CP144_MYCTO
ID CP144_MYCTO Reviewed; 434 AA.
AC P9WPL0; L0TAD0; O33180;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Cytochrome P450 144;
DE EC=1.14.-.-;
GN Name=cyp144; OrderedLocusNames=MT1827;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46097.1; -; Genomic_DNA.
DR PIR; B70511; B70511.
DR RefSeq; WP_003408772.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPL0; -.
DR SMR; P9WPL0; -.
DR BindingDB; P9WPL0; -.
DR EnsemblBacteria; AAK46097; AAK46097; MT1827.
DR KEGG; mtc:MT1827; -.
DR PATRIC; fig|83331.31.peg.1967; -.
DR HOGENOM; CLU_033716_0_2_11; -.
DR Proteomes; UP000001020; 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; IPR002397; Cyt_P450_B.
DR InterPro; IPR017972; Cyt_P450_CS.
DR InterPro; IPR036396; Cyt_P450_sf.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
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..434
FT /note="Cytochrome P450 144"
FT /id="PRO_0000426933"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 132
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 326
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 383
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 385
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 434 AA; 47219 MW; 030ECFE134BC050C CRC64;
MRRSPKGSPG AVLDLQRRVD QAVSADHAEL MTIAKDANTF FGAESVQDPY PLYERMRAAG
SVHRIANSDF YAVCGWDAVN EAIGRPEDFS SNLTATMTYT AEGTAKPFEM DPLGGPTHVL
ATADDPAHAV HRKLVLRHLA AKRIRVMEQF TVQAADRLWV DGMQDGCIEW MGAMANRLPM
MVVAELIGLP DPDIAQLVKW GYAATQLLEG LVENDQLVAA GVALMELSGY IFEQFDRAAA
DPRDNLLGEL ATACASGELD TLTAQVMMVT LFAAGGESTA ALLGSAVWIL ATRPDIQQQV
RANPELLGAF IEETLRYEPP FRGHYRHVRN ATTLDGTELP ADSHLLLLWG AANRDPAQFE
APGEFRLDRA GGKGHISFGK GAHFCVGAAL ARLEARIVLR LLLDRTSVIE AADVGGWLPS
ILVRRIERLE LAVQ