ID A6UZL5_PSEA7 Unreviewed; 482 AA.
AC A6UZL5;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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:ABR85087.1};
GN OrderedLocusNames=PSPA7_0864 {ECO:0000313|EMBL:ABR85087.1};
OS Pseudomonas aeruginosa (strain PA7).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=381754 {ECO:0000313|EMBL:ABR85087.1, ECO:0000313|Proteomes:UP000001582};
RN [1] {ECO:0000313|EMBL:ABR85087.1, ECO:0000313|Proteomes:UP000001582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7 {ECO:0000313|EMBL:ABR85087.1,
RC ECO:0000313|Proteomes:UP000001582};
RA Dodson R.J., Harkins D., Paulsen I.T.;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABR85087.1, ECO:0000313|Proteomes:UP000001582}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PA7 {ECO:0000313|EMBL:ABR85087.1,
RC ECO:0000313|Proteomes:UP000001582};
RX PubMed=20107499; DOI=10.1371/journal.pone.0008842;
RA Roy P.H., Tetu S.G., Larouche A., Elbourne L., Tremblay S., Ren Q.,
RA Dodson R., Harkins D., Shay R., Watkins K., Mahamoud Y., Paulsen I.T.;
RT "Complete genome sequence of the multiresistant taxonomic outlier
RT Pseudomonas aeruginosa PA7.";
RL PLoS ONE 5:E8842-E8842(2010).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000744; ABR85087.1; -; Genomic_DNA.
DR RefSeq; WP_012074231.1; NC_009656.1.
DR AlphaFoldDB; A6UZL5; -.
DR GeneID; 77219225; -.
DR KEGG; pap:PSPA7_0864; -.
DR HOGENOM; CLU_010645_2_0_6; -.
DR Proteomes; UP000001582; 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; 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; 55600 MW; 1E20EB3A28C38D8D CRC64;
MEEKTRLTTA AGAPVVDNQN VQTAGPRGPM LLQDVWFLEK LAHFDREVIP ERRMHAKGSA
AYGTFTVTHD ITPYTRAKIF SQVGKKTDMF LRFSTVAGER GAADAERDIR GFSMRFYTEE
GNWDLVGNNT PVFYLRDPLK FPDLNHVVKR DPRTNLRNAT FKWDFFSHLP ESLHQLTIDF
SDRGLPKSYR HIHGFGSHTF SFINASNERF WVKFHLKTQQ GIENLTNAEA AEVIAQDRES
SQRDLYESIE KGDFPRWKMY VQIMPEKEAA TYRYNPFDLT KVWPHGDYPL IEVGFFELNR
NPDNYFAEVE QAAFTPANVV PGIGFSPDKM LQGRLFSYGD AHRYRLGVNH HQIPVNAARC
PHQVYHRDGG MRVDGNNAHQ RVSYEPNSFN QWQEQPDFSE PPLSLEGAAD HWNHRVDDDY
FSQPAALFRL FTDEQKQRLF DNIAEDIRDV PEQIQRRQIG LFHKIDPAYG KGVADALGLK
LD
//
