CP128_MYCTO
ID CP128_MYCTO Reviewed; 489 AA.
AC P9WPN6; D0EW74; F2GJB1; P63713; Q59572;
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=Putative cytochrome P450 128;
DE EC=1.14.-.-;
GN Name=cyp128; OrderedLocusNames=MT2330;
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AE000516; AAK46612.1; -; Genomic_DNA.
DR PIR; H70729; H70729.
DR RefSeq; WP_003411663.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPN6; -.
DR SMR; P9WPN6; -.
DR EnsemblBacteria; AAK46612; AAK46612; MT2330.
DR KEGG; mtc:MT2330; -.
DR PATRIC; fig|83331.31.peg.2505; -.
DR HOGENOM; CLU_033716_0_2_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 3: Inferred from homology;
KW Cell membrane; Heme; Iron; Membrane; Metal-binding; Monooxygenase;
KW Oxidoreductase; Transmembrane; Transmembrane helix.
FT CHAIN 1..489
FT /note="Putative cytochrome P450 128"
FT /id="PRO_0000426920"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 315..335
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 383..403
FT /note="Helical"
FT /evidence="ECO:0000255"
FT BINDING 435
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 489 AA; 53313 MW; 633F233CEF03AD7A CRC64;
MTATQSPPEP APDRVRLAGC PLAGTPDVGL TAQDATTALG VPTRRRASSG GIPVATSMWR
DAQTVRTYGP AVAKALALRV AGKARSRLTG RHCRKFMQLT DFDPFDPAIA ADPYPHYREL
LAGERVQYNP KRDVYILSRY ADVREAARNH DTLSSARGVT FSRGWLPFLP TSDPPAHTRM
RKQLAPGMAR GALETWRPMV DQLARELVGG LLTQTPADVV STVAAPMPMR AITSVLGVDG
PDEAAFCRLS NQAVRITDVA LSASGLISLV QGFAGFRRLR ALFTHRRDNG LLRECTVLGK
LATHAEQGRL SDDELFFFAV LLLVAGYEST AHMISTLFLT LADYPDQLTL LAQQPDLIPS
AIEEHLRFIS PIQNICRTTR VDYSVGQAVI PAGSLVLLAW GAANRDPRQY EDPDVFRADR
NPVGHLAFGS GIHLCPGTQL ARMEGQAILR EIVANIDRIE VVEPPTWTTN ANLRGLTRLR
VAVTPRVAP