Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5X2D9 (KATG1_LEGPA)

Last modified May 5, 2009. Version 38. 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 1
      Short name=CP 1
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 1
Gene names
Name: katG1
Ordered Locus Names: lpp2454
OrganismLegionella pneumophila (strain Paris) [Complete proteome] [HAMAP]
Taxonomic identifier297246 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. HAMAP MF_01961

Donor + H2O2 = oxidized donor + 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.

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: HAMAP

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 721721Catalase-peroxidase 1 HAMAP MF_01961
PRO_0000354820

Sites

Active site991Proton acceptor By similarity
Metal binding2641Iron (heme axial ligand) By similarity
Site951Transition state stabilizer By similarity

Amino acid modifications

Cross-link98 ↔ 223Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249) By similarity
Cross-link223 ↔ 249Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5X2D9-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: 353ACF8C86D71A60

FASTA72180,503
        10         20         30         40         50         60 
MDGKVGNTAT GCPVIHGGMT SAETSNTAWW PNALNLDILH QHDTKTNPMG KDFNYREEVK 

        70         80         90        100        110        120 
KLDFVAFKKD LHALMTDSQA WWPADWGHYG GLMIRMSWHA AGSYRVADGR GGAGTGNQRF 

       130        140        150        160        170        180 
APLNSWPDNV NLDKARRLLW PIKKKYGNKI SWADLIVLAG TIAYESMGLK TFGFGFGRED 

       190        200        210        220        230        240 
IWHPEKDVYW GSEQEWLGAK RYDDKDRQSL ETPLAAVQMG LIYVNPEGVN GQPDPLRTAQ 

       250        260        270        280        290        300 
DVRVTFGRMA MNDEETVALT AGGHTVGKCH GNGNAKFLGP EPEAADIEDQ GLGWINKTTR 

       310        320        330        340        350        360 
GIGRNTVSSG IEGAWTTHPT QWDNGYFYLL LNYDWELKKS PAGAWQWEPI HIKEEDKPVD 

       370        380        390        400        410        420 
VEDPAIRHNP IMTDADMAIK MDPVYRKIAE RFYKDPDYFA EVFARAWFKL THRDMGPKTR 

       430        440        450        460        470        480 
YIGPDVPKED LIWQDPVPSG NRAYDIAAAK AKIAASNLTI GEMVSTAWDS ARTFRGSDKR 

       490        500        510        520        530        540 
GGANGARIRL KPQKDWEGNE PQRLTKVLRI LEGIAADTGA SVADVIVLAG NVGIEKAAKA 

       550        560        570        580        590        600 
AGFDIIVPFA PGRGDATDDM TDAESFDVLE PLHDGYRNWL KKAYDVRPEE LMLDRTQLMG 

       610        620        630        640        650        660 
LTAHEMTVLV GGLRVLGTNH NNTQHGVFTD RVGVLTNDFF VNLTDMANVW IPSKDNLYEI 

       670        680        690        700        710        720 
RDRKAGNIKW TATRVDLVFG SNSILRSYAE VYAQDDNKGK FIQDFVAAWT KVMNADRFDL 


A 

« Hide

References

[1]"Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity."
Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L., Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J., Glaser P., Buchrieser C.
Nat. Genet. 36:1165-1173(2004) [PubMed: 15467720] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CR628336 Genomic DNA. Translation: CAH13607.1.
RefSeqYP_124759.1.

3D structure databases

ModBaseSearch...

Protein family/group databases

PeroxiBase2641. LpnCP02_Paris.

Genome annotation databases

GeneID3116473.
GenomeReviewsGene locus lpp2454 in contig CR628336_GR.
KEGGlpp:lpp2454.

Organism-specific databases

LegioListlpp2454.
CMRSearch...

Phylogenomic databases

HOGENOMQ5X2D9.
OMAQ5X2D9. WPNALNL.

Enzyme and pathway databases

BioCycLPNE297246:LPP2454-MON.

Family and domain databases

HAMAPMF_01961.
[Tree]
InterProIPR000763. Catalase_proxase.
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. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG1_LEGPA
AccessionPrimary (citable) accession number: Q5X2D9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 23, 2004
Last modified: May 5, 2009
This is version 38 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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