C135B_MYCBO
ID C135B_MYCBO Reviewed; 472 AA.
AC P63716; A0A1R3XVR2; O53765; X2BFF0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Putative cytochrome P450 135B1;
DE EC=1.14.-.-;
GN Name=cyp135B1; OrderedLocusNames=BQ2027_MB0583;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; LT708304; SIT99179.1; -; Genomic_DNA.
DR RefSeq; NP_854243.1; NC_002945.3.
DR RefSeq; WP_003402992.1; NC_002945.4.
DR AlphaFoldDB; P63716; -.
DR SMR; P63716; -.
DR PATRIC; fig|233413.5.peg.631; -.
DR OMA; RDRMYAM; -.
DR Proteomes; UP000001419; 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 Gene3D; 1.10.630.10; -; 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 Pfam; PF00067; p450; 1.
DR PRINTS; PR00463; EP450I.
DR PRINTS; PR00385; P450.
DR SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT CHAIN 1..472
FT /note="Putative cytochrome P450 135B1"
FT /id="PRO_0000052294"
FT REGION 442..472
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 388
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:0000250"
SQ SEQUENCE 472 AA; 50688 MW; B7E2898BEE80863F CRC64;
MSGTSSMGLP PGPRLSGSVQ AVLMLRHGLR FLTACQRRYG SVFTLHVAGF GHMVYLSDPA
AIKTVFAGNP SVFHAGEANS MLAGLLGDSS LLLIDDDVHR DRRRLMSPPF HRDAVARQAG
PIAEIAAANI AGWPMAKAFA VAPKMSEITL EVILRTVIGA SDPVRLAALR KVMPRLLNVG
PWATLALANP SLLNNRLWSR LRRRIEEADA LLYAEIADRR ADPDLAARTD TLAMLVRAAD
EDGRTMTERE LRDQLITLLV AGHDTTATGL SWALERLTRH PVTLAKAVQA ADASAAGDPA
GDEYLDAVAK ETLRIRPVVY DVGRVLTEAV EVAGYRLPAG VMVVPAIGLV HASAQLYPDP
ERFDPDRMVG ATLSPTTWLP FGGGNRRCLG ATFAMVEMRV VLREILRRVE LSTTTTSGER
PKLKHVIMVP HRGARIRVRA TRDVSATSQA TAQGAGCPAA RGGGPSRAVG SQ