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Reviewed, UniProtKB/Swiss-Prot Q1BQP0 (KATG2_BURCA)

Last modified June 16, 2009. Version 25. 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: Bcen_3169
OrganismBurkholderia cenocepacia (strain AU 1054) [Complete proteome] [HAMAP]
Taxonomic identifier331271 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length728 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

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

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.

Subunit structure

Homodimer or homotetramer By similarity.

Post-translational modification

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

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_0000354733

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
Q1BQP0-1 [UniParc].

Last modified July 11, 2006. 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 AU 1054."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Lykidis A., LiPuma J.J., Konstantinidis K., Tiedje J.M., Richardson P.
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000379 Genomic DNA. Translation: ABF78065.1.
RefSeqYP_623038.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4095370.
GenomeReviewsGene locus Bcen_3169 in contig CP000379_GR.
KEGGbcn:Bcen_3169.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1BQP0.
OMAQ1BQP0. NGWANSV.

Enzyme and pathway databases

BioCycBCEN331271:BCEN_3169-MON.

Family and domain databases

HAMAPMF_01961.
[Tree]
InterProIPR000763. Catalase_proxase.
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_BURCA
AccessionPrimary (citable) accession number: Q1BQP0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: July 11, 2006
Last modified: June 16, 2009
This is version 25 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