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Q8X1N3 (KATG_BLUGR) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 48. 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:CPX
OrganismBlumeria graminis
Taxonomic identifier34373 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaLeotiomycetesErysiphalesErysiphaceaeBlumeria

Protein attributes

Sequence length730 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

Donor + H2O2 = oxidized donor + 2 H2O.

2 H2O2 = O2 + 2 H2O.

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.

Sequence caution

The sequence AAL56991.1 differs from that shown. Reason: Erroneous initiation.

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 – 730730Catalase-peroxidase
PRO_0000354104

Sites

Active site931Proton acceptor By similarity
Metal binding2661Iron (heme axial ligand) By similarity
Site891Transition state stabilizer By similarity

Amino acid modifications

Cross-link92 ↔ 225Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-251) By similarity
Cross-link225 ↔ 251Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-92) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8X1N3 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 7C547BA50B90F4F7

FASTA73081,024
        10         20         30         40         50         60 
MGDSKCPYRD ANVAGGGTHN KDWWPETLKL DALRQHTAES NPLGKDFDYA SAFKTLDYEG 

        70         80         90        100        110        120 
LKKDLKDLMT DSQDWWPADF GHYGGFFVRM AWHSAGTYRS IDGRGGGGQG QHRFAPLNSW 

       130        140        150        160        170        180 
PDNGNLDKAR RLLWPIKQKY GNKISWADLY LLTGNVAIES MGGKTFGFAC GRPDTWEADD 

       190        200        210        220        230        240 
ATFWGNETKW LGNDARYKNG SKDPKDIYTR QLEKPLSAVH MGLIYVNPEG PDGIPDPVAS 

       250        260        270        280        290        300 
ARDIRTTFRR MAMNDEETVA LIAGGHTFGK THGAAPATHL GKEPEGAPIE AQGLGWANSY 

       310        320        330        340        350        360 
RSGKGPDTIT SGLEVIWTKT PINWSNHYLE YLFKYDWELT KSPGGANQWT AKNAEAFIPD 

       370        380        390        400        410        420 
AFDPNKKHPP RMLTTDLALR HDKEYEKISL RFLENPDQFA DAFARAWFKL LHRDMGPRSR 

       430        440        450        460        470        480 
WLGPEIPKEE LIWEDPIPEI DHPIISQEDI NNLKKEILSS GVGHNKLIQT AWASASTFRG 

       490        500        510        520        530        540 
GDKRGGANGA RIRLAPQKDW KVNNPPQLTC VLETLGKIQS SFNSSQTGGK IVSLADLIIL 

       550        560        570        580        590        600 
AGCAALEKAA GVPVPFSPGR ADASQEQTDI KSFSNLEPVA DGFRNFGRST PRARAEHMLV 

       610        620        630        640        650        660 
DRAQLLTLTP PELTALVGGL RVLDTNFDGS SCGVFTKRPG QLTNDFFVNL LDPAISWKGI 

       670        680        690        700        710        720 
DEDEFFEGID RKTDEKKWIG SRADLVFGSQ AELRAIAEVY GSADGNEKLI KDFIAAWNKV 

       730 
MNLDLFNLAH 

« Hide

References

[1]"Blumeria graminis catalase/peroxidase plays roles in scavenging activated oxygen species in oxidative burst during barley-powdery mildew interactions."
Zhang Z., Gurr S.J.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF329396 Genomic DNA. Translation: AAL56991.1. Different initiation.

3D structure databases

HSSPHSSP built from PDB template 1ITK based on UniProtKB O59651.
ModBaseSearch...

Protein family/group databases

PeroxiBase1960. BgCP.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

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_BLUGR
AccessionPrimary (citable) accession number: Q8X1N3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 25, 2008
Last modified: October 19, 2011
This is version 48 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families