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Database: UniProt/TrEMBL
Entry: A0A127Q5B2_9BURK
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ID   A0A127Q5B2_9BURK        Unreviewed;       494 AA.
AC   A0A127Q5B2;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=CPter91_2867 {ECO:0000313|EMBL:AMP05213.1};
OS   Collimonas pratensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Collimonas.
OX   NCBI_TaxID=279113 {ECO:0000313|EMBL:AMP05213.1, ECO:0000313|Proteomes:UP000074561};
RN   [1] {ECO:0000313|EMBL:AMP05213.1, ECO:0000313|Proteomes:UP000074561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ter91 {ECO:0000313|EMBL:AMP05213.1,
RC   ECO:0000313|Proteomes:UP000074561};
RA   Song C., Schmidt R., de Jager V., Krzyzanowska D., Jongedijk E., Cankar K.,
RA   Beekwilder J., van Veen A., de Boer W., van Veen J.A., Garbeva P.;
RT   "Exploring the genomic traits of fungus-feeding bacterial genus
RT   Collimonas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP013234; AMP05213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A127Q5B2; -.
DR   STRING; 279113.CPter91_2867; -.
DR   KEGG; cpra:CPter91_2867; -.
DR   PATRIC; fig|279113.9.peg.2831; -.
DR   Proteomes; UP000074561; Chromosome.
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; cd08154; catalase_clade_1; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
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; CATALASE; 1.
DR   PANTHER; PTHR11465:SF23; CATALASE-2; 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; PS00438; CATALASE_2; 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   ECO:0000256|RuleBase:RU000498};
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   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN          12..393
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..406
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        8..32
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        380..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         340
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   494 AA;  54809 MW;  436CBD40A1208E00 CRC64;
     MLAGAVSAQT MTRDSGAPVG DNQNSQTAGP GGPSLLQDAH LIEKLQRFDR ERIPERVVHA
     RGTGAIGEFV SAGNLLQLTR ASLFAEAGKK TRVFVRFSTV IHPKGSPETL RDPRGFATKF
     YTDQGNWDLV GNNLPVFFIR DAIKFPDMVH SLKPSPVTNV QDPNRFFDFF SHQPESTSML
     TRVYSDLGIP ASYRMMDGNG VHAYKMVNAQ NQVRYVKFHW KSLQGEKNLT RAEAARVQGE
     DFNNLTNDLY AAIKRGDFPK WDLYVQILKP EDLGKFKFDP LDATKIWPDI PETKIGTMTL
     NKVPDNFFES TEMVAFAPSR LVPGIEASED RLLQGRLFSY ADTQLHRLGP NNQLIPVNQP
     LVKVNNYNAD GAGDTGKRNG DVNYQPSRQS GSAVDDPAYK SVQTPLSGST QQAAIAKTDN
     FSQAGSFYRS LAKQDRENLV GNLAADLGQV KDAETKQIML SHFYKADVEY GTRLTAAVKG
     DLNDVQKRAQ KLIE
//
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