UniProt: A0A090ICQ2

Database: UniProt
Entry: A0A090ICQ2_9GAMM

LinkDB:  A0A090ICQ2_9GAMM 
Original site:  A0A090ICQ2_9GAMM

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (24)   

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ID   A0A090ICQ2_9GAMM        Unreviewed;       483 AA.
AC   A0A090ICQ2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=catA {ECO:0000313|EMBL:CED59721.1};
GN   ORFNames=MVIS_1748 {ECO:0000313|EMBL:CED59721.1}, NVI5450_1316
GN   {ECO:0000313|EMBL:SGY92031.1};
OS   Moritella viscosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=80854 {ECO:0000313|EMBL:CED59721.1, ECO:0000313|Proteomes:UP000032438};
RN   [1] {ECO:0000313|Proteomes:UP000032438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Hjerde E.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CED59721.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Hjerde Erik;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SGY92031.1, ECO:0000313|Proteomes:UP000183794}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NVI 5450 {ECO:0000313|EMBL:SGY92031.1};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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|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; LN554852; CED59721.1; -; Genomic_DNA.
DR   EMBL; FPLD01000042; SGY92031.1; -; Genomic_DNA.
DR   RefSeq; WP_045110032.1; NZ_FRDV01000057.1.
DR   STRING; 80854.MVIS_1748; -.
DR   KEGG; mvs:MVIS_1748; -.
DR   PATRIC; fig|80854.5.peg.1861; -.
DR   HOGENOM; CLU_010645_2_0_6; -.
DR   OrthoDB; 9761719at2; -.
DR   Proteomes; UP000032438; Chromosome complete sequence.
DR   Proteomes; UP000183794; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032438}.
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   483 AA;  55133 MW;  B6D4F3635E35E873 CRC64;
     MSKKLTTAAG CPVAHNQNVQ TAGKRGPQLL QDVWFLEKLA HFDREVIPER RMHAKGSGAY
     GTFTVTHDIT RFTKAKIFSA IGKKTEMFTR FTTVAGERGA ADAERDIRGF AMKFYTEEGN
     WDLVGNNTPV FFLRDPLKFP DLNHAVKRDP RTNMRSAKNN WDFWTSLPEA LHQITIVMSD
     RGIPATYRHM HGFGSHTYSF INSDNERFWV KFHFKSQQGI KNLSDAESEI LIGKDRESHH
     RDLLESIDNR DFPKWTLQIQ IMPEDDASKV PYNPFDLTKI WPHSDYPLME VGEFELNRNP
     ENFFAEVEQS AFNPASVVPG ISFSPDKMLQ GRLFSYGDAQ RYRLGVNHHS IPVNAPRCPV
     HSYHRDGAMR VDGNYGGTLG YEPNDQGEWA EQPDFSEPPL SLDGAAAHWD HREDDDYFSQ
     PGDLFRLMTA EKQAILFDNT ARNLGGVPEE IQIRHLRHCF KADPDYGHGI AKLLGIDVSK
     YQN
//

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