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 01-APR-2015, entry version 26. 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. 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., RA Usui T., Takahashi S., Sugimoto Y., Osada H.; RT "Identification of cytochrome P450s required for fumitremorgin RT biosynthesis 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 RT the 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 CC shows activity with fumitremorgin C. CC {ECO:0000269|PubMed:18683158}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 12-alpha,13-alpha- CC dihydroxyfumitremorgin C = diphosphate + fumitremorgin B. CC {ECO:0000269|PubMed:18683158}. CC -!- PATHWAY: Alkaloid biosynthesis. {ECO:0000269|PubMed:18683158}. CC -!- SIMILARITY: Belongs to the tryptophan dimethylallyltransferase CC family. {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 ProteinModelPortal; B9WZX7; -. DR HOGENOM; HOG000200278; -. DR BRENDA; 2.5.1.110; 508. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0050364; F:tryptophan dimethylallyltransferase activity; IEA:InterPro. DR GO; GO:0009820; P:alkaloid metabolic process; IEA:UniProtKB-KW. DR InterPro; IPR017795; Aromatic_prenylTrfase_DMATS. DR InterPro; IPR012148; Trp_dimethylallyltransferase. DR Pfam; PF11991; Trp_DMAT; 1. DR PIRSF; PIRSF000509; Trp_DMAT; 1. DR TIGRFAMs; TIGR03429; arom_pren_DMATS; 1. PE 1: Evidence at protein level; KW Alkaloid metabolism; Prenyltransferase; Transferase. FT CHAIN 1 427 12-alpha,13-alpha-dihydroxyfumitremorgin FT C prenyltransferase. FT /FTId=PRO_0000424114. FT BINDING 94 94 Substrate. {ECO:0000250}. FT BINDING 105 105 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 192 192 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 194 194 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 268 268 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 353 353 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 355 355 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 419 419 Dimethylallyl diphosphate. {ECO:0000250}. FT BINDING 423 423 Dimethylallyl diphosphate. {ECO:0000250}. FT CONFLICT 165 165 R -> K (in Ref. 2; ACF22981). FT {ECO:0000305}. FT CONFLICT 171 171 P -> A (in Ref. 2; ACF22981). FT {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 //