ID   Q3JIV6_BURP1            Unreviewed;       708 AA.
AC   Q3JIV6;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 114.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE            EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN   Name=katE {ECO:0000313|EMBL:ABA52109.1};
GN   OrderedLocusNames=BURPS1710b_A1340 {ECO:0000313|EMBL:ABA52109.1};
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372 {ECO:0000313|EMBL:ABA52109.1, ECO:0000313|Proteomes:UP000002700};
RN   [1] {ECO:0000313|EMBL:ABA52109.1, ECO:0000313|Proteomes:UP000002700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b {ECO:0000313|EMBL:ABA52109.1,
RC   ECO:0000313|Proteomes:UP000002700};
RA   Woods D.E., Nierman W.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000256|ARBA:ARBA00010660}.
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DR   EMBL; CP000125; ABA52109.1; -; Genomic_DNA.
DR   RefSeq; WP_004529427.1; NC_007435.1.
DR   AlphaFoldDB; Q3JIV6; -.
DR   EnsemblBacteria; ABA52109; ABA52109; BURPS1710b_A1340.
DR   KEGG; bpm:BURPS1710b_A1340; -.
DR   HOGENOM; CLU_010645_3_0_4; -.
DR   Proteomes; UP000002700; Chromosome II.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; CATALASE; 1.
DR   PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRNR:PIRNR038927};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927}.
FT   DOMAIN          43..431
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..33
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        90
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        163
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         87
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         127
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         176
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         373
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         377
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:PIRSR038927-2"
FT   BINDING         384
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ   SEQUENCE   708 AA;  78332 MW;  7F7955E042421ED3 CRC64;
     MADSDRNAPH ETPRAAQPDD ARADRKSQDL EPYRSKPQGE ALRTNQGVRI ADDQNTLRAG
     ARGPSLLEDF IMREKITHFD HERIPERVVH ARGSAAHGVF RVYESMAEYT KAAFLQDPAK
     ETPVYVRFST VQGPRGSADT VRDVRGFAVK FYTDEGNYDL VGNNMPVFFI QDAIKFPDFV
     HAVKPEAPNE MPTGASAHDT FWDFVSLVPE SAHMVAWLMS DRAIPRSFRT MEGFGVHTFR
     FVNAQGVARF VKLHWRPVLG SYSLLWDEAQ KIAGHDPDFH RRDLWEAIER GDYPEYELGV
     QIIEARDQHA FGFDLLDPTK LIPEETVPVK LIGKMTLNRN PDNFFAETEQ VAFHPGHLVP
     GIDFTDDPLL QGRLFSYTDT QLSRLGGPNF HELPINRPVC PFANLQRDAM HRQTIDVGQA
     SYEPNSLNGG WPKETDPAGR DGGFDSYPEA VEGAKVRVRS GSFADHFSQA ALFYQSMSDV
     ERRHIRDAYR FELGKVTRPE IRARVVDEIL ARFDAGLAAE VAEGLGLPPP PTSAPAIVAQ
     PLSPALSLLT RGKRSVRSRK VALVATPGAD TRLIERVRRA LTDARAVPVL VAPTLARIGE
     LTPEATLAGM PSVMFDAVFV CGGDGDGRDL VHSSDARHFL QEAFKHLKAI AAVGSGRQLL
     GAAHLPEQGD GVCVGHAADL DQVVAKFFDA LSEHRVWSRE PLAQGVPA
//