ID A0A0F6AVA0_BRUA1 Unreviewed; 499 AA.
AC A0A0F6AVA0;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ACD74278.1};
GN OrderedLocusNames=BAbS19_II07850 {ECO:0000313|EMBL:ACD74278.1};
OS Brucella abortus (strain S19).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=430066 {ECO:0000313|EMBL:ACD74278.1, ECO:0000313|Proteomes:UP000002565};
RN [1] {ECO:0000313|EMBL:ACD74278.1, ECO:0000313|Proteomes:UP000002565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S19 {ECO:0000313|EMBL:ACD74278.1,
RC ECO:0000313|Proteomes:UP000002565};
RX PubMed=18478107; DOI=10.1371/journal.pone.0002193;
RA Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S.,
RA Bricker B., Yu G., Du L., Sobral B.W.;
RT "Genome sequence of Brucella abortus vaccine strain S19 compared to
RT virulent strains yields candidate virulence genes.";
RL PLoS ONE 3:E2193-E2193(2008).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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 Evidence={ECO:0000256|ARBA:ARBA00000720};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|ARBA:ARBA00005329}.
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DR EMBL; CP000888; ACD74278.1; -; Genomic_DNA.
DR RefSeq; WP_002966234.1; NC_010740.1.
DR AlphaFoldDB; A0A0F6AVA0; -.
DR SMR; A0A0F6AVA0; -.
DR GeneID; 58777726; -.
DR KEGG; bmc:BAbS19_II07850; -.
DR HOGENOM; CLU_010645_4_1_5; -.
DR OMA; NPSWTCY; -.
DR Proteomes; UP000002565; Chromosome 2.
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 Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1.
DR PANTHER; PTHR11465:SF61; CATALASE; 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; Heme-dependent catalase-like; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038928-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559}.
FT DOMAIN 8..394
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 127
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:0000256|PIRSR:PIRSR038928-2"
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
//