ID A0A0D1YQ85_9EURO Unreviewed; 514 AA.
AC A0A0D1YQ85;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Benzoate 4-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV11_00670 {ECO:0000313|EMBL:KIV84922.1};
OS Exophiala sideris.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1016849 {ECO:0000313|EMBL:KIV84922.1, ECO:0000313|Proteomes:UP000053599};
RN [1] {ECO:0000313|EMBL:KIV84922.1, ECO:0000313|Proteomes:UP000053599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 121828 {ECO:0000313|EMBL:KIV84922.1,
RC ECO:0000313|Proteomes:UP000053599};
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 Exophiala sideris CBS121828.";
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; KN846951; KIV84922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D1YQ85; -.
DR STRING; 1016849.A0A0D1YQ85; -.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000053599; 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:UP000053599};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 514 AA; 57930 MW; 5011EA51C39FF477 CRC64;
MFVSSIFSPW TLLLLPVLYF VLPYLRNWSL LKVPGPLPAA LTNLWLMYQC RRGRRYQAVN
NLHKKYGKVV RIQPNHVSIA DDSAIPIIYG HGNGFLKSEY YDAFVSIQRG LFNTRDRIEH
TRKRKVVSHT FSAKSIGQFE QYIHANLELF VRKWTDLSQN RANPSTGYAS IDALHWFNYL
AFDIIGDLAF GMPFGMLERE KDYAEIRKSP DAPPATAPAI EVLNRRGEVS GTLGCLPQLK
PYAKYLPDPF FSKGVEAVEN LAGIAIARVK QRLDNPNTDR VDLLARLMEG KDAKGEKLGR
EELTAEALTQ LIAGSDTTSN TACAILYYIV RTPGVVENLQ KELDANIPPG VPTYEQVKDL
DYVQWVINET MRIHSTSSLG LPRLVPSATP ENPNPQPVEI LGYAFPPGTA LSVPSYTIHH
STEIWGDDAD DFVPERWSEK RLTARQKEAF IPFSTGPRAC VGRNVAEMEL KCMVGTVFRN
FEFRDEHAGP METREGFLRK PLGYNVGLRL RKGI
//
