ID   BCA_STRVP               Reviewed;         483 AA.
AC   P33569; F2R2M1;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Bromoperoxidase-catalase;
DE            EC=1.11.1.-;
GN   Name=bca; OrderedLocusNames=SVEN_4860;
OS   Streptomyces venezuelae (strain ATCC 10712 / CBS 650.69 / DSM 40230 / JCM
OS   4526 / NBRC 13096 / PD 04745).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=953739;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC   04745;
RX   PubMed=8868441; DOI=10.1099/13500872-142-3-657;
RA   Facey S., Gross F., Vining L.C., Yang K., van Pee K.-H.;
RT   "Cloning, sequencing and disruption of a bromoperoxidase-catalase gene in
RT   Streptomyces venezuelae: evidence that it is not required for chlorination
RT   in chloramphenicol biosynthesis.";
RL   Microbiology 142:657-665(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10712 / CBS 650.69 / DSM 40230 / JCM 4526 / NBRC 13096 / PD
RC   04745;
RX   PubMed=21463507; DOI=10.1186/1471-2164-12-175;
RA   Pullan S.T., Chandra G., Bibb M.J., Merrick M.;
RT   "Genome-wide analysis of the role of GlnR in Streptomyces venezuelae
RT   provides new insights into global nitrogen regulation in actinomycetes.";
RL   BMC Genomics 12:175-175(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10013};
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; X74791; CAA52796.1; -; Genomic_DNA.
DR   EMBL; FR845719; CCA58146.1; -; Genomic_DNA.
DR   PIR; S37055; S37055.
DR   RefSeq; WP_015036046.1; NZ_CP029197.1.
DR   AlphaFoldDB; P33569; -.
DR   SMR; P33569; -.
DR   STRING; 953739.SVEN_4860; -.
DR   PRIDE; P33569; -.
DR   EnsemblBacteria; CCA58146; CCA58146; SVEN_4860.
DR   KEGG; sve:SVEN_4860; -.
DR   PATRIC; fig|953739.5.peg.7372; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   OMA; ADHLPVN; -.
DR   Proteomes; UP000006854; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; PTHR11465; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Reference proteome.
FT   CHAIN           1..483
FT                   /note="Bromoperoxidase-catalase"
FT                   /id="PRO_0000085018"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         337
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   483 AA;  54088 MW;  B58CF8230B8A2F55 CRC64;
     MTQGPLTTEA GAPVADNQNS ETAGVGGPVL VQDQLLLEKL AHFNRERIPE RVVHARGAGA
     YGTFTLTRDV SRWTRAAFLS EVGKRTETFL RFSTVAGSLG AADAVRDPRG WALKFYTEEG
     NYDLVGNNTP VFFIKDAIKF PDFIHTQKRD PYTGSQEADN VWDFWGLSPE STHQVTWLFG
     DRGIPASYRH MNGYGSHTYQ WNNEAGEVFW VKYHFKTDQG IKNLTQDEAN RLAGEDPDSH
     QRDLREAIER GDFPTWTVQV QIMPAADAAG YRFNPFDLTK VWPHEDYPPV EIGTLELNRN
     PENIFAEVEQ SIFSPAHFVP GIGPSPDKML QGRLFAYGDA HRYRVGINAD HLPVNRPHAT
     EARTHSRDGF LYDGRHKGAK NYEPNSFGGP VQTDRPLWQP TPVTGVTGDH AAPSHAEDDD
     FTQAGDLYRL MSEDEKGRLI DNLSGFIAKV SRDDIAERAI GNFRRADEDF GKRLEAAVQA
     LRG