ID   BPOC_MYCTO              Reviewed;         262 AA.
AC   P9WNH0; 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 34.
DE   RecName: Full=Putative non-heme bromoperoxidase BpoC;
GN   Name=bpoC; OrderedLocusNames=MT0580;
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   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WNH1}.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44803.1; -; Genomic_DNA.
DR   PIR; E70548; E70548.
DR   RefSeq; WP_003402925.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNH0; -.
DR   SMR; P9WNH0; -.
DR   ESTHER; myctu-bpoC; 6_AlphaBeta_hydrolase.
DR   EnsemblBacteria; AAK44803; AAK44803; MT0580.
DR   GeneID; 45424518; -.
DR   KEGG; mtc:MT0580; -.
DR   PATRIC; fig|83331.31.peg.611; -.
DR   HOGENOM; CLU_020336_50_1_11; -.
DR   Proteomes; UP000001020; 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   3: Inferred from homology;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..262
FT                   /note="Putative non-heme bromoperoxidase BpoC"
FT                   /id="PRO_0000427128"
FT   ACT_SITE        87
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
FT   ACT_SITE        211
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
FT   ACT_SITE        239
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
FT   BINDING         21
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
FT   BINDING         87..88
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
FT   BINDING         120
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
FT   BINDING         239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P9WNH1"
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