ID   CATA_BRUME              Reviewed;         499 AA.
AC   P0A326; Q59170;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=BMEII0893;
OS   Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=16M / ATCC 23456 / NCTC 10094;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL54135.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008918; AAL54135.1; ALT_INIT; Genomic_DNA.
DR   PIR; AD3621; AD3621.
DR   RefSeq; WP_002966234.1; NZ_GG703779.1.
DR   AlphaFoldDB; P0A326; -.
DR   SMR; P0A326; -.
DR   STRING; 224914.BMEII0893; -.
DR   EnsemblBacteria; AAL54135; AAL54135; BMEII0893.
DR   GeneID; 45125730; -.
DR   KEGG; bme:BMEII0893; -.
DR   PATRIC; fig|224914.52.peg.2468; -.
DR   eggNOG; COG0753; Bacteria.
DR   OMA; WTCYVQV; -.
DR   Proteomes; UP000000419; Chromosome II.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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; 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; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW   Peroxidase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..499
FT                   /note="Catalase"
FT                   /id="PRO_0000084981"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000250"
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   499 AA;  56446 MW;  8AC86DEC18F87648 CRC64;
     MTDRPIMTTS AGAPIPDNQN SLTAGERGPI LMQDYQLIEK LSHQNRERIP ERAVHAKGWG
     AYGTLTITGD ISRYTKAKVL QPGAQTPMLA RFSTVAGELG AADAERDVRG FALKFYTQEG
     NWDLVGNNTP VFFVRDPLKF PDFIHTQKRH PRTHLRSATA MWDFWSLSPE SLHQVTILMS
     DRGLPTDVRH INGYGSHTYS FWNDAGERYW VKFHFKTMQG HKHWTNAEAE QVIGRTREST
     QEDLFSAIEN GEFPKWKVQV QIMPELDADK TPYNPFDLTK VWPHADYPPI DIGVMELNRN
     PENYFTEVEN AAFSPSNIVP GIGFSPDKML QARIFSYADA HRHRLGTHYE SIPVNQPKCP
     VHHYHRDGQM NVYGGIKTGN PDAYYEPNSF NGPVEQPSAK EPPLCISGNA DRYNHRIGND
     DYSQPRALFN LFDAAQKQRL FSNIAAAMKG VPGFIVERQL GHFKLIHPEY EAGVRKALKD
     AHGYDANTIA LNEKITAAE