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Reviewed, UniProtKB/Swiss-Prot Q0CD12 (KATG_ASPTN)

Last modified February 9, 2010. Version 23. 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
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase
Gene names
Name: katG
ORF Names: ATEG_08422
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length737 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

2 H2O2 = O2 + 2 H2O.

Donor + H2O2 = oxidized donor + 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.

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: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 737737Catalase-peroxidase
PRO_0000354103

Sites

Active site901Proton acceptor By similarity
Metal binding2601Iron (heme axial ligand) By similarity
Site861Transition state stabilizer By similarity

Amino acid modifications

Cross-link89 ↔ 219Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-245) By similarity
Cross-link219 ↔ 245Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-89) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CD12-1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 59F5B80D7B3F9425

FASTA73781,333
        10         20         30         40         50         60 
MGESKCPVNF AGGGTRNKDW WPDQLRLNIL RQHTSASNPL DADFDYAAAF NSLDYNALKK 

        70         80         90        100        110        120 
DLEALMTDSQ DWWPADFGHY GGLFIRMAWH SAGTYRVFDG RGGAGQGQQR FAPLNSWPDN 

       130        140        150        160        170        180 
ASLDKARRLL WPIKQKYGNK ISWADLMILA GNVALESMGF KPFGFSGGRA DTWEADESVY 

       190        200        210        220        230        240 
WGGEKTWFPK GNDVRYPNDD IYTRDLENPL AASHMGLIYV NPEGPNGNPD PKAAARDIRV 

       250        260        270        280        290        300 
TFGRMAMNDE ETVALIAGGH SFGKTHGASS GDHCGPEPEA AGLEAQGLGW QSKYGSGSGR 

       310        320        330        340        350        360 
DAITSGLEVT WTKTPTRWST NFLEYLFAFD WELTKSPAGA NQWVAKNADA IIPDAFDPSK 

       370        380        390        400        410        420 
KHKPQMLTTD LALRYDPAYE KIARRFLENP DQFADAFARA WFKLTHRDMG PRARYVGPEV 

       430        440        450        460        470        480 
PSEVLIWQDP IPAVNHPLVD ASDIASLKQA ILNSGVDRSK FVSTAWAAAS TFRGGDKRGG 

       490        500        510        520        530        540 
ANGARIRLAP QRDWEVNNQP WLKESLAALE KIQSSFNGSR SDRKKISLAD LIVLAGCAAV 

       550        560        570        580        590        600 
ESAAQEAGHA VSVPFTPGRM DASQEETDVE SFSHMEPVAD GFRNYSTAPT RRRAEHYLVD 

       610        620        630        640        650        660 
KAQMLTLSAP EMTALVGGLR ALNANYDGSA HGVFTSRPGY LTNDFFVNLL DMGTTWKPTD 

       670        680        690        700        710        720 
ASGELYEGAD RRTGSKKWTA TRVDLVFGSH AELRAIAEVY GSSDGERKFV KDFVAAWNKV 

       730 
MNLDRFDLKR ENVPARL 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476605 Genomic DNA. Translation: EAU31595.1.
RefSeqXP_001217043.1.

3D structure databases

SMRQ0CD12. Positions 14-728.
ModBaseSearch...

Protein family/group databases

PeroxiBase3413. AteCP01.

Genome annotation databases

GeneID4353293.

Phylogenomic databases

OrthoDBEOG9CVHR8.

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.
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_ASPTN
AccessionPrimary (citable) accession number: Q0CD12
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: October 17, 2006
Last modified: February 9, 2010
This is version 23 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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