ID A0R4K0_MYCS2 Unreviewed; 400 AA.
AC A0R4K0;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 115.
DE SubName: Full=Cytochrome P450 109 {ECO:0000313|EMBL:ABK71599.1};
DE EC=1.14.-.- {ECO:0000313|EMBL:ABK71599.1};
GN OrderedLocusNames=MSMEG_5861 {ECO:0000313|EMBL:ABK71599.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:ABK71599.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK71599.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
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DR EMBL; CP000480; ABK71599.1; -; Genomic_DNA.
DR RefSeq; WP_011730851.1; NZ_SIJM01000007.1.
DR RefSeq; YP_890088.1; NC_008596.1.
DR AlphaFoldDB; A0R4K0; -.
DR STRING; 246196.MSMEG_5861; -.
DR PaxDb; 246196-MSMEI_5702; -.
DR GeneID; 66737149; -.
DR KEGG; msm:MSMEG_5861; -.
DR PATRIC; fig|246196.19.peg.5704; -.
DR eggNOG; COG2124; Bacteria.
DR OMA; WGHRNPD; -.
DR OrthoDB; 502624at2; -.
DR Proteomes; UP000000757; 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; cd11078; CYP130-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:SF2; CYTOCHROME P450 130; 1.
DR PANTHER; PTHR46696; 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|ARBA:ARBA00022617, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU000461};
KW Metal-binding {ECO:0000256|RuleBase:RU000461};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033,
KW ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU000461};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
SQ SEQUENCE 400 AA; 44946 MW; 6B111F480F3A2B35 CRC64;
MSLPTVEPVL DPYDYDFHED PYPYYKRLRD EAPLYRNDER NFWALSRHED VLKGFRNSTA
LSNKHGVSLD PVSRNDEAHR VMSFLALDDP AHLRLRTLVS KGFTPRRIRE LEARVTEIAV
QHLEIALQSD SFDFVDDFAG KLPMDVISEL MGVPEEDRVR IRALADGVMH REDGVADVPA
SAIAASGELL VYYADMVKRR RRNVSDDLTS ALVEAEIDGD KLTDDEIMAF LFLMVVAGNE
TTTKLLANAA YWGFKNPDQL APVFDDHSQI PLWVEETLRY DTSSQILARA VVEDLTFYGT
TVPAGDVLVL LAGSANRDER AFDDPDEYRI GRDIGSKLVS FGSGAHFCLG AHLARMEARV
ALAELFKRIR GYDVDESASV RVHSSSVRGF AHLPITVEKR
//