O52762 (CATA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:	katA
Ordered Locus Names:	PA4236

Organism

Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)

Taxonomic identifier

208964 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas

Protein attributes

Sequence length	482 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group.
Enzyme regulation	By peroxide and bfr-bound iron.
Subunit structure	Heteromultimer. Possibly an alpha2beta-heterotrimer where the alpha subunit is a 56 kDa protein and the beta subunit a 45 kDa protein.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 482	482	Catalase		PRO_0000084994
Sites
	Active site	55	1	By similarity
	Active site	128	1	By similarity
	Metal binding	338	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O52762 [UniParc]. Last modified June 1, 1998. Version 1. Checksum: 84E5ABA647CAB414	FASTA	482	55,589
	10 20 30 40 50 60 MEEKTRLTTA AGAPVVDNQN VQTAGPRGPM LLQDVWFLEK LAHFDREVIP ERRMHAKGSA 70 80 90 100 110 120 AYGTFTVTHD ITPYTRAKIF SQVGKKTDMF LRFSTVAGER GAADAERDIR GFSMRFYTEQ 130 140 150 160 170 180 GNWDLVGNNT PVFYLRDPLK FPDLNHVVKR DPRTNLRNAT FKWDFFSHLP ESLHQLTIDF 190 200 210 220 230 240 SDRGLPKSYR HIHGFGSHTF SFINANNERF WVKFHFKTQQ GIENLTNAEA AEVIAQDRES 250 260 270 280 290 300 SQRDLYESIE KGDFPRWKMY VQIMPEKEAA TYRYNPFDLT KVWPHGDYPL IEVGFFELNR 310 320 330 340 350 360 NPDNYFAEVE QAAFTPANVV PGIGFSPDKM LQGRLFSYGD AHRYRLGVNH HQIPVNAARC 370 380 390 400 410 420 PHQVYHRDGG MRVDGNNAHQ RVTYEPNSFN QWQEQPDFSE PPLSLEGAAD HWNHRVDDDY 430 440 450 460 470 480 YSQPAALFHL FTDEQKQRLF ANIAEDIRDV PEQIQRRQIG LFLKVDPAYG KGVADALGLK LD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Bacterioferritin A modulates catalase A (KatA) activity and resistance to hydrogen peroxide in Pseudomonas aeruginosa." Ma J.-F., Ochsner U.A., Klotz M.G., Nanayakkara V.K., Howell M.L., Johnson Z., Posey J.E., Vasil M.L., Monaco J.J., Hassett D.J. J. Bacteriol. 181:3730-3742(1999) [PubMed: 10368148] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: FRD1.
[2]	"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen." Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V. Nature 406:959-964(2000) [PubMed: 10984043] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[3]	"Biofouling in water treatment systems: effect of membrane properties on biofilm formation." Liddor M. Thesis (2005), Ben-Gurion University, Israel Cited for: PROTEIN SEQUENCE OF 7-27 AND 218-238. Strain: ATCC 33467 / type 1 smooth and ATCC 33468 / type 2 mucoid.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF047025 Genomic DNA. Translation: AAC03118.1. AE004091 Genomic DNA. Translation: AAG07624.1.
PIR	B83113.
RefSeq	NP_252926.1. NC_002516.2.
3D structure databases
ProteinModelPortal	O52762.
SMR	O52762. Positions 6-477.
ModBase	Search...
Proteomic databases
PRIDE	O52762.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	881831.
GenomeReviews	Gene locus PA4236 in contig AE004091_GR.
KEGG	pae:PA4236.
PATRIC	19843163. VBIPseAer58763_4437.
Organism-specific databases
PseudoCAP	PA4236.
Phylogenomic databases
HOGENOM	HBG339355.
OMA	HSYHRDG.
ProtClustDB	CLSK868543.
Enzyme and pathway databases
BioCyc	PAER208964:PA4236-MONOMER.
Family and domain databases
InterPro	IPR018028. Catalase. IPR020835. Catalase-like_dom. IPR024708. Catalase_AS. IPR024711. Catalase_clade1/3. IPR011614. Catalase_core. IPR002226. Catalase_haem_BS. IPR010582. Catalase_immune_responsive. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
KO	K03781.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_PSEAE

Accession

Primary (citable) accession number: O52762

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	June 1, 1998
Last modified:	January 25, 2012
This is version 75 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program