ID A4T5Y4_MYCGI Unreviewed; 404 AA.
AC A4T5Y4;
DT 15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 15-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 91.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ABP43803.1};
GN OrderedLocusNames=Mflv_1321 {ECO:0000313|EMBL:ABP43803.1};
OS Mycolicibacterium gilvum (strain PYR-GCK) (Mycobacterium gilvum (strain
OS PYR-GCK)).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350054 {ECO:0000313|EMBL:ABP43803.1};
RN [1] {ECO:0000313|EMBL:ABP43803.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43803.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Miller C., Richardson P.;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABP43803.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYR-GCK {ECO:0000313|EMBL:ABP43803.1};
RX PubMed=23469141;
RA Badejo A.C., Badejo A.O., Shin K.H., Chai Y.G.;
RT "A Gene Expression Study of the Activities of Aromatic Ring-Cleavage
RT Dioxygenases in Mycobacterium gilvum PYR-GCK to Changes in Salinity and pH
RT during Pyrene Degradation.";
RL PLoS ONE 8:E58066-E58066(2013).
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; CP000656; ABP43803.1; -; Genomic_DNA.
DR AlphaFoldDB; A4T5Y4; -.
DR STRING; 350054.Mflv_1321; -.
DR KEGG; mgi:Mflv_1321; -.
DR eggNOG; COG2124; Bacteria.
DR HOGENOM; CLU_033716_0_2_11; -.
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; cd11033; CYP142-like; 1.
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 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};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
SQ SEQUENCE 404 AA; 45314 MW; F0635CAD3058D8D8 CRC64;
MPPPLHSPAF YAGDPFPAYR ELRATDPVTW NEEHGFWALL KYEDIRYVST NPALFSSARG
ITVPDPAIEN PVMEGSLIFT DPPRHRRLRK LINSGFTRRQ VAILEPKLRA FARTALDAID
PAGGTEFAER IAAPLPTRMI AELLGAPDED WEQFRRWSDA AVGMDDPDVE LDTFTAMGEL
YQYFEKLIAL RRNGALRDSD DLLSVLVAAE VDGVRLSDQD LLQFCLLLLV AGNETTRNLI
ALGTLALIEH PQQFRLLREH PELIPTAVEE FLRYTSPVAN MTRCATRDVE MRGRLIREGQ
YVTMLYGSAN RDEDIFGPTS EQLDVTRNPN PHLAFGCGEH SCLGAQLARL EARVLFEELL
ARFEHIEPAG EVLRMQATMV PGVRAMPVRL RAATDPRRAK ARAG
//
