UniProt: A0A1G7F331

Database: UniProt
Entry: A0A1G7F331_9FLAO

LinkDB:  A0A1G7F331_9FLAO 
Original site:  A0A1G7F331_9FLAO

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (21)   

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ID   A0A1G7F331_9FLAO        Unreviewed;       495 AA.
AC   A0A1G7F331;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=SAMN05421544_1191 {ECO:0000313|EMBL:SDE70343.1};
OS   Riemerella columbipharyngis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Riemerella.
OX   NCBI_TaxID=1071918 {ECO:0000313|EMBL:SDE70343.1, ECO:0000313|Proteomes:UP000198517};
RN   [1] {ECO:0000313|EMBL:SDE70343.1, ECO:0000313|Proteomes:UP000198517}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24015 {ECO:0000313|EMBL:SDE70343.1,
RC   ECO:0000313|Proteomes:UP000198517};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNAS01000019; SDE70343.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7F331; -.
DR   STRING; 1071918.SAMN05421544_1191; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000198517; 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:SF9; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198517}.
FT   DOMAIN          7..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
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   495 AA;  57557 MW;  CB68AB682A13F544 CRC64;
     MNEKKITTAA GSPYYEHEDS QTVGPRGPVL LQDFVLQEKL AHFVRERIPE RIVHAKGTGA
     YGKFTVTHDI TKYTRAKIFS KIGNTCKIFT RFSTVGGEMG SADTERDPRG FAIKFYTEDG
     NWDLVGNNTP VFFIKDAKKF PDFIHTQKRH PRTHLKSHTM MWDFWSLNPE SLHQVLILMS
     DRGTPYGYRH MNGYGSHTFS MINDQNERVW VKFHFKTQQG IKNFNEAEAE EMKGKNPDFA
     QEDLVNAIEN GNFPKWTMYI QIMTEEQTNE FKWNPFDITK VWPHEEYPLI EVGEIELNEI
     PVNYFAHVEL STFSPSNLID GISFSPDKML QGRLFSYPDA QRYRVGVNAH QLEVNRCPFA
     VNNYHRDGAM ADSSRYQDSP NYYPNSFDNI KPDVAYKALE YDIDNNRVAH YDRNYDDNDH
     FTQPGLLYSK VMTEEEKTNL VNNIANHMKK IDGPKREQII NKQLCHFFRA HIELGIRIAT
     TLGVHIDMNS MHHDR
//

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