ID G5EJY5_PHACH Unreviewed; 1057 AA.
AC G5EJY5;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:BAL05197.1};
GN Name=PcCYP_187a {ECO:0000313|EMBL:BAL05197.1};
OS Phanerodontia chrysosporium (White-rot fungus) (Sporotrichum pruinosum).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Phanerochaetaceae; Phanerodontia.
OX NCBI_TaxID=2822231 {ECO:0000313|EMBL:BAL05197.1};
RN [1] {ECO:0000313|EMBL:BAL05197.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 34541 {ECO:0000313|EMBL:BAL05197.1};
RA Hirosue S., Hiratsuka N., Ichinose H., Wariishi H.;
RT "Phanerochaete chrysosporium cytochrome P450.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2
CC reduced [cytochrome P450]; Xref=Rhea:RHEA:24040, Rhea:RHEA-
CC COMP:14627, Rhea:RHEA-COMP:14628, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:55376, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:60344; EC=1.6.2.4;
CC Evidence={ECO:0000256|ARBA:ARBA00036596};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|ARBA:ARBA00001917};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|ARBA:ARBA00010018}.
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DR EMBL; AB597910; BAL05197.1; -; mRNA.
DR AlphaFoldDB; G5EJY5; -.
DR SMR; G5EJY5; -.
DR VEuPathDB; FungiDB:AGR57_3013; -.
DR GO; GO:0070330; F:aromatase activity; IEA:InterPro.
DR GO; GO:0010181; F:FMN binding; IEA:InterPro.
DR GO; GO:0020037; F:heme binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:InterPro.
DR CDD; cd06206; bifunctional_CYPOR; 1.
DR CDD; cd11068; CYP120A1; 1.
DR Gene3D; 3.40.50.360; -; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR023206; Bifunctional_P450_P450_red.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001094; Flavdoxin-like.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR029039; Flavoprotein-like_sf.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF127; BIFUNCTIONAL CYTOCHROME P450_NADPH--P450 REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00258; Flavodoxin_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR Pfam; PF00067; p450; 1.
DR PIRSF; PIRSF000209; Bifunctional_P450_P450R; 1.
DR PRINTS; PR00369; FLAVODOXIN.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF52218; Flavoproteins; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
DR PROSITE; PS51384; FAD_FR; 1.
DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1.
PE 2: Evidence at transcript level;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Heme {ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRSR:PIRSR000209-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000209-1};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 494..634
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 671..900
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 402
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:PIRSR000209-1"
SQ SEQUENCE 1057 AA; 116449 MW; 71179747F031C4F5 CRC64;
MATPIPSPPS VPFLGHVTII DREVAIYSYN LLAKQYGEIY QLSMMGSKVV VICSQELLHE
VSDEKRFRKV PSSALDQVGN AAGEGLFTAH GDNPNWHLTH RILMPALSTM NTRNMFDDMV
DIVNQPVQKW ERFGPRYKID PSQDFTALTL EAITFCAMSY RMNTFYVEGV HPFARAMADF
LVESGNRALR PGIVQPLMRA TNSKYEENIK TMQKYVDDVY NQRKENPTDK KDILNLMMYG
KDPKTGERSS EKTIKENLLT FLIAGHETTS GMLTFILYYL LKNPEAMRKL REEVDTMIGS
RTMTVDDVHK LPYLIAVMRE TLRLGPPAPA RGTAPFEDAL LKGKYPVAKD GRIYCGIYMV
HRDPKVWGED AEEFRPERML DGRFEALPPE AWQPFGFGVR ACIGRPFAWQ EAQITVVYLM
QRFTFVMHDP SYDLQLKQTL TIKPHEFFIR TIPRTDRPSI VPVATPSSTL LRDQTAPAAQ
PPVTTPGEGG GHRMYVLCGS NTGTCEAFAQ RIASDATVHG FKAVIGTLDS AAGHLPSDGP
VVVVTASFEG QPADNAAHFV SWLSALNGSE LADVSFAAFG CGNRDWASTY QRIPTLCDDT
MAARGGKRHA PRGEGDAGSS DLFESFEHWE AGLWEALQKT HGTTKVEGRQ EAIKVSTVDA
GTARATALRQ PDTMLGTVVE NRLLTSPGVA EKHHIEFQLP DGLTYRTGDY LAILPMNPSR
DVQRVLAHFS LLPDQEVTIS AAGPSPLPTG RPVNVSSLLS GYVELSQAAT TRDLRILIDA
AKSEDTKAAL SELLDGYAEK VQAGRLSVLD ILEAHPGLDI SFALFLQLLP SMRVRQYSIS
SSPLADPTRA SLTVSVLSAV PTAGRREPFL GVASTYLASL RAGDCVQLAV RPSAAAFHPP
ADPAVPLVLF CAGAGLAPMR GFLQERVLQK QAGRDVATSI LFFGCRSPQH DFLYADSDLR
TWTELGVVDV RPAFSRETEQ SAGCKYVQDR VWADREDVVK VWQAGAKVYV CGSGRMATAV
KQRLVEIIAA QLNVDSEQAT DTFNKIIKGR FATDVFE
//
