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Reviewed, UniProtKB/Swiss-Prot Q9ZGM4 (KATG1_LEGPN)

Last modified June 16, 2009. Version 44. 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
Synonyms: katB
OrganismLegionella pneumophila
Taxonomic identifier446 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella

Protein attributes

Sequence length721 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Ref.1

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.

Subcellular location

Cytoplasm. Ref.2

Induction

Induced during exponential growth. Ref.1

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
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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_0000354815

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
Q9ZGM4-1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: D96347BDAD0B719C

FASTA72180,500
        10         20         30         40         50         60 
MDGKVGSTTT GCPVIHGGMT STGTSNTAWW PNALNLDILH QHDTKTNPME KDFNYREEVK 

        70         80         90        100        110        120 
KLDFEALKKD 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 RYDGKSRESL ENPLAAVQMG LIYVNPEGVN GQPDPLRTAQ 

       250        260        270        280        290        300 
DVRVTFGRMA MNDEETVALT AGGHTVGKCH GNGNAKLLGP NPEAANVEDQ GLGWINKTTR 

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

       370        380        390        400        410        420 
VEDPAIRHNP IMTDADMAMK MDPVYRKIAE RFYQDPDYFA EVFARAWFKL THRDMGPKTR 

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

       490        500        510        520        530        540 
GGANGARIRL KPQKDWEGNE PQRLTKVLQI LEDIATDTGA SVADVIILAG NVGIEKAAKA 

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

       610        620        630        640        650        660 
LTAHEMTVLV GGLRVLGTNH NNTQYGVFTD RVGALTNDFF VNLTDMANVW IPSKDNLYEI 

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


A 

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References

[1]"Legionella pneumophila catalase-peroxidases: cloning of the katB gene and studies of KatB function."
Bandyopadhyay P., Steinman H.M.
J. Bacteriol. 180:5369-5374(1998) [PubMed: 9765568] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
Strain: JR32.
[2]"Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function."
Bandyopadhyay P., Steinman H.M.
J. Bacteriol. 182:6679-6686(2000) [PubMed: 11073912] [Abstract]
Cited for: SUBCELLULAR LOCATION.
Strain: JR32.

Cross-references

Sequence databases

AF078110 Genomic DNA. Translation: AAC64361.1.

3D structure databases

HSSPHSSP built from PDB template 1MWV based on UniProtKB Q939D2.
ModBaseSearch...

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_LEGPN
AccessionPrimary (citable) accession number: Q9ZGM4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 1, 1999
Last modified: June 16, 2009
This is version 44 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