UniProt: A0A098U6I0

Database: UniProt
Entry: A0A098U6I0_9BURK

LinkDB:  A0A098U6I0_9BURK 
Original site:  A0A098U6I0_9BURK

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (22)   

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ID   A0A098U6I0_9BURK        Unreviewed;       481 AA.
AC   A0A098U6I0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=IA69_20015 {ECO:0000313|EMBL:KGF80109.1};
OS   Massilia sp. JS1662.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF80109.1, ECO:0000313|Proteomes:UP000029701};
RN   [1] {ECO:0000313|EMBL:KGF80109.1, ECO:0000313|Proteomes:UP000029701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS1662 {ECO:0000313|EMBL:KGF80109.1,
RC   ECO:0000313|Proteomes:UP000029701};
RA   Fida T.T., Spain J.C.;
RT   "Identification of Arachidin-3 degrading bacteria in the peanut
RT   rhizosphere.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGF80109.1}.
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DR   EMBL; JPQD01000023; KGF80109.1; -; Genomic_DNA.
DR   RefSeq; WP_036236742.1; NZ_JPQD01000023.1.
DR   AlphaFoldDB; A0A098U6I0; -.
DR   Proteomes; UP000029701; Unassembled WGS sequence.
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; 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: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; 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          6..390
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         336
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   481 AA;  54053 MW;  DD7A487069FE4645 CRC64;
     MGRELTTAAG APVADNQNVE TAGARGPMLL QDVWHLEKLA HFHREVIPER RMHAKGSGAY
     GRFVVTADIS RYTKAALFAR VGNECEVFAR FSTVAGERGA ADAERDIRGF ALKFYTSEGN
     WDIVGNNTPV FFLRDPLKFP DLNHAVKRDP QTNLRSPANN WDFWTLLPEA LHQVTIVMSE
     RGIPASYRHM HGFGSHTYSF INADNERTWV KFHFVCEQGI RNLTDAEAAA RIGADRDSAG
     RDLFDSIARG EHPRWVFKIQ VMTERQAADC PFNPFDLTKV WPHGDYPLID VGMLELNRNP
     ANYFAEVEQA AFTPANVVPG VSFSPDRMLQ SRLFAYGDAQ RYRLGVNHHH IPVNAPRCPV
     HSFHRDGAMR TDGNHGGTIG YEPNSLGEWR QQGAFAEPPL QVNGAATRWD HRQDDDYYSQ
     PRALFRLMDA AQRQHLFENT ARALQGVPAA IQQRHIRNCS QADEAYGLGV ASALETYRQG
     S
//

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