ID FTMH_ASPFM Reviewed; 427 AA. AC B9WZX7; D3TIT5; DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot. DT 14-APR-2009, sequence version 1. DT 12-AUG-2020, entry version 42. DE RecName: Full=12-alpha,13-alpha-dihydroxyfumitremorgin C prenyltransferase; DE EC=2.5.1.110; DE AltName: Full=Fumitremorgin biosynthesis protein H; GN Name=ftmPT2; Synonyms=ftmH; OS Neosartorya fumigata (Aspergillus fumigatus). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=746128; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=BM939; RX PubMed=19226505; DOI=10.1002/cbic.200800787; RA Kato N., Suzuki H., Takagi H., Asami Y., Kakeya H., Uramoto M., Usui T., RA Takahashi S., Sugimoto Y., Osada H.; RT "Identification of cytochrome P450s required for fumitremorgin biosynthesis RT in Aspergillus fumigatus."; RL ChemBioChem 10:920-928(2009). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RC STRAIN=NIH 5233 / ATCC 13073; RX PubMed=18683158; DOI=10.1002/cbic.200800240; RA Grundmann A., Kuznetsova T., Afiyatullov S.S., Li S.M.; RT "FtmPT2, an N-prenyltransferase from Aspergillus fumigatus, catalyses the RT last step in the biosynthesis of fumitremorgin B."; RL ChemBioChem 9:2059-2063(2008). CC -!- FUNCTION: Catalyzes the prenylation of 12-alpha,13-alpha- CC dihydroxyfumitremorgin C to fumitremorgin B in the biosynthesis of CC indole alkaloids such as fumitremorgins and verruculogen. Also shows CC activity with fumitremorgin C. {ECO:0000269|PubMed:18683158}. CC -!- CATALYTIC ACTIVITY: CC Reaction=12alpha,13alpha-dihydroxyfumitremorgin C + dimethylallyl CC diphosphate = diphosphate + fumitremorgin B; Xref=Rhea:RHEA:35971, CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:64531, CC ChEBI:CHEBI:72764; EC=2.5.1.110; CC Evidence={ECO:0000269|PubMed:18683158}; CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:18683158}. CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB436628; BAH24002.1; -; Genomic_DNA. DR EMBL; EU622826; ACF22981.1; -; mRNA. DR SMR; B9WZX7; -. DR MEROPS; M77.004; -. DR BioCyc; MetaCyc:MONOMER-18768; -. DR BRENDA; 2.5.1.110; 508. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW. DR CDD; cd13929; PT-DMATS_CymD; 1. DR InterPro; IPR033964; Aro_prenylTrfase. DR InterPro; IPR017795; Aro_prenylTrfase_DMATS. DR InterPro; IPR012148; DMATS-type_fun. DR PANTHER; PTHR40627; PTHR40627; 1. DR Pfam; PF11991; Trp_DMAT; 1. DR PIRSF; PIRSF000509; Trp_DMAT; 1. DR SFLD; SFLDS00036; Aromatic_Prenyltransferase; 1. DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1. PE 1: Evidence at protein level; KW Alkaloid metabolism; Prenyltransferase; Transferase. FT CHAIN 1..427 FT /note="12-alpha,13-alpha-dihydroxyfumitremorgin C FT prenyltransferase" FT /id="PRO_0000424114" FT BINDING 94 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 105 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 192 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 194 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 268 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 353 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 355 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 419 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT BINDING 423 FT /note="Dimethylallyl diphosphate" FT /evidence="ECO:0000250" FT CONFLICT 165 FT /note="R -> K (in Ref. 2; ACF22981)" FT /evidence="ECO:0000305" FT CONFLICT 171 FT /note="P -> A (in Ref. 2; ACF22981)" FT /evidence="ECO:0000305" SQ SEQUENCE 427 AA; 48584 MW; 26F23D63CE60F100 CRC64; MTIPTEISCP EEDAFQLLDK FSWFPSDDQR RWWEYTGPYL LKLLRDAKYP QKDQVPCLYL LQQLLVPYLG TFPVVGQAPL PWWSNVTTYG VPFELSWNLL HNIVRIGFEP LSHLAESGVD AFNKTAPEEC VSRLACLDNT IDLARFRHFQ HHLLVTPEEE TWLLREKAPL PKSGRGQQTL AVEFQNGGIS AKAYFFPGMK SLATGLSPGK LILDSIERLA LPGLKEPVHH LRSTLGLQDD GHPTDTAIAP FLLGVDLCTP ERSRLKFYVT DQVVSWDRVA DMWTLRGKRL EDPQCADGLA LLRKLWDLLA IPEGYRSNIR PDFAFGTPPP EDYRPVMMAN WTLSPKKKFP DPQIYLLTVG MNDAVVMDAL VAFYEVLGWT DLASTYKDKV ASYFPGPDFT KTNYIHSGVS FSYRHSKPYL SVYYSPF //