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Reviewed, UniProtKB/Swiss-Prot Q9ZKX5 (CATA_HELPJ)

Last modified June 16, 2009. Version 58. 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: jhp_0809
OrganismHelicobacter pylori J99 (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesHelicobacteraceaeHelicobacter

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

Subcellular location

Cytoplasm Probable.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   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

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 505505Catalase
PRO_0000084988

Sites

Active site561 By similarity
Active site1291 By similarity
Metal binding3391Iron (heme axial ligand) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZKX5-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 475A07EF6EF9B309

FASTA50558,527
        10         20         30         40         50         60 
MVNKDVKQTT AFGAPVWDDN NVITAGPRGP VLLQSTWFLE KLAAFDRERI PERVVHAKGS 

        70         80         90        100        110        120 
GAYGTFTVTK DITKYTKAKI FSKVGKKTEC FFRFSTVAGE KGSADAVRDP RGFAMKYYTE 

       130        140        150        160        170        180 
EGNWDLVGNN TPVFFIRDAI KFPDFIHTQK RDPQTNLPNP DMVWDFWSNV PESLYQVTWV 

       190        200        210        220        230        240 
MSDRGIPKSF RHMDGFGSHT FSLINAKGER FWVKFHFETM QGVKHLTNEE AAEVRKYDPD 

       250        260        270        280        290        300 
SNQRDLFDAI AGGDFPKWKM SIQVMPEEDA KKYRFHPFDV TKIWYLQDYP LMEVGIVELN 

       310        320        330        340        350        360 
KNPENYFAEV EQAAFTPANV VPGIGYSPDR MLQGRLFSYG DTHRYRLGVN YPQIPVNRPR 

       370        380        390        400        410        420 
CPFHSSSRDG YMQNGYYGSL QNYTPSSLPG YKEDKSARDP KFNLAHIEKE FEVWNWDYRA 

       430        440        450        460        470        480 
EDSDYYTQPG DYYRSLPADE KERLYDTIGG SLAHVTHKEI VDKQLEHFKK ADPKYAEGVK 

       490        500 
KALEKHQKMM KDMHAKDMHH MKKKK 

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed: 9923682] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AE001439 Genomic DNA. Translation: AAD06391.1.
PIRF71885.
RefSeqNP_223527.1.

3D structure databases

HSSPHSSP built from PDB template 2CAG based on UniProtKB P42321.
SMRQ9ZKX5. Positions 1-491.
ModBaseSearch...

Proteomic databases

PRIDEQ9ZKX5.

Genome annotation databases

GeneID890086.
GenomeReviewsGene locus jhp_0809 in contig AE001439_GR.
KEGGhpj:jhp0809.
NMPDRfig|85963.1.peg.805.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9ZKX5.
OMAQ9ZKX5. NCPFRAR.

Enzyme and pathway databases

BioCycHPYL85963:JHP0809-MON.
BRENDA1.11.1.6. 295085.

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_HELPJ
AccessionPrimary (citable) accession number: Q9ZKX5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 58 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