ID A0A0D2JNE7_9EURO Unreviewed; 515 AA.
AC A0A0D2JNE7;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Benzoate 4-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=Z520_12280 {ECO:0000313|EMBL:KIX92009.1};
OS Fonsecaea multimorphosa CBS 102226.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX NCBI_TaxID=1442371 {ECO:0000313|EMBL:KIX92009.1, ECO:0000313|Proteomes:UP000053411};
RN [1] {ECO:0000313|EMBL:KIX92009.1, ECO:0000313|Proteomes:UP000053411}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 102226 {ECO:0000313|EMBL:KIX92009.1,
RC ECO:0000313|Proteomes:UP000053411};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Fonsecaea multimorphosa CBS 102226.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KN848113; KIX92009.1; -; Genomic_DNA.
DR RefSeq; XP_016626132.1; XM_016782766.1.
DR AlphaFoldDB; A0A0D2JNE7; -.
DR STRING; 1442371.A0A0D2JNE7; -.
DR GeneID; 27718026; -.
DR VEuPathDB; FungiDB:Z520_12280; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000053411; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd11061; CYP67-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
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 PANTHER; PTHR24305:SF29; BENZOATE-PARA-HYDROXYLASE; 1.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
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|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000053411};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 515 AA; 57933 MW; E3ECE9F5BE1E7181 CRC64;
MVIVAMPLGA HLVIWSITIF LGYYILPYLT TYSSLRRIPA ASFWAAFSNF WLALQSRRVK
RSLTVHEAHL RKGEVVRIQP NHVSIANKNA IQIIYGHGNG FLKSDFYDAF VTFGPGLFST
RDRNEHTRKR KTVSHTFSAK SVAQFEQYMR CHLDVLIRQW DGRCQNANGQ FARIDSMRWS
NYLAFDIIGD LAFGQPFGML EKGQDITEVK SKIDGQISYC RAIESINVRG ELMNTLGSVP
FLIPYAKYIP DPLVQRGLRA KGGVHGIGVA SVSARLEAGS GHDRVDILAR LIEGKDENGQ
PMGKAELLSE ALTQIVAGSD TTSTALCALT YWMLKTPRIL ERLQKELDSV LPDDVEIPTF
EQVKDLPYLK MVINEALRVH PPVSLGLPRV VPPGPGVELC GHFFPPGTVL SVPIYTMHHS
KEIWGSDADE FKPERWETVT EEQRAAFIPF SVGPRSCIGR NVAEMELILA VATIAFRYDF
RLYEEEWSLR ESLLRKPTGC EIGIRLRVRP QNSTI
//
