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BPOC_MYCTU
ID   BPOC_MYCTU              Reviewed;         262 AA.
AC   P9WNH1; L0T713; O06420; Q7D9N2;
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 non-heme bromoperoxidase BpoC;
GN   Name=bpoC; OrderedLocusNames=Rv0554;
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 [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.m111.011627;
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).
RN   [3] {ECO:0007744|PDB:3HZO}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 2-262 IN COMPLEX WITH SUBSTRATE
RP   ANALOGS, AND SUBUNIT.
RA   Johnston J.M., Baker E.N.;
RT   "The structure of Rv0554 from Mycobacterium tuberculosis.";
RL   Submitted (JUN-2009) to the PDB data bank.
RN   [4] {ECO:0007744|PDB:3E3A, ECO:0007744|PDB:3HSS, ECO:0007744|PDB:3HYS}
RP   X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 2-262 IN COMPLEX WITH SUBSTRATE
RP   ANALOGS, SUBUNIT, AND ACTIVE SITE.
RX   PubMed=20693690; DOI=10.1107/s0907444910025771;
RA   Johnston J.M., Jiang M., Guo Z., Baker E.N.;
RT   "Structural and functional analysis of Rv0554 from Mycobacterium
RT   tuberculosis: testing a putative role in menaquinone biosynthesis.";
RL   Acta Crystallogr. D 66:909-917(2010).
RN   [5] {ECO:0007744|PDB:7LD8}
RP   X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 2-262.
RA   DeBouver N.D., Dranow D.M., Lorimer D.D., Horanyi P.S., Edwards T.E.;
RT   "Crystal structure of putative non-heme bromoperoxidase BpoC from
RT   Mycobacterium tuberculosis H37Rv.";
RL   Submitted (JAN-2021) to the PDB data bank.
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20693690, ECO:0000269|Ref.3}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AL123456; CCP43292.1; -; Genomic_DNA.
DR   PIR; E70548; E70548.
DR   RefSeq; NP_215068.1; NC_000962.3.
DR   RefSeq; WP_003402925.1; NZ_NVQJ01000036.1.
DR   PDB; 3E3A; X-ray; 2.35 A; A/B=2-262.
DR   PDB; 3HSS; X-ray; 1.90 A; A/B=2-262.
DR   PDB; 3HYS; X-ray; 2.30 A; A/B=2-262.
DR   PDB; 3HZO; X-ray; 2.60 A; A/B=2-262.
DR   PDB; 7LD8; X-ray; 1.50 A; A=2-262.
DR   PDBsum; 3E3A; -.
DR   PDBsum; 3HSS; -.
DR   PDBsum; 3HYS; -.
DR   PDBsum; 3HZO; -.
DR   PDBsum; 7LD8; -.
DR   AlphaFoldDB; P9WNH1; -.
DR   SMR; P9WNH1; -.
DR   STRING; 83332.Rv0554; -.
DR   ESTHER; myctu-bpoC; 6_AlphaBeta_hydrolase.
DR   PaxDb; P9WNH1; -.
DR   DNASU; 887535; -.
DR   GeneID; 45424518; -.
DR   GeneID; 887535; -.
DR   KEGG; mtu:Rv0554; -.
DR   TubercuList; Rv0554; -.
DR   eggNOG; COG2267; Bacteria.
DR   OMA; DWIDMFT; -.
DR   PhylomeDB; P9WNH1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0019806; F:bromide peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR000639; Epox_hydrolase-like.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PRINTS; PR00111; ABHYDROLASE.
DR   PRINTS; PR00412; EPOXHYDRLASE.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..262
FT                   /note="Putative non-heme bromoperoxidase BpoC"
FT                   /id="PRO_0000414587"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000305|PubMed:20693690"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000305|PubMed:20693690"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000305|PubMed:20693690"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:20693690, ECO:0000305|Ref.3"
FT   BINDING         87..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:20693690, ECO:0000305|Ref.3"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:20693690, ECO:0000305|Ref.3"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:20693690, ECO:0000305|Ref.3"
FT   STRAND          6..18
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           25..28
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   TURN            29..32
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           33..38
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   STRAND          42..46
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           52..54
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           62..75
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   STRAND          80..86
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           88..99
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           101..103
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   STRAND          104..111
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           118..133
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           139..150
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           153..156
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           159..171
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           178..184
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           193..196
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   STRAND          203..208
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   STRAND          212..214
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           216..225
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           241..244
FT                   /evidence="ECO:0007829|PDB:7LD8"
FT   HELIX           246..259
FT                   /evidence="ECO:0007829|PDB:7LD8"
SQ   SEQUENCE   262 AA;  28381 MW;  26C4F811521EE0DD CRC64;
     MINLAYDDNG TGDPVVFIAG RGGAGRTWHP HQVPAFLAAG YRCITFDNRG IGATENAEGF
     TTQTMVADTA ALIETLDIAP ARVVGVSMGA FIAQELMVVA PELVSSAVLM ATRGRLDRAR
     QFFNKAEAEL YDSGVQLPPT YDARARLLEN FSRKTLNDDV AVGDWIAMFS MWPIKSTPGL
     RCQLDCAPQT NRLPAYRNIA APVLVIGFAD DVVTPPYLGR EVADALPNGR YLQIPDAGHL
     GFFERPEAVN TAMLKFFASV KA
 
 
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