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A0QGA4 (KATG_MYCA1) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 35. 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:MAV_2753
OrganismMycobacterium avium (strain 104) [Complete proteome] [HAMAP]
Taxonomic identifier243243 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length748 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
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 – 748748Catalase-peroxidase HAMAP MF_01961
PRO_0000354835

Sites

Active site1141Proton acceptor By similarity
Metal binding2791Iron (heme axial ligand) By similarity
Site1101Transition state stabilizer By similarity

Amino acid modifications

Cross-link113 ↔ 238Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-264) By similarity
Cross-link238 ↔ 264Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-113) By similarity

Sequences

Sequence LengthMass (Da)Tools
A0QGA4 [UniParc].

Last modified January 9, 2007. Version 1.
Checksum: 6BEDEBA89861472A

FASTA74881,661
        10         20         30         40         50         60 
MSSDTSASRP PQPDTGTASK SESENPAIPS PHPKSNAPLT NRDWWPNQID VSRLHPHVAE 

        70         80         90        100        110        120 
ANPLGEDFDY AEEFAKLDVE ALKADVISVM TTSQDWWPAD YGHYGGLFIR MSWHAAGTYR 

       130        140        150        160        170        180 
IHDGRGGGGQ GMQRFAPLNS WPDNVSLDKA RRLLWPVKKK YGNKISWADL IIFAGNCALE 

       190        200        210        220        230        240 
SMGFKTFGFA FGREDVWEPE EILWGEEDEW LGTDKRYPGT GERELAQPYG ATTMGLIYVN 

       250        260        270        280        290        300 
PEGPEGKPDP IAAAIDIRET FGRMAMNDEE TAALIVGGHS FGKTHGAGDA DLVGPEPEAA 

       310        320        330        340        350        360 
PIEQQGLGWK SSYGTGVGKD AITSGLEVVW TPTPTKWDNT FLETLYGYEW ELTKSPAGAW 

       370        380        390        400        410        420 
QFTAKDGAGA GTIPDPFGGP GRAPTMLVTD ISLRESPIYR DITRRWLDHP EELADAFAKA 

       430        440        450        460        470        480 
WYKLLHRDMG PVSRFLGPWV PEPQLWQDPV PPVDHPLVDD NDVAALKDKV LASGLSVPQL 

       490        500        510        520        530        540 
VKTAWSAAGS YRNTDKRGGA NGGRLRLQPQ RNWEANEPSE LDKVLPVLEK IQQDFNASAS 

       550        560        570        580        590        600 
GGKKISLADL IVLAGSAAVE KAAKDAGYEI SVHFAPGRTD ASQESTDVDS FAVLEPRADG 

       610        620        630        640        650        660 
FRNFARPGEK APLEQLLLER AYLLGVTGPE MTVLVGGLRA LGANHGGSKH GVFTDRPGAL 

       670        680        690        700        710        720 
TNDFFVNLLD MGTEWKASET AENVYEGHDR ATGALKWTAT ANDLVFGSNS VLRALAEVYA 

       730        740 
QDDNQGKFVE DFVAAWVKVM NNDRFDLK 

« Hide

References

[1]Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 104.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000479 Genomic DNA. Translation: ABK67811.1.
RefSeqYP_881942.1. NC_008595.1.

3D structure databases

ProteinModelPortalA0QGA4.
SMRA0QGA4. Positions 41-748.
ModBaseSearch...

Protein-protein interaction databases

STRINGA0QGA4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBMYCT00000012069; EBMYCP00000011955; EBMYCG00000012067.
GeneID4528744.
GenomeReviewsGene locus MAV_2753 in contig CP000479_GR.
KEGGmav:MAV_2753.
PATRIC17987201. VBIMycAvi38287_2687.
TIGRMAV_2753.

Phylogenomic databases

eggNOGCOG0376.
GeneTreeEBGT00050000017549.
HOGENOMHBG285610.
OMAQGKFVED.
PhylomeDBA0QGA4.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycMAVI243243:MAV_2753-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_MYCA1
AccessionPrimary (citable) accession number: A0QGA4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: January 9, 2007
Last modified: December 14, 2011
This is version 35 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