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Q04657 (KATG_MYCIT) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 68. 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
Protein Mi85
Gene names
Name:katG
Synonyms:Mi85
OrganismMycobacterium intracellulare
Taxonomic identifier1767 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length746 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. 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
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 – 746746Catalase-peroxidase HAMAP MF_01961
PRO_0000055570

Sites

Active site1141Proton acceptor By similarity
Metal binding2771Iron (heme axial ligand) By similarity
Site1101Transition state stabilizer By similarity

Amino acid modifications

Cross-link113 ↔ 236Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-262) By similarity
Cross-link236 ↔ 262Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-113) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q04657 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: 15F35F7F5028F2B2

FASTA74681,418
        10         20         30         40         50         60 
MSSDTSSSRP PQPDSGTASK SESENPAIPS PKPKAHAPLT NRDWWPDQVD VSSLHPHSPL 

        70         80         90        100        110        120 
SNPLGDDFDY AAEFAKLDVE ALKADMISLM TTSQDWWPAD YGHYGGLFIR MSWHAAGTYR 

       130        140        150        160        170        180 
IHDGRGGAGQ GMQRFAPLNS WPDNASLDKA RRLLWPIKKK YGNKISWADL ITYAGNVALE 

       190        200        210        220        230        240 
SMGFKTFGFG FGREDVWEPE EILWGEEEEW LGTDKRYSGE RELAQPYGAT TMGLIYVNPE 

       250        260        270        280        290        300 
GPEGKPDPIA AAIDIRETFG RMAMNDEETA ALIVGGHSFG KTHGAGDADL VGPEPEAAPI 

       310        320        330        340        350        360 
EQQGLGWKSS YGTGSGKDAI TSGLEVVWTP TPTKWDNSFL ETLYGYEWEL TKSPAGAWQF 

       370        380        390        400        410        420 
TAKDGAGAGT IPDPFGGAGR APTMLVTDIS LRESPIYADI TRRWLDHPEE LADAFAKAWY 

       430        440        450        460        470        480 
KLLHRDMGPI SRYLGPWVAE PQLWQDPVPA VDHELVDDND VAALKKKVLD SGLSIPQLVK 

       490        500        510        520        530        540 
TAWSAAASYR NTDKRGGANG GRLRLQPQRS WEVNEPSELD KVLPVLEKIQ QDFNASASGG 

       550        560        570        580        590        600 
KKISLADLIV LAGSAAVEKA AKDAGYEISV HFAPGRTDAS QESTDVESFA VLEPRADGFR 

       610        620        630        640        650        660 
NYIRPGEKAP LEQLLIERAY LLGVTGPEMT VLVGGLRALG ANHGSSKHGV FTDRPGALTN 

       670        680        690        700        710        720 
DFFVNLLDMG TEWKASETAE NVYEGRDRAS GALKWTATAN DLVFGSNSVL RGLVEVYAQD 

       730        740 
DAHGKFVEDF VAAWVKVMNS DRFDLK 

« Hide

References

[1]"The catalase-peroxidase of Mycobacterium intracellulare: nucleotide sequence analysis and expression in Escherichia coli."
Morris S.L., Nair J., Rouse D.A.
J. Gen. Microbiol. 138:2363-2370(1992) [PubMed: 1336034] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86741 Genomic DNA. Translation: AAA25360.1.
PIRA47685.

3D structure databases

ProteinModelPortalQ04657.
SMRQ04657. Positions 41-746.
ModBaseSearch...

Protein family/group databases

PeroxiBase2433. MinCP01.

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_MYCIT
AccessionPrimary (citable) accession number: Q04657
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: October 19, 2011
This is version 68 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