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Q9AP06 (KATG_BURCE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 50. 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
Synonyms:katA
OrganismBurkholderia cepacia (Pseudomonas cepacia)
Taxonomic identifier292 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiaBurkholderia cepacia complex

Protein attributes

Sequence length760 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Required for maintaining the normal activity of the TCA cycle. Ref.1

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
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 – 760760Catalase-peroxidase HAMAP MF_01961
PRO_0000354738

Sites

Active site921Proton acceptor By similarity
Metal binding2681Iron (heme axial ligand) By similarity
Site881Transition state stabilizer By similarity

Amino acid modifications

Cross-link91 ↔ 227Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-253) By similarity
Cross-link227 ↔ 253Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9AP06 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 5ECA94CF843676C4

FASTA76083,315
        10         20         30         40         50         60 
MSNEGQCPFN HANGGGTTNR DWWPNELRLD LLSQHSSKTD PLDPGFNYAE AFNSLDLDAL 

        70         80         90        100        110        120 
RKDLAALMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRMG DGRGGAGRGQ QRFAPLNSWP 

       130        140        150        160        170        180 
DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGDVALTTM GFKTFGYAGG REDTWEPDRD 

       190        200        210        220        230        240 
VYWGSETTWL GGDLRYDKGG ACESQHGGNA GRNLENPLAA VQMDLIYNPE GGPDGNPDPV 

       250        260        270        280        290        300 
AAAYDIREVF GRMAMNDEET VALIAGGHAF GKTHGAGPAD NVGLEPEAAG LEQQGLGWKN 

       310        320        330        340        350        360 
SFGTGKGADT ITSGLEVTWS DTPTQWGMGF FKNLFGYEWE LTKSPAGAHQ WVAKNAEPTI 

       370        380        390        400        410        420 
PHAHDPSKKL LPTMLTTDLS LRFDPVYEKI SRHFMDNPDV FADAFARAWF KLTHRDMGPR 

       430        440        450        460        470        480 
ARYLGPDVPT EELIWQDPIP AVDHVLTTRN VAPLKETILA SGLSVAELVS TAWASASTFR 

       490        500        510        520        530        540 
GSDKRGGANG ARIRLAPQKD WAVNEPARLA KVLKVLERIQ GEFNSTQPGG KKISLADLIV 

       550        560        570        580        590        600 
LAGGAGIEQA AKRAGHDVVV PFAPGRMDAS QEQTDAHSFA VLEPVADGFR NFVKGKFAVP 

       610        620        630        640        650        660 
AEALLIDKAQ LLTLTAPQMT ALVGGLRVLN VQTGDEKHGV FTDQPETLTV DFFRNLLDMA 

       670        680        690        700        710        720 
TEWKPIAGED TYEGRDRRTG ELKWTGTRVD LVFGSNAVLR ALSEVYASAD GEAKFIRDFV 

       730        740        750        760 
AAWVKVMNLD RFDLACKKRW YIDASGLPGE PALSARIQWR 

« Hide

References

[1]"A minor catalase/peroxidase from Burkholderia cenocepacia is required for normal aconitase activity."
Lefebre M.D., Flannagan R.S., Valvano M.A.
Microbiology 151:1975-1985(2005) [PubMed: 15942004] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
Strain: C5424.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF317697 Genomic DNA. Translation: AAG60688.1.

3D structure databases

HSSPHSSP built from PDB template 2CCA based on UniProtKB Q50555.
ProteinModelPortalQ9AP06.
SMRQ9AP06. Positions 16-735.
ModBaseSearch...

Protein family/group databases

PeroxiBase2323. BcCP01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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.
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_BURCE
AccessionPrimary (citable) accession number: Q9AP06
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 1, 2001
Last modified: October 19, 2011
This is version 50 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