P0A323 (CATA_BORPE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:	katA
Ordered Locus Names:	BP3852

Organism

Bordetella pertussis

Taxonomic identifier

520 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

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. Ref.1
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group By similarity.
Subunit structure	Homodimer By similarity.
Miscellaneous	Essential for protection against exogenous H2O2; however its absence does not affect survival of B.pertussis within human polymorphonuclear leukocytes.
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 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_0000084979
Sites
	Active site	57	1	By similarity
	Active site	130	1	By similarity
	Metal binding	340	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A323 [UniParc]. Last modified March 15, 2005. Version 1. Checksum: 7CB73E08975C219F	FASTA	482	54,508
	10 20 30 40 50 60 MNAMTNKTLT TAAGAPVADN NNTMTAGPRG PALLQDVWFL EKLAHFDRER IPERVVHAKG 70 80 90 100 110 120 SGAYGTFTVT HDISRYTRAR IFAEVGKQTP LFLRFSTVAG ERGAADAERD VRGFAIKFYT 130 140 150 160 170 180 DEGNWDLVGN NTPVFFIRDP LKFPDFIHTQ KRDPKTNLRN ATAAWDFWSL NPESLHQVTI 190 200 210 220 230 240 LMSDRGLPQN YRQQHGFGSH TYSFVNDAGE RFYVKFHFKS QQGIACYTDG EAAELVGRDR 250 260 270 280 290 300 ESAQRDLFQN IEQGQFPRWT LKVQVMPEAE AATYHINPFD LTKVWPHADY PLIEVGVLEL 310 320 330 340 350 360 NKNPENYFAE VEQAAFTPAN VVPGIGFSPD KMLQGRLFSY GDTHRYRLGI NHHQIPVNAP 370 380 390 400 410 420 RCPFHSFHRD GMGRVDGNGG ATLNYEPNSF GEWREAKHAA EPPLALDGQA ADRWNHRVDE 430 440 450 460 470 480 DYYSQPGALF RLMNDDQKQQ LFGNIGRHMA GVPEEIQRRQ LEHFRRADPA YAAGVAKALG LK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular characterization of catalase from Bordetella pertussis: identification of the katA promoter in an upstream insertion sequence." DeShazer D., Wood G.E., Friedman R.L. Mol. Microbiol. 14:123-130(1994) [PubMed: 7830550] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION OF ITS ROLE IN SURVIVAL IN HUMAN POLYMORPHONUCLEAR LEUKOCYTES. Strain: BP504.
[2]	"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica." Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J. Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tohama I / ATCC BAA-589 / NCTC 13251.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U07800 Unassigned DNA. Translation: AAA18481.1. BX640422 Genomic DNA. Translation: CAE44107.1.
PIR	S60757.
RefSeq	NP_882347.1. NC_002929.2.
3D structure databases
ProteinModelPortal	P0A323.
SMR	P0A323. Positions 6-481.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	2664864.
GenomeReviews	Gene locus BP3852 in contig BX470248_GR.
KEGG	bpe:BP3852.
PATRIC	21161396. VBIBorPer7866_4162.
Phylogenomic databases
HOGENOM	HBG339355.
OMA	RDPYKFP.
PhylomeDB	P0A323.
ProtClustDB	CLSK524242.
Enzyme and pathway databases
BioCyc	BPER257313:BP3852-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_BORPE

Accession

Primary (citable) accession number: P0A323
Secondary accession number(s): P48062

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 15, 2005
Last sequence update:	March 15, 2005
Last modified:	January 25, 2012
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program