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Database: UniProt
Entry: A0A135UK25_9PEZI
LinkDB: A0A135UK25_9PEZI
Original site: A0A135UK25_9PEZI 
ID   A0A135UK25_9PEZI        Unreviewed;       498 AA.
AC   A0A135UK25;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Prostacyclin synthase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CSAL01_04294 {ECO:0000313|EMBL:KXH60716.1};
OS   Colletotrichum salicis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1209931 {ECO:0000313|EMBL:KXH60716.1, ECO:0000313|Proteomes:UP000070121};
RN   [1] {ECO:0000313|EMBL:KXH60716.1, ECO:0000313|Proteomes:UP000070121}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 607.94 {ECO:0000313|EMBL:KXH60716.1,
RC   ECO:0000313|Proteomes:UP000070121};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum salicis CBS 607.94.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXH60716.1}.
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DR   EMBL; JFFI01001364; KXH60716.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135UK25; -.
DR   STRING; 1209931.A0A135UK25; -.
DR   OrthoDB; 1782613at2759; -.
DR   Proteomes; UP000070121; Unassembled WGS sequence.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd11040; CYP7_CYP8-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR47582; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   PANTHER; PTHR47582:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602403-1,
KW   ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000070121}.
FT   BINDING         425
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ   SEQUENCE   498 AA;  55470 MW;  53C3D30F924D7FA1 CRC64;
     MLGILGLDNG FVPSLALLTA IPVMLYLAHL VRSPVAMDAK EPPLLRPKVP FIGHIIGIFK
     HSWDAKSKAP MFTLPTLGCK IFDPFLRDLI KGMAGASAQM MKAWDDPAFY GPWVKSLYGG
     MAGQSLLTLN ISAVGGIATA LNEIGDDVEV ADLYMWNREL FTLASTDSLY GSKNPLRVDK
     KLIEEYWDYE ADVNKLMLGI FPSIIARKGY CGQALFEEVF KSFFDSQLHE SDDFLSLVKD
     RRKLSISFDM TSAEAAKIEL IFLHGAVSNT FPEFYWFFTR IFSQPEHLSR LREEVQGVIE
     EKGRDVVDER EKRVFVLHME KSEEKCPLLM SCFREAHRLY AAGILAREVM TDTTISDGKM
     SYTVKKDWQI SVPQKILQTD FGIWGDDALE FIGDRFLKIA KEKGEAVVNA AVRGFLGFGG
     GKHICPGRYI ASGELLGFLA LLVAGFDVTS SDGDAFTVPK ATSVPLTGSF GKPVPGNDLR
     GRMRRRAGWE DVQWEVVA
//
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