ID A0A167BDR2_9PEZI Unreviewed; 523 AA.
AC A0A167BDR2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cytochrome p450 monooxygenase {ECO:0000313|EMBL:KZL81200.1};
GN ORFNames=CI238_08706 {ECO:0000313|EMBL:KZL81200.1};
OS Colletotrichum incanum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=1573173 {ECO:0000313|EMBL:KZL81200.1, ECO:0000313|Proteomes:UP000076584};
RN [1] {ECO:0000313|EMBL:KZL81200.1, ECO:0000313|Proteomes:UP000076584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MAFF 238704 {ECO:0000313|EMBL:KZL81200.1,
RC ECO:0000313|Proteomes:UP000076584};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) 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:KZL81200.1}.
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DR EMBL; LFIW01001728; KZL81200.1; -; Genomic_DNA.
DR STRING; 1573173.A0A167BDR2; -.
DR OrthoDB; 1351063at2759; -.
DR Proteomes; UP000076584; 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; cd11041; CYP503A1-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; PTHR46206; CYTOCHROME P450; 1.
DR PANTHER; PTHR46206:SF3; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR602403-1};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000076584}.
FT BINDING 462
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 523 AA; 59295 MW; 55A407B56BCDCF43 CRC64;
MDGTETARSP LGARGFTLDA SVKPLPYFLT TVLVVLFVYS MQSSKLNIPS INQKKRFELT
NSRPKRNYLI NARGIIRQWF SKNPNKPTRL ISDMGETIVL PPSMANEIRN NNHLSFTEFS
KEFFQTKYPG FNAFAEGTHD SITLVVINKD LTKQLAKVTE PLAEETSLAL RDIFTENKDW
HSIPMRATIL HFIARISSRV FLGTELCRNE SWLEITKNYT LNGFTAADRL REYPPFLRNF
VHWFLPGCQS ARKQIQEAAA IIQPIIDKRH ALKAQAIADG RPTPEYHDAI EWFEQASVSK
GMPHDPALSQ LFLSTVAIHT TTDLLGQVLV DLAKNPEIIK DLQKEALDVL KDGGWKKTSL
YSMKLLDSVV KESQRIKPLQ LASMQRVATT DVTLSDGTFI PKGTCVCVSS HAHWDPKVYP
EPEHWDGYRF YRMREQTGQE NVSQLVSTSP EHLGFGHGKH ACPGRFFAAN EIKIALVHIL
LQYEWKIPTG ANTDITDYGI SPALNPNLEL EIRRRSDEVD LNF
//