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
//