ID A0A0D2ELP5_9EURO Unreviewed; 524 AA.
AC A0A0D2ELP5;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Benzoate 4-monooxygenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV05_05038 {ECO:0000313|EMBL:KIW56373.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW56373.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW56373.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW56373.1,
RC ECO:0000313|Proteomes:UP000054342};
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 xenobiotica CBS118157.";
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; KN847319; KIW56373.1; -; Genomic_DNA.
DR RefSeq; XP_013316957.1; XM_013461503.1.
DR AlphaFoldDB; A0A0D2ELP5; -.
DR STRING; 348802.A0A0D2ELP5; -.
DR GeneID; 25326946; -.
DR HOGENOM; CLU_001570_14_0_1; -.
DR OrthoDB; 408598at2759; -.
DR Proteomes; UP000054342; 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; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF172; P450, PUTATIVE (EUROFUNG)-RELATED; 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:UP000054342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 524 AA; 59764 MW; C7907148434D3B18 CRC64;
MSVMASSAHV HGTFPVFPLW EATVVLLIGA ALLYPVICYF HDPKKLRRFP APSIAGFTNL
WMMFQQYNHN RALSTHAAHE KLGKIVRVGP NHISFVGRQA TKDIYGHGTP AQKDKFYISF
TGTHESSLDV TDRHMHSEKR KRLAAAFAQK RIADMEHLVV EDIQRLLVRF DKAVDEQELI
NVRWYINMLL FDLTGDLVFS QNLGCVERGD DLMQAQKLDG TKYWTKPADA LRNSLRIGST
MGWNADLFPY LKRLTWWHEG WKGGADFTAI VLHMVRTRLE REKEGVELND FFKSLVWDRN
GDPLGLEIGE MVAECGLLLN AGSDTTSIVL TGTIYLLTKW PRTAEKLRKE LDDALGDSDD
HGVCAFDEVK NLPYLRACVD EAMRMRPPLR GGLPRVTPPE GMMIAGEWIA GNTTVSVPTY
SLHHDPDLFS DPWTYKPERW LEDDAADLQQ VFIPFSAGGR GCIGRNVSYL ELLVVVSTLM
RRYEFEFEKP DFELETKDTV NAHPGPMMMR IRRRKRNVDH EEIV
//
