ID A1UDY6_MYCSK Unreviewed; 413 AA.
AC A1UDY6;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:ABL91044.1};
GN OrderedLocusNames=Mkms_1843 {ECO:0000313|EMBL:ABL91044.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL91044.1};
RN [1] {ECO:0000313|EMBL:ABL91044.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL91044.1};
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) 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; CP000518; ABL91044.1; -; Genomic_DNA.
DR AlphaFoldDB; A1UDY6; -.
DR STRING; 189918.Mkms_1843; -.
DR KEGG; mkm:Mkms_1843; -.
DR HOGENOM; CLU_033716_0_0_11; -.
DR OrthoDB; 5241086at2; -.
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; 2.
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 413 AA; 45505 MW; 55C3EA3962B523C7 CRC64;
MSAPIIDAAA RVFATPRAYT DEPALHAALT HLRAHAPVSW VDVDGYRPFW AVTKHADIMA
IERANTVFTN SPRSVLMTAT ADELQAGVGI RTLIHLDDPE HRDLRAIGAD WFRPKAMRAL
KVRVDELARI YVDKMLATGP ECDFVQEVAV NYPLYVIMSL LGVPEADFPL MLKLTQELFG
SDDEEFQRGD SSEEQMAALL EMFQYFTALT ASRREHPTDD LASAIANARL GGEPLSDIDT
VSYYAIVAAA GHDTTSATIS GGMLALIEHP DQLRRLQADP GLMGLAAEEM IRWVTPVKAF
MRTAAQDTEV RGVPIKAGES LLLSYVSGNR DDDVFDAPFR FDVGRDPNRH VSFGYGVHFC
LGAALARMEV NSFFAELLPR LRSVELAGRP EHVATTFVGG LKHLPIRYAL RPA
//
