UniProt/TrEMBL: A0A071L4H2

Database: UniProt/TrEMBL
Entry: A0A071L4H2_PSEAI

LinkDB:  A0A071L4H2_PSEAI 
Original site:  A0A071L4H2_PSEAI

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Ontology (5)   
   GO (5)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (6)   
   EMBL (6)   
Protein domain (14)   
   InterPro (8)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (27)   

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ID   A0A071L4H2_PSEAI        Unreviewed;       482 AA.
AC   A0A071L4H2; A0A1S1C9J9;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katA {ECO:0000313|EMBL:CRP06613.1};
GN   ORFNames=CAZ10_34145 {ECO:0000313|EMBL:OTI55308.1}, DT376_00295
GN   {ECO:0000313|EMBL:RCI76856.1}, GNQ48_26550
GN   {ECO:0000313|EMBL:MUI38574.1}, GUL26_34385
GN   {ECO:0000313|EMBL:MZZ17359.1}, IPC1295_31500
GN   {ECO:0000313|EMBL:RPM03809.1}, PAERUG_P19_London_7_VIM_2_05_10_03326
GN   {ECO:0000313|EMBL:CRP06613.1};
OS   Pseudomonas aeruginosa.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=287 {ECO:0000313|EMBL:RCI76856.1, ECO:0000313|Proteomes:UP000253594};
RN   [1] {ECO:0000313|EMBL:CRP06613.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=P19_London_7_VIM_2_05_10 {ECO:0000313|EMBL:CRP06613.1};
RA   Radhakrishnan R., Underwood A., Al-Shahib A.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000045039}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P19_London_7_VIM_2_05_10 {ECO:0000313|Proteomes:UP000045039};
RA   Radhakrishnan Rajesh, Underwood Anthony, Al-Shahib Ali;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OTI55308.1, ECO:0000313|Proteomes:UP000194857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S567_C10_BS {ECO:0000313|EMBL:OTI55308.1,
RC   ECO:0000313|Proteomes:UP000194857};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:RPM03809.1, ECO:0000313|Proteomes:UP000284767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA-W36 {ECO:0000313|EMBL:RPM03809.1,
RC   ECO:0000313|Proteomes:UP000284767};
RA   Feschi L., Jeukens J., Emond-Rheault J.-G., Kukavica-Ibrulj I., Boyle B.,
RA   Levesque R.C.;
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN   [5] {ECO:0000313|EMBL:RCI76856.1, ECO:0000313|Proteomes:UP000253594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-305 {ECO:0000313|EMBL:RCI76856.1,
RC   ECO:0000313|Proteomes:UP000253594};
RA   Ballaben A.S., Darini A.L.C., Doi Y.;
RT   "Mechanisms of high-level aminoglycoside resistance among Gram-negative
RT   pathogens in Brazil.";
RL   Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EMBL:RPM03809.1, ECO:0000313|Proteomes:UP000284767}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA-W36 {ECO:0000313|EMBL:RPM03809.1,
RC   ECO:0000313|Proteomes:UP000284767};
RA   Freschi L., Vincent A.T., Jeukens J., Emond-Rheault J.-G.,
RA   Kukavica-Ibrulj I., Dupont M.-J., Charette S.J., Boyle B., Levesque R.C.;
RT   "The Pseudomonas aeruginosa pan-genome provides new insights on its
RT   population structure, horizontal gene transfer and pathogenicity.";
RL   Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN   [7] {ECO:0000313|EMBL:MUI38574.1, ECO:0000313|Proteomes:UP000433532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PA221 {ECO:0000313|EMBL:MUI38574.1,
RC   ECO:0000313|Proteomes:UP000433532};
RA   Khan M., Rice S.A., Willcox M.D.P., Stapleton F.;
RT   "Genomes of ocular Pseudomonas aeruginosa isolates.";
RL   Submitted (NOV-2019) to the EMBL/GenBank/DDBJ databases.
RN   [8] {ECO:0000313|EMBL:MZZ17359.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=VNMU148 {ECO:0000313|EMBL:MZZ17359.1};
RA   Snesrud E., Galac M.R., Mc Gann P., Valentine K., Viacheslav K.;
RT   "Bacteria Cultured from War Wounds Associated with the Conflict in Eastern
RT   Ukraine.";
RL   Submitted (JAN-2020) 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|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}.
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:RCI76856.1}.
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DR   EMBL; CVVU01000204; CRP06613.1; -; Genomic_DNA.
DR   EMBL; WOAD01000032; MUI38574.1; -; Genomic_DNA.
DR   EMBL; WXZT01000048; MZZ17359.1; -; Genomic_DNA.
DR   EMBL; NFFZ01000030; OTI55308.1; -; Genomic_DNA.
DR   EMBL; QORE01000002; RCI76856.1; -; Genomic_DNA.
DR   EMBL; NSNE01000031; RPM03809.1; -; Genomic_DNA.
DR   RefSeq; WP_003103909.1; NZ_WYAF01000033.1.
DR   OMA; KFRWNVF; -.
DR   Proteomes; UP000045039; Unassembled WGS sequence.
DR   Proteomes; UP000194857; Unassembled WGS sequence.
DR   Proteomes; UP000253594; Unassembled WGS sequence.
DR   Proteomes; UP000284767; Unassembled WGS sequence.
DR   Proteomes; UP000433532; Unassembled WGS sequence.
DR   Proteomes; UP000644192; 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          8..393
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        128
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         338
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   482 AA;  55589 MW;  84E5ABA647CAB414 CRC64;
     MEEKTRLTTA AGAPVVDNQN VQTAGPRGPM LLQDVWFLEK LAHFDREVIP ERRMHAKGSA
     AYGTFTVTHD ITPYTRAKIF SQVGKKTDMF LRFSTVAGER GAADAERDIR GFSMRFYTEQ
     GNWDLVGNNT PVFYLRDPLK FPDLNHVVKR DPRTNLRNAT FKWDFFSHLP ESLHQLTIDF
     SDRGLPKSYR HIHGFGSHTF SFINANNERF WVKFHFKTQQ GIENLTNAEA AEVIAQDRES
     SQRDLYESIE KGDFPRWKMY VQIMPEKEAA TYRYNPFDLT KVWPHGDYPL IEVGFFELNR
     NPDNYFAEVE QAAFTPANVV PGIGFSPDKM LQGRLFSYGD AHRYRLGVNH HQIPVNAARC
     PHQVYHRDGG MRVDGNNAHQ RVTYEPNSFN QWQEQPDFSE PPLSLEGAAD HWNHRVDDDY
     YSQPAALFHL FTDEQKQRLF ANIAEDIRDV PEQIQRRQIG LFLKVDPAYG KGVADALGLK
     LD
//

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