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Database: UniProt
Entry: P9WPN3
LinkDB: P9WPN3
Original site: P9WPN3 
ID   CP132_MYCTU             Reviewed;         461 AA.
AC   P9WPN3; L0T9I0; P77900;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Putative cytochrome P450 132;
DE            EC=1.14.-.-;
GN   Name=cyp132; OrderedLocusNames=Rv1394c; ORFNames=MTCY21B4.11c;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
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).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; AL123456; CCP44153.1; -; Genomic_DNA.
DR   PIR; H70899; H70899.
DR   RefSeq; WP_003911514.1; NZ_NVQJ01000050.1.
DR   RefSeq; YP_177807.1; NC_000962.3.
DR   AlphaFoldDB; P9WPN3; -.
DR   SMR; P9WPN3; -.
DR   STRING; 83332.Rv1394c; -.
DR   PaxDb; 83332-Rv1394c; -.
DR   DNASU; 886738; -.
DR   GeneID; 886738; -.
DR   KEGG; mtu:Rv1394c; -.
DR   TubercuList; Rv1394c; -.
DR   eggNOG; COG2124; Bacteria.
DR   InParanoid; P9WPN3; -.
DR   OrthoDB; 7376058at2; -.
DR   PhylomeDB; P9WPN3; -.
DR   Proteomes; UP000001584; 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; IBA:GO_Central.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   CDD; cd20620; CYP132-like; 1.
DR   Gene3D; 1.10.630.10; Cytochrome P450; 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   PANTHER; PTHR24291:SF189; CYTOCHROME P450 4V2; 1.
DR   PANTHER; PTHR24291; CYTOCHROME P450 FAMILY 4; 1.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; Cytochrome P450; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..461
FT                   /note="Putative cytochrome P450 132"
FT                   /id="PRO_0000052287"
FT   BINDING         409
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   461 AA;  52229 MW;  2DEF61C8A10E0CF3 CRC64;
     MATATTQRPL KGPAKRMSTW TMTREAITIG FDAGDGFLGR LRGSDITRFR CAGRRFVSIS
     HPDYVDHVLH EARLKYVKSD EYGPIRATAG LNLLTDEGDS WARHRGALNS TFARRHLRGL
     VGLMIDPIAD VTAARVPGAQ FDMHQSMVET TLRVVANALF SQDFGPLVQS MHDLATRGLR
     RAEKLERLGL WGLMPRTVYD TLIWCIYSGV HLPPPLREMQ EITLTLDRAI NSVIDRRLAE
     PTNSADLLNV LLSADGGIWP RQRVRDEALT FMLAGHETTA NAMSWFWYLM ALNPQARDHM
     LTELDDVLGM RRPTADDLGK LAWTTACLQE SQRYFSSVWI IAREAVDDDI IDGHRIRRGT
     TVVIPIHHIH HDPRWWPDPD RFDPGRFLRC PTDRPRCAYL PFGGGRRICI GQSFALMEMV
     LMAAIMSQHF TFDLAPGYHV ELEATLTLRP KHGVHVIGRR R
//
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