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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//