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Database: UniProt
Entry: H6MX61_GORPV
LinkDB: H6MX61_GORPV
Original site: H6MX61_GORPV 
ID   H6MX61_GORPV            Unreviewed;       487 AA.
AC   H6MX61;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 50.
DE   SubName: Full=Cytochrome P450 monooxygenase {ECO:0000313|EMBL:AFA72983.1};
GN   OrderedLocusNames=GPOL_c19420 {ECO:0000313|EMBL:AFA72983.1};
OS   Gordonia polyisoprenivorans (strain DSM 44266 / VH2).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1112204 {ECO:0000313|EMBL:AFA72983.1, ECO:0000313|Proteomes:UP000009154};
RN   [1] {ECO:0000313|EMBL:AFA72983.1, ECO:0000313|Proteomes:UP000009154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44266 / VH2 {ECO:0000313|Proteomes:UP000009154};
RX   PubMed=22327575; DOI=10.1128/AEM.07969-11;
RA   Hiessl S., Schuldes J., Thurmer A., Halbsguth T., Broker D., Angelov A.,
RA   Liebl W., Daniel R., Steinbuchel A.;
RT   "Involvement of two latex-clearing proteins during rubber degradation and
RT   insights into the subsequent degradation pathway revealed by the genome
RT   sequence of Gordonia polyisoprenivorans strain VH2.";
RL   Appl. Environ. Microbiol. 78:2874-2887(2012).
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; CP003119; AFA72983.1; -; Genomic_DNA.
DR   RefSeq; WP_014359721.1; NC_016906.1.
DR   AlphaFoldDB; H6MX61; -.
DR   STRING; 1112204.GPOL_c19420; -.
DR   KEGG; gpo:GPOL_c19420; -.
DR   eggNOG; COG2124; Bacteria.
DR   HOGENOM; CLU_001570_5_1_11; -.
DR   OMA; WKETRSQ; -.
DR   Proteomes; UP000009154; 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   CDD; cd11053; CYP110-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:SF166; CYTOCHROME P450 12A4, MITOCHONDRIAL-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|RuleBase:RU000461}; Iron {ECO:0000256|RuleBase:RU000461};
KW   Metal-binding {ECO:0000256|RuleBase:RU000461};
KW   Monooxygenase {ECO:0000256|RuleBase:RU000461, ECO:0000313|EMBL:AFA72983.1};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU000461};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009154}.
SQ   SEQUENCE   487 AA;  52961 MW;  8BF1D019D51BDFE4 CRC64;
     MTASTEYHPA LTGRWFDAAP DAASGLVSTC AEAGPLSASD ADALPAPPTP RRATVRNALR
     FARREGDVVF ADAARCGDVL TYDLPGAPGR LVVISDPAHV RSVLTADPAI APSATRLSPL
     RPIVGPDSVL TTLAEQHRRQ RTALLPSFHR TSVARYTDVI EQASAAHLDR WPTNRRVRVD
     RIAQAITLDV IMAVIFGIHA ADGVLTDDVP DVATTAERHL RDATRRFLRW SSSAVGTVAQ
     LLNASHPEPV GLLAWGVRHL DAAIAEVIAE RRAGGHASDD DVMSALLAAR AIDGLPLSDS
     EIRDELVSLL LAGHETTATT IAWAFERLTR HPEVYAQARS AAAEGDDEFV GAVITETMRC
     RPVVPSVARE LQRPWRFGTH RCESGDIAVV STLLLHHRDD LYPHPFDFRP DRFIGTRTDP
     MTLLPFGGGN RRCLGAHLAM TELQIVVGDI LRRVELETHD RPAERPRYRN VTMIPARGGT
     VRALSVD
//
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