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Reviewed, UniProtKB/Swiss-Prot B1K6I9 (KATG2_BURCC)

Last modified February 9, 2010. Version 17. 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-peroxidase 2
      Short name=CP 2
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 2
Gene names
Name: katG2
Ordered Locus Names: Bcenmc03_5078
OrganismBurkholderia cenocepacia (strain MC0-3) [Complete proteome] [HAMAP]
Taxonomic identifier406425 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length728 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

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

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

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer By similarity. HAMAP MF_01961

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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: HAMAP

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 728728Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000354737

Sites

Active site921Proton acceptor By similarity
Metal binding2551Iron (heme axial ligand) By similarity
Site881Transition state stabilizer By similarity

Amino acid modifications

Cross-link91 ↔ 214Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-240) By similarity
Cross-link214 ↔ 240Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) By similarity

Sequences

Sequence LengthMass (Da)Tools
B1K6I9-1 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 24FBBA5BA38AAB9C

FASTA72879,926
        10         20         30         40         50         60 
MSNEGKCPFN HGKRNGTTNR DWWPNQLNLK ILHQHSSEAD PMDPGFDYAE AFNSLDLAAV 

        70         80         90        100        110        120 
KADLRALMTA SQDWWPADFG HYGPFFVRMA WHSAGTYRTG DGRGGAGRGQ QRFAPLNSWP 

       130        140        150        160        170        180 
DNVGLDKARR LIWPVKQKYG RKISWADLIV LTGNVALESM GFKTFGFAGG REDSWEPDED 

       190        200        210        220        230        240 
VYWGMESTWL DDKRYSGDRQ LETPLAAVQM GLIYVNPEGP NGNPDPLASA RDIRETFARM 

       250        260        270        280        290        300 
AMNDEETVAL IAGGHTFGKT HGAGDASHVG PEPEAAPLEQ MGLGWKSSFG SGKAGDAIGS 

       310        320        330        340        350        360 
GLEVIWTSTP TQWSNNFFWN LFGYDWELTK SPAGAHQWQP KGGAGADSVP DPFEPGKRRV 

       370        380        390        400        410        420 
PTMLTSDIAL RADPTYEKIS RRFFENPNEF AEAFARAWFK LTHRDMGPRV RYLGPEVPSE 

       430        440        450        460        470        480 
ELLWQDPIPM PDHPQVDEQD VSALKAKVLA SGLSVSELVS TAWASASTFR GSDKRGGANG 

       490        500        510        520        530        540 
ARVRLAPQKD WEVNQPAQLA TVLEVLGALQ VEFNRAATGG KQVSLADLIV IAGNAGVEQA 

       550        560        570        580        590        600 
AAAAGVEITV PFTPGRGDAS AEQTDVDSMA VLEPIADGFR NYLKGAYTIP AEKLLIDKAQ 

       610        620        630        640        650        660 
LLSLSAPEMT VLIGGLRVLG TNVGDSKHGV FTDRREVLTN DFFRNLLDMG TEWKPTSEAN 

       670        680        690        700        710        720 
EAYEGRDRAT GELKWLASRV DLVFGSHSQL RALSEVYGSE DSQQKFVRDF VAAWTKVMNA 


DRFDIKHN 

« Hide

References

[1]"Complete sequence of chromosome 2 of Burkholderia cenocepacia MC0-3."
Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Tiedje J., Richardson P.
Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000959 Genomic DNA. Translation: ACA94208.1.
RefSeqYP_001778698.1.

3D structure databases

SMRB1K6I9. Positions 15-725.
ModBaseSearch...

Genome annotation databases

GeneID6127890.
GenomeReviewsGene locus Bcenmc03_5078 in contig CP000959_GR.
KEGGbcm:Bcenmc03_5078.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG285610.
OMANGWANSV.

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]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
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 nameKATG2_BURCC
AccessionPrimary (citable) accession number: B1K6I9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: April 29, 2008
Last modified: February 9, 2010
This is version 17 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