ID   CP128_MYCTU             Reviewed;         489 AA.
AC   P9WPN7; 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 41.
DE   RecName: Full=Putative cytochrome P450 128;
DE            EC=1.14.-.-;
GN   Name=cyp128; OrderedLocusNames=Rv2268c; ORFNames=MTCY339.42;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Vasilevskaya A.V., Alyapkina Y.S., Usanov S.A.;
RT   "Polymorphism of cytochrome P450 of drug resistant form of Mycobacterium
RT   tuberculosis.";
RL   Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
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; GQ900522; ACX47921.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP45049.1; -; Genomic_DNA.
DR   PIR; H70729; H70729.
DR   RefSeq; NP_216784.1; NC_000962.3.
DR   RefSeq; WP_003411663.1; NZ_NVQJ01000008.1.
DR   AlphaFoldDB; P9WPN7; -.
DR   SMR; P9WPN7; -.
DR   STRING; 83332.Rv2268c; -.
DR   PaxDb; P9WPN7; -.
DR   DNASU; 888025; -.
DR   GeneID; 888025; -.
DR   KEGG; mtu:Rv2268c; -.
DR   TubercuList; Rv2268c; -.
DR   eggNOG; COG2124; Bacteria.
DR   OMA; GRVHYNP; -.
DR   PhylomeDB; P9WPN7; -.
DR   BioCyc; MetaCyc:G185E-6485-MON; -.
DR   BRENDA; 1.14.15.27; 3445.
DR   Proteomes; UP000001584; 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:0036199; F:cholest-4-en-3-one 26-monooxygenase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0008395; F:steroid hydroxylase activity; IBA:GO_Central.
DR   GO; GO:0006707; P:cholesterol catabolic process; IBA:GO_Central.
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; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..489
FT                   /note="Putative cytochrome P450 128"
FT                   /id="PRO_0000052284"
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