ID   CATA_BRUAB              Reviewed;         499 AA.
AC   P0A327; Q577G4; Q59170;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 31.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=BruAb2_0827;
OS   Brucella abortus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Brucellaceae; Brucella.
OX   NCBI_TaxID=235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RC   STRAIN=19;
RX   MEDLINE=95050323; PubMed=7961511;
RA   Sha Z., Stabel T.J., Mayfield J.E.;
RT   "Brucella abortus catalase is a periplasmic protein lacking a standard
RT   signal sequence.";
RL   J. Bacteriol. 176:7375-7377(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941 / Biovar 1;
RX   PubMed=15805518; DOI=10.1128/JB.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L.,
RA   Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison
RT   to the highly similar genomes of Brucella melitensis and Brucella
RT   suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
CC       serves to protect cells from the toxic effects of hydrogen
CC       peroxide.
CC   -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC   -!- COFACTOR: Heme group.
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the catalase family.
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DR   EMBL; U11439; AAA64655.1; -; Genomic_DNA.
DR   EMBL; AE017224; AAX76220.1; -; Genomic_DNA.
DR   PIR; A55227; A55227.
DR   RefSeq; YP_223581.1; -.
DR   HSSP; P42321; 1M85.
DR   GeneID; 3341589; -.
DR   GenomeReviews; AE017224_GR; BruAb2_0827.
DR   KEGG; bmb:BruAb2_0827; -.
DR   HOGENOM; P0A327; -.
DR   OMA; P0A327; TQKRHPK.
DR   BioCyc; BABO262698:BRUAB2_0827-MON; -.
DR   BRENDA; 1.11.1.6; 575.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002226; Catalase.
DR   InterPro; IPR010582; Catalase-rel_immune_responsive.
DR   InterPro; IPR011614; Catalase_N.
DR   InterPro; IPR018028; Catalase_rel_subgroup.
DR   Gene3D; G3DSA:2.40.180.10; Catalase_N; 1.
DR   PANTHER; PTHR11465; Catalase; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PRINTS; PR00067; CATALASE.
DR   ProDom; PD000510; Catalase; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; FALSE_NEG.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide;
KW   Iron; Metal-binding; Oxidoreductase; Periplasm; Peroxidase.
FT   INIT_MET      1      1       Removed.
FT   CHAIN         2    499       Catalase.
FT                                /FTId=PRO_0000084980.
FT   ACT_SITE     55     55       By similarity.
FT   ACT_SITE    127    127       By similarity.
FT   METAL       337    337       Iron (heme axial ligand) (By similarity).
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
//