQKLAQIQAGIDLEWFSYFKDELTLDESESATLQSNELVKEQIKTQNKLALDLKESQFALKVYFYPHLKSIATGKSTHDLIFDSVLKLSQKHDSIQPAFQVLCDYVSRRNHSAEVDQHGALHARLLSCDLIDPAKSRVKIYLLEKTVSLSVMEDLWTLGGQRVDASTMDGLDMLRELWSLLKVPTGHLEYPKGYLELGEIPNEQLPSMANYTLHHNDPMPEPQVYFTVFGMNDAEISNALTIFFQRHGFDDMAKNYRVFLQDSYPYHDFESLNYLHAYISFSYRRNKPYLSVYLHTFETGRWPVFADSPISFDAYRRCELSTK
What is the function of this protein?
Tryptophan dimethylallyltransferase; part of the gene cluster that mediates the biosynthesis of fungal ergot alkaloid (PubMed:10071219, PubMed:14732265, PubMed:14700635, PubMed:15904941, PubMed:17308187, PubMed:17720822).  DmaW catalyzes the first step of ergot alkaloid biosynthesis by condensing dimethylallyl diphosphate (DMAP) and tryptophan to form 4-dimethylallyl-L-tryptophan (PubMed:14732265).  The second step is catalyzed by the methyltransferase easF that methylates 4-dimethylallyl-L-tryptophan in the presence of S-adenosyl-L-methionine, resulting in the formation of 4-dimethylallyl-L-abrine (By similarity).  The catalase easC and the FAD-dependent oxidoreductase easE then transform 4-dimethylallyl-L-abrine to chanoclavine-I which is further oxidized by easD in the presence of NAD(+), resulting in the formation of chanoclavine-I aldehyde (PubMed:20118373, PubMed:21409592).  Agroclavine dehydrogenase easG then mediates the conversion of chanoclavine-I aldehyde to agroclavine via a non-enzymatic adduct reaction: the substrate is an iminium intermediate that is formed spontaneously from chanoclavine-I aldehyde in the presence of glutathione (PubMed:20735127, PubMed:21494745).  The presence of easA is not required to complete this reaction (PubMed:21494745).  Further conversion of agroclavine to paspalic acid is a two-step process involving oxidation of agroclavine to elymoclavine and of elymoclavine to paspalic acid, the second step being performed by the elymoclavine oxidase cloA (PubMed:16538694, PubMed:17720822).  Paspalic acid is then further converted to D-lysergic acid (PubMed:15904941).  Ergopeptines are assembled from D-lysergic acid and three different amino acids by the D-lysergyl-peptide-synthetases composed each of a monomudular and a trimodular nonribosomal peptide synthetase subunit (PubMed:14700635, PubMed:15904941).  LpsB and lpsC encode the monomodular subunits responsible for D-lysergic acid activation and incorporation into the ergopeptine backbone (PubMed:14700635).  LpsA1 and A2 subunits encode the trimodular nonribosomal peptide synthetase assembling the tripeptide portion of ergopeptines (PubMed:14700635).  LpsA1 is responsible for formation of the major ergopeptine, ergotamine, and lpsA2 for alpha-ergocryptine, the minor ergopeptine of the total alkaloid mixture elaborated by C. purpurea (PubMed:17560817, PubMed:19139103).  D-lysergyl-tripeptides are assembled by the nonribosomal peptide synthetases and released as N-(D-lysergyl-aminoacyl)-lactams (PubMed:24361048).  Cyclolization of the D-lysergyl-tripeptides is performed by the Fe(2+)/2-ketoglutarate-dependent dioxygenase easH which introduces a hydroxyl group into N-(D-lysergyl-aminoacyl)-lactam at alpha-C of the aminoacyl residue followed by spontaneous condensation with the terminal lactam carbonyl group (PubMed:24361048).
What are the official names of this protein?
Tryptophan dimethylallyltransferase 1, 4-dimethylallyltryptophan synthase 1, DMATS 1, All-trans-hexaprenyl-diphosphate synthase 1, L-tryptophan dimethylallyl transferase 1.
What is the protein family that this protein belongs to?
Belongs to the tryptophan dimethylallyltransferase family.