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Database: UniProt
Entry: A0A1J7JNL5_9PEZI
LinkDB: A0A1J7JNL5_9PEZI
Original site: A0A1J7JNL5_9PEZI 
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
//
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