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C0ZSW0 (KATG_RHOE4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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:RER_12250
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length740 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 – 740740Catalase-peroxidase HAMAP MF_01961
PRO_1000216226

Sites

Active site1101Proton acceptor By similarity
Metal binding2721Iron (heme axial ligand) By similarity
Site1061Transition state stabilizer By similarity

Amino acid modifications

Cross-link109 ↔ 231Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257) By similarity
Cross-link231 ↔ 257Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-109) By similarity

Sequences

Sequence LengthMass (Da)Tools
C0ZSW0 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 89718B33D8DBE547

FASTA74080,838
        10         20         30         40         50         60 
MSDSCPVAHD GNTASTSESE NPAIPSPTPT GNRPRTNRDW WPNQPDLSVL HAHSSKSNPM 

        70         80         90        100        110        120 
GADFDYAQEF AKLDVEALKR DVIALMTASQ DWWPADYGHY GGLFVRMSWH AAGTYRIADG 

       130        140        150        160        170        180 
RGGGGQGAQR FAPLNSWPDN ASLDKARRLL WPVKQKYGKQ VSWADLLVFA GNCALESMGF 

       190        200        210        220        230        240 
TTFGFGFGRE DIWEPEEIYW GPEDTWLGDE RYSGDRELSG PLGAVQMGLI YVNPEGPNGQ 

       250        260        270        280        290        300 
PDPVAAARDI RETFARMAMN DVETAALIAG GHTFGKTHGA GPADLVGPEP EGAPVEQQGL 

       310        320        330        340        350        360 
GWKSAFGTGV GKDAITSGLE VVWTPTPTKW DNTFLEILYG YDWELTKSPA GAWQWIPKDG 

       370        380        390        400        410        420 
AGAGTIPDPF DSSAGRTPTM LTTDLSLRLD PTYEKITRRW LDHPEEFAEE FAKAWYKLLH 

       430        440        450        460        470        480 
RDMGPVTRYL GPWVPEPQLW QDPVPSADDQ LIGDADIAIL KSRLLDSGLS VSQLVSTAWA 

       490        500        510        520        530        540 
SAASFRSTDM RGGANGARIR LEPQKNWEVN EPATLSAVLQ TLERVQQEFN QAGGAKVSLA 

       550        560        570        580        590        600 
DLIVLGGTAA VEQAAKNAGQ DITVSFTPGR TDATQEQTDV DSFEVLEPRA DGFRNYLKGG 

       610        620        630        640        650        660 
EKIPAEILLV DRAYMLSLTP PEVTVLVGGL RALNANFGKT GHGVFTDRPE TLTNDFFVNL 

       670        680        690        700        710        720 
LDMGTEWKPS KTEENVYDGV DRATGDPKYT ATAVDLVFGS NSQLRALSEV YASEDAKQKF 

       730        740 
AEDFAAAWTK VMDLDRFDVN 

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008957 Genomic DNA. Translation: BAH31933.1.
RefSeqYP_002764672.1. NC_012490.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC0ZSW0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7713139.
GenomeReviewsGene locus RER_12250 in contig AP008957_GR.
KEGGrer:RER_12250.
PATRIC23188774. VBIRhoEry66701_1689.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAKRHAPSM.
ProtClustDBPRK15061.

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
[Tree]
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[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. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_RHOE4
AccessionPrimary (citable) accession number: C0ZSW0
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: January 25, 2012
This is version 21 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