ID W5TC58_9NOCA Unreviewed; 445 AA.
AC W5TC58;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:AHH16822.1};
GN ORFNames=NONO_c20220 {ECO:0000313|EMBL:AHH16822.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH16822.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH16822.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH16822.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
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; CP006850; AHH16822.1; -; Genomic_DNA.
DR RefSeq; WP_025348310.1; NZ_CP006850.1.
DR AlphaFoldDB; W5TC58; -.
DR STRING; 1415166.NONO_c20220; -.
DR KEGG; nno:NONO_c20220; -.
DR PATRIC; fig|1415166.3.peg.2054; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_1_11; -.
DR Proteomes; UP000019150; Chromosome.
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 Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR PANTHER; PTHR46696:SF1; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
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 Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150}.
SQ SEQUENCE 445 AA; 50182 MW; BFECC24D88D99D8E CRC64;
MTDHRQPRYE FDRHSPQYRD RFDTITDEMH RRCPIAWSPT YGGHWVAAGS REVFSLARSE
NVSSDHDPNG ERRGYHGITI PFPETGIPIR NGILEMDPPE QRLWRQVLNP YLSPAAVQRW
IPLVDEVVRA SLDDRIESGS IDFVDDLANI VPAVLTLAML GIRLDKWQLY CEPAHASVYT
PPNSPDTPRV RRMHEAMGLD LMTNLIEVRE HPRPGIVNEL AHMEIDGAAP PDIEILGMLG
LLIGGGFDTT TALTAHALEW LSDHPDERQT LSAERDLLLN SATEEFLRYF TPAPGDGRTI
AADCEYAGTS FKEGERLWLS WAMANRDPQL FPDPNTVDLD RKANRHFSFG LGIHRCIGSN
VARTVFKRML VAVLDRMPDF RCDPDGAVHY DTIGVIQGMR RLPATFTPGP RLGPGVEETL
QTLQRVCEEQ RLAEPVTVRR DSAEI
//
