ID M2YHL6_PSEFD Unreviewed; 1035 AA.
AC M2YHL6;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Bifunctional cytochrome P450/NADPH--P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE Includes:
DE RecName: Full=Cytochrome P450 {ECO:0000256|PIRNR:PIRNR000209};
DE EC=1.14.14.1 {ECO:0000256|PIRNR:PIRNR000209};
DE Includes:
DE RecName: Full=NADPH--cytochrome P450 reductase {ECO:0000256|PIRNR:PIRNR000209};
DE EC=1.6.2.4 {ECO:0000256|PIRNR:PIRNR000209};
GN ORFNames=MYCFIDRAFT_88699 {ECO:0000313|EMBL:EME77285.1};
OS Pseudocercospora fijiensis (strain CIRAD86) (Black leaf streak disease
OS fungus) (Mycosphaerella fijiensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Pseudocercospora.
OX NCBI_TaxID=383855 {ECO:0000313|EMBL:EME77285.1, ECO:0000313|Proteomes:UP000016932};
RN [1] {ECO:0000313|EMBL:EME77285.1, ECO:0000313|Proteomes:UP000016932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIRAD86 {ECO:0000313|EMBL:EME77285.1,
RC ECO:0000313|Proteomes:UP000016932};
RX PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA Grigoriev I.V.;
RT "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT genomes of eighteen Dothideomycetes fungi.";
RL PLoS Pathog. 8:E1003037-E1003037(2012).
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|PIRNR:PIRNR000209};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein
CC reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein
CC reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-
CC COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:30879, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC ChEBI:CHEBI:142491; EC=1.14.14.1;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRNR:PIRNR000209,
CC ECO:0000256|PIRSR:PIRSR000209-1};
CC -!- SIMILARITY: In the N-terminal section; belongs to the cytochrome P450
CC family. {ECO:0000256|PIRNR:PIRNR000209}.
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DR EMBL; KB446566; EME77285.1; -; Genomic_DNA.
DR RefSeq; XP_007932061.1; XM_007933870.1.
DR AlphaFoldDB; M2YHL6; -.
DR STRING; 383855.M2YHL6; -.
DR GeneID; 19342731; -.
DR KEGG; pfj:MYCFIDRAFT_88699; -.
DR eggNOG; KOG0157; Eukaryota.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_7_0_1; -.
DR OrthoDB; 1691317at2759; -.
DR Proteomes; UP000016932; Unassembled WGS sequence.
DR GO; GO:0070330; F:aromatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003958; F:NADPH-hemoprotein reductase activity; IEA:UniProtKB-UniRule.
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; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR008254; Flavodoxin/NO_synth.
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; 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; PR00463; EP450I.
DR PRINTS; PR00385; P450.
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 3: Inferred from homology;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982,
KW ECO:0000256|PIRNR:PIRNR000209}; FAD {ECO:0000256|PIRNR:PIRNR000209};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW ECO:0000256|PIRNR:PIRNR000209};
KW FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR000209};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Heme {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Iron {ECO:0000256|PIRNR:PIRNR000209, ECO:0000256|PIRSR:PIRSR000209-1};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000209,
KW ECO:0000256|PIRSR:PIRSR000209-1};
KW Monooxygenase {ECO:0000256|PIRNR:PIRNR000209};
KW NADP {ECO:0000256|PIRNR:PIRNR000209};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000209};
KW Reference proteome {ECO:0000313|Proteomes:UP000016932};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR000209}.
FT DOMAIN 497..637
FT /note="Flavodoxin-like"
FT /evidence="ECO:0000259|PROSITE:PS50902"
FT DOMAIN 668..874
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT BINDING 405
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 1035 AA; 114727 MW; 6728E1AF5A3CD751 CRC64;
MASNVPQPKA WPIIGNVLDV DTVNMTQSFE RLADKYGEIY KLDLLGKPTY VISSVALVAE
VCDEKRFCKK IDTFLNQLRL AVGDGLFTAH NHEHNWGVAH RALMPAFGPL PIQAMYDEMY
DIASQLVSKW ARDGADHEIN VTDDMTRLTL DSIALCAMDY RFNSFYHEEV HEFIRAMGDV
LLESGKRAMR SKIEAWLNPS AEKKFFADIA TLKKVAQQCI DRRRAGPGKK DLLDAMLNGK
DPKTGEKLSD ESIINNMITF LVAGHETTSG MLSFTLFYLL KNPETLQRAQ QEVDSVVGSG
PIEFKHIKEL KYIEAALREA LRLCPTTVGF SVGPVPGTKG PVTLAGKYVL PPDAVIMILG
TRSGRDPKVF GEDAAEFKPE RMHDEHFNKL PPGAWKPFGN GMRGCIGRPF AWQEAILALG
IILQNFNLRF ADPSYELKIA ETLTIKPDNL LIKAQLRDGI DPIQLSKKLH GEIRTAAREE
PAKHLASSKS SGDSGQLTIF FGSSAGTCEG LAQSLAASAR VRGFDTVVKS LDAAVDRFPK
DHPVIIITCT YEGQPPDNAK IFVEWLKTAD RSKFEGAQVT IFGCGHRDWV STYQKMPRTI
EGELTAKGAA LLAPRGETDT SQGTILDDFD AWTSRLWPSI SADGKEYSSA SSLELRLSTN
SRASHLHHKV WDAKVVSNRR ITSLEAPEKR HVTISLPRDM QYDAGDYLAV LPLNNQQLVS
RVLRRFSLPW DTAMTITSGS HATIPENREL PVALILSGYI ELGARASRKS RDVLSEHSKL
SLADERGSII DILERHPDIS IPFGTFLELH MPLRLRQYSI SSSPLADPSL ATITFSVIES
DEHIGTATSY LKSLEPGSTL QVAVKKSSAA FHLPLDESIP VIMVAAGTGL APFRGFLQER
AVKAEAGRQL GEALLFVGCR DPNQDKIFAE ELAQWENLGV VKVRYAYSRA SEQSDGCRYV
QDRVYKEAAE IARLFDLGAR IYICGSGAMG RSVSDVAVRL LVEEAEDKGE KLSEEDARLR
WEKWRGERYA LDVFD
//
