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Reviewed, UniProtKB/Swiss-Prot P0A323 (CATA_BORPE)

Last modified November 3, 2009. Version 29. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Catalase
    EC=1.11.1.6
Gene names
Name: katA
Ordered Locus Names: BP3852
OrganismBordetella pertussis [Complete proteome] [HAMAP]
Taxonomic identifier520 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482Catalase
PRO_0000084979

Sites

Active site571 By similarity
Active site1301 By similarity
Metal binding3401Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A323-1 [UniParc].

Last modified March 15, 2005. Version 1.
Checksum: 7CB73E08975C219F

FASTA48254,508
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.

Cross-references

Sequence databases

U07800 Unassigned DNA. Translation: AAA18481.1.
BX640422 Genomic DNA. Translation: CAE44107.1.
PIRS60757.
RefSeqNP_882347.1.

3D structure databases

HSSPHSSP built from PDB template 1M85 based on UniProtKB P42321.
ModBaseSearch...

Genome annotation databases

GeneID2664864.
GenomeReviewsGene locus BP3852 in contig BX470248_GR.
KEGGbpe:BP3852.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP0A323.
OMANIARHIN.

Enzyme and pathway databases

BioCycBPER257313:BP3852-MON.
BRENDA1.11.1.6. 21511.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_BORPE
AccessionPrimary (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: November 3, 2009
This is version 29 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents