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Database: UniProt
Entry: V2X075_MONRO
LinkDB: V2X075_MONRO
Original site: V2X075_MONRO 
ID   V2X075_MONRO            Unreviewed;       502 AA.
AC   V2X075;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   SubName: Full=Benzoate 4-monooxygenase cytochrome p450 {ECO:0000313|EMBL:ESK87212.1};
GN   ORFNames=Moror_5832 {ECO:0000313|EMBL:ESK87212.1};
OS   Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS   (Crinipellis roreri).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK87212.1, ECO:0000313|Proteomes:UP000017559};
RN   [1] {ECO:0000313|EMBL:ESK87212.1, ECO:0000313|Proteomes:UP000017559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK87212.1,
RC   ECO:0000313|Proteomes:UP000017559};
RX   PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA   Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA   Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA   Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA   Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT   "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT   Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT   mechanisms of the biotrophic and necrotrophic phases.";
RL   BMC Genomics 15:164-164(2014).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR602403-1};
CC   -!- PATHWAY: Secondary metabolite biosynthesis.
CC       {ECO:0000256|ARBA:ARBA00005179}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC       {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ESK87212.1}.
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DR   EMBL; AWSO01000820; ESK87212.1; -; Genomic_DNA.
DR   RefSeq; XP_007853475.1; XM_007855284.1.
DR   AlphaFoldDB; V2X075; -.
DR   STRING; 1381753.V2X075; -.
DR   KEGG; mrr:Moror_5832; -.
DR   HOGENOM; CLU_001570_14_4_1; -.
DR   OrthoDB; 1776156at2759; -.
DR   Proteomes; UP000017559; Unassembled WGS sequence.
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; cd11062; CYP58-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR   PANTHER; PTHR24305:SF157; N-ACETYLTRYPTOPHAN 6-HYDROXYLASE IVOC-RELATED; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00465; EP450IV.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR602403-1};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461, ECO:0000313|EMBL:ESK87212.1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000017559};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..502
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004712073"
FT   BINDING         446
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:PIRSR602403-1"
SQ   SEQUENCE   502 AA;  56725 MW;  D37A0FB0C1DFE9B6 CRC64;
     MNQAFIAIAL AIAVTLFVRL VRPDPLKRNP GPLLARWTWL YRAYYDIVVG GGWVAHLHNL
     HEQYGPVVRV GRNELHFTEP AAYADIYNSP YKMPKDPDLY RRAFEIGLPP GVFSVVNAKD
     HSEIKSLFSS YFSRKSVLKL ENVIQERIDK LISQLLKNHK TIPASMNHAF RCVTLDVISL
     YTLRTNPDTT SFPTFHHPAI LGVDDSIAAT WVFKHLTLLK NIAIRLPTWL IMRILPTSSA
     RLEIQAEIEK QVDIAMRDSQ KYDPDSESNL NVFYTLLSNA RIEGKLRRPN RVSREWLITE
     GTSLQVAGSD TVGNACTIGA RCLVRDNAVR AKLVQELETA WPDQGNHLPL ERLEKLPYLT
     AVIKESLRLS FGVVSPMNRV APEGGAVIAG HPVPPGTIVS IANPFVHMNP EIFPDPARFN
     PERWLEDKVH SLDRYLVSFG KGPRSCLGIN LAWCELYLIL GNIFRKLDFH GDSDLRSEVQ
     YKDFFVPLYK GDVLSATVSE RL
//
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