ID A0A1J7JNL5_9PEZI Unreviewed; 517 AA.
AC A0A1J7JNL5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Benzoate 4-monooxygenase cytochrome P450 {ECO:0000313|EMBL:OIW31472.1};
GN ORFNames=CONLIGDRAFT_697695 {ECO:0000313|EMBL:OIW31472.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW31472.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW31472.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW31472.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) 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|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; KV875095; OIW31472.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7JNL5; -.
DR STRING; 1408157.A0A1J7JNL5; -.
DR InParanoid; A0A1J7JNL5; -.
DR OrthoDB; 3184603at2759; -.
DR Proteomes; UP000182658; 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; IPR002401; Cyt_P450_E_grp-I.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24305; CYTOCHROME P450; 1.
DR PANTHER; PTHR24305:SF147; 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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461, ECO:0000313|EMBL:OIW31472.1};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000182658}.
SQ SEQUENCE 517 AA; 59432 MW; 037198C86E2DEE26 CRC64;
MSSTFSIDGA LAIVTVNNGL RLFGLWFVYR LLLTLYNISP FHPLYKFPGP RLAAASYLYE
AWYDLVKVGR YSWEIKAMHE KYGPIVRINP EELHCDDYDF VEEIYPSIAN RIRDKHPHFL
AAFAGPLTVS TFATRDHETH RIRRSAISKF FSRQQMLRYE PEIHDMAQKM CSKVLRLTES
GQIINALDPF NCFTADAISQ YCFGEPFGFL DRPDFEQNYK RAFEVLVATS HIFRHIPILR
HTIGLMPALG PYLGPDIAYM VKSMHETIPN HVIKAQQQQK SGEGRRVFTE IMDAPIPDEH
KTPYRLSGEG WSLVAAGSET TAASLTAITF FLLSQPEKLA RLREELKHED PQKLSWVQLE
KYPYLHGVIF ESFRVALGIS GRLPRVARND DLVYNNRGFH YVVPKGTAIG MSAFINHYNE
EMFPEPEKYE PERWIDAEGK PNYVMEKYIM SFSKGSRQCI GMHLAFCELY LVTAAMALRV
LPHLKLYDTT YEDIKYDFDA LTPQPKKGAR GVRITGI
//