ID A0A1A2U081_MYCSC Unreviewed; 492 AA.
AC A0A1A2U081;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Cytochrome P450 {ECO:0000313|EMBL:OBI08715.1};
GN ORFNames=A5679_09105 {ECO:0000313|EMBL:OBI08715.1};
OS Mycobacterium scrofulaceum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1783 {ECO:0000313|EMBL:OBI08715.1, ECO:0000313|Proteomes:UP000092207};
RN [1] {ECO:0000313|EMBL:OBI08715.1, ECO:0000313|Proteomes:UP000092207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2838 {ECO:0000313|EMBL:OBI08715.1,
RC ECO:0000313|Proteomes:UP000092207};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR602403-1};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family.
CC {ECO:0000256|ARBA:ARBA00010617, ECO:0000256|RuleBase:RU000461}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBI08715.1}.
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DR EMBL; LZJY01000063; OBI08715.1; -; Genomic_DNA.
DR RefSeq; WP_067274718.1; NZ_LZJY01000063.1.
DR AlphaFoldDB; A0A1A2U081; -.
DR OrthoDB; 9764248at2; -.
DR Proteomes; UP000092207; Unassembled WGS sequence.
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; cd11045; CYP136-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 1.
DR InterPro; IPR001128; Cyt_P450.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR002403; Cyt_P450_E_grp-IV.
DR InterPro; IPR036396; Cyt_P450_sf.
DR PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR PANTHER; PTHR24291:SF191; STEROL 14-DEMETHYLASE; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00465; EP450IV.
DR SUPFAM; SSF48264; Cytochrome P450; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|PIRSR:PIRSR602403-1, ECO:0000256|RuleBase:RU000461};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR602403-1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR602403-1};
KW Monooxygenase {ECO:0000256|RuleBase:RU000461};
KW Oxidoreductase {ECO:0000256|RuleBase:RU000461}.
FT BINDING 439
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000256|PIRSR:PIRSR602403-1"
SQ SEQUENCE 492 AA; 55909 MW; 3F6387F4A2DD44D9 CRC64;
MTATISTPQY LLDQARRRFT PTLNTIPGMG AVEKRLLAHD FETKVLAEPP AGSGLKPVVG
DAGLPILGHI IEMFRGGPDY ALHLYRTRGP LHYLDSPIMP AVTALGPDAT QAVFSNKNKD
FSQKGWHPVI GPFFNRGLMM LDFDEHMYHR RIMQEAFTRT RLTGYVEHID RVASDIVANW
PTNDARFLFH PAMKELTLDI ASLVFMGHEP GTDHELVTKV NQAFTITTRA GGAIIRQPIP
PFKWWRGLRA RKLLEDYFIE RVQERRHATG TDMLTVLCHT EDDDGNSFTD ADIVNHMIFL
MMAAHDTSTS TTTTMVYNMA ANPEWQERAR EESARLGDGP LDIEALEKLE TLELIMNESL
RMVTPLPFNM RQAVRDTELL GHYIPAGTNI TIWPGMNHRL PELWTDPDKF DPERFAEPRS
EHKKHRYAFA PFGGGAHKCI GMVFGQLEVK TVVHRLLRRY RLELARPGYQ PHWDYGGMPI
PMDGMPIVLR PL
//
