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Q1R185 (KATG_CHRSD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase-peroxidase

Short name=CP
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase
Gene names
Name:katG
Ordered Locus Names:Csal_0159
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length717 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. HAMAP MF_01961

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity.

Subunit structure

Homodimer or homotetramer By similarity. HAMAP MF_01961

Post-translational modification

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

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

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 717717Catalase-peroxidase HAMAP MF_01961
PRO_0000354761

Sites

Active site921Proton acceptor By similarity
Metal binding2601Iron (heme axial ligand) By similarity
Site881Transition state stabilizer By similarity

Amino acid modifications

Cross-link91 ↔ 219Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-245) By similarity
Cross-link219 ↔ 245Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1R185 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 38EB720EB9D80F35

FASTA71780,005
        10         20         30         40         50         60 
MSGKCPVMHG GNTSTGTSNK DWWPEGINLD ILHQHDRKTN PMDPDFNYRE EVKKLDVQAL 

        70         80         90        100        110        120 
KNDLRQLMVD SQAWWPADWG SYVGMFARVA WHSAGSYRLA DGRGGGGTGN QRFAPLNSWP 

       130        140        150        160        170        180 
DNVNTDKGRR LLWPIKKKYG NKISWADLMV LSGTIAYEVA GLKTYGFAFG REDIWHPEKD 

       190        200        210        220        230        240 
IYWGDEKEWL APSDERYADV EKPDTMENPL AAVQMGLIYV NPEGVNGQPD PQKTAEQVRE 

       250        260        270        280        290        300 
TFARMAMNDE ETAALTAGGH TIGKCHGNGE AENLSAEPEA ADVEYQGIGW MNTKGRGIGR 

       310        320        330        340        350        360 
DTVVSGIEGA WTKNPTQWDM GWFDMLFNHE WELKKSPAGA WQWEPVDIAE EDMPVDVEDP 

       370        380        390        400        410        420 
SIRRMPIMTD ADMAMKVDPV YNEICRKFMD DPEYFSETFA KAWFKLTHRD LGPKARYIGP 

       430        440        450        460        470        480 
DVPADDLIWQ DPIPAGSIAY CEEVVKQKIA ESGLSIGEMV STAWDSARTY RGSDMRGGAN 

       490        500        510        520        530        540 
GARIRLAPQK TWPGNEPERL AKVLDVYERI SAETGASIAD VIVLGGSVGI ERAAKAAGHD 

       550        560        570        580        590        600 
VHVPFLKGRG DATDEMTDAA SFAPLEPLAD GFRNWQKQDY VVKPEEMLLD RAQLMGLTGP 

       610        620        630        640        650        660 
EMTVLIGGMR VLGTNHGGTR HGVFTDREGQ LTNDFFVNLT DMGNTWKPAG NNVYEIRDRE 

       670        680        690        700        710 
TDAVKWTASR VDLVFGSNSL LRSYAEVYAQ DDNEEKFVND FVAAWTKVMN ADRFDVA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000285 Genomic DNA. Translation: ABE57523.1.
RefSeqYP_572222.1. NC_007963.1.

3D structure databases

ProteinModelPortalQ1R185.
SMRQ1R185. Positions 18-716.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1R185.

Protein family/group databases

PeroxiBase2697. CsalCP01_DSM3043.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4026228.
GenomeReviewsGene locus Csal_0159 in contig CP000285_GR.
KEGGcsa:Csal_0159.
NMPDRfig|290398.4.peg.579.
PATRIC21444008. VBIChrSal113723_0163.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHBG285610.
OMAWPNALNL.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycCSAL290398:CSAL_0159-MONOMER.

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
[Tree]
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
KOK03782.
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
TIGRFAMsTIGR00198. Cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_CHRSD
AccessionPrimary (citable) accession number: Q1R185
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families