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Q8TS34 (KATG_METAC) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 64. 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
Ordered Locus Names:MA_0972
OrganismMethanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Taxonomic identifier188937 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina

Protein attributes

Sequence length736 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

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
   Technical termComplete proteome
Reference proteome
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 – 736736Catalase-peroxidase HAMAP MF_01961
PRO_0000354968

Sites

Active site1021Proton acceptor By similarity
Metal binding2651Iron (heme axial ligand) By similarity
Site981Transition state stabilizer By similarity

Amino acid modifications

Cross-link101 ↔ 224Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-250) By similarity
Cross-link224 ↔ 250Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-101) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TS34 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 67A0508CD91BFA7A

FASTA73681,051
        10         20         30         40         50         60 
MGGNVMTDDK MNSVTSGANK QETGRDMSNR DWWPNHLKLE ILHQHSSKSN PMGEDFNYAK 

        70         80         90        100        110        120 
EFKSLDLAAV KKDLAALMTD SQDWWPADFG HYGPLFIRMA WHSAGTYRAG DGRGGGGRGQ 

       130        140        150        160        170        180 
QRFAPLNSWP DNVNLDKARR LLWPIKQKYG RKISWADLMI LTGNVAMETM GFKTFGFGGG 

       190        200        210        220        230        240 
REDVWEPDQD VYWGSEDTWL GDERYTGDRD LENPLAAVQM GLIYVNPEGP NGNPDPIAAA 

       250        260        270        280        290        300 
KDIREVFARM AMNDEETVAL IAGGHAFGKT HGAGPASHVG PEPEAASIEA QGLGWKSSFG 

       310        320        330        340        350        360 
TGKGDDTITG GLEVTWTNTP TKWSNNFFRI LFGYEWELTK SPAGAYQWKP KGGAGAGTIP 

       370        380        390        400        410        420 
DAHDPSKRHA PSMMTTDLSL RFDPVYEKIS RHFYENPGQL ADSFARAWFK LTHRDMGPRA 

       430        440        450        460        470        480 
RYLGPEVPAE ELIWQDPIPA VNHELIDEKD IAFLKDRILA SGLSISQLVS TAWVSASTFR 

       490        500        510        520        530        540 
GSDKRGGANG ARIRLAPQKD WEVNQPAELA KVLNTLEGIQ SEFNSAASGG KKVSLADLIV 

       550        560        570        580        590        600 
LAGCAGVEQA AKNAGYDVTV PFLPGRMDAL QEQTDVVSFA LLEPIADGFR NYLKAQYPLP 

       610        620        630        640        650        660 
AEELLVDKAQ LLTLTAPEMT VLVGGMRVLN TNFGHTQHGV FTQKPEALTN DFFVNLLDMG 

       670        680        690        700        710        720 
TEWKAVSDVK DIFEGCDRKT GEVKWTGTRV DLIFGSNSQL RALAEVYGSA DAQEKFVQDF 

       730 
VAAWTKVMNL DRFDLA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE010299 Genomic DNA. Translation: AAM04404.1.
RefSeqNP_615924.1. NC_003552.1.

3D structure databases

HSSPHSSP built from PDB template 2CCA based on UniProtKB Q50555.
ProteinModelPortalQ8TS34.
SMRQ8TS34. Positions 28-736.
ModBaseSearch...

Protein family/group databases

PeroxiBase2324. MacCP01_C2A.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1472862.
GenomeReviewsGene locus MA_0972 in contig AE010299_GR.
KEGGmac:MA0972.
NMPDRfig|188937.1.peg.950.

Phylogenomic databases

HOGENOMHBG285610.
OMAKRHAPSM.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycMACE188937:MA0972-MONOMER.

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]
KOK03782.
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_METAC
AccessionPrimary (citable) accession number: Q8TS34
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 1, 2002
Last modified: November 16, 2011
This is version 64 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