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Reviewed, UniProtKB/Swiss-Prot Q5WZY1 (KATG2_LEGPL)

Last modified February 9, 2010. Version 45. 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

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Names and origin

Protein namesRecommended name:
    Catalase-peroxidase 2
      Short name=CP 2
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 2
Gene names
Name: katG2
Ordered Locus Names: lpl0250
OrganismLegionella pneumophila (strain Lens) [Complete proteome] [HAMAP]
Taxonomic identifier297245 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

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Protein attributes

Sequence length749 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. HAMAP MF_01961

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. HAMAP MF_01961

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.

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Ontologies

Keywords
   Biological processHydrogen peroxide
   DomainSignal
   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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2727 Potential
Chain28 – 749722Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000354819

Sites

Active site1081Proton acceptor By similarity
Metal binding2701Iron (heme axial ligand) By similarity
Site1041Transition state stabilizer By similarity

Amino acid modifications

Cross-link107 ↔ 229Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) By similarity
Cross-link229 ↔ 255Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q5WZY1-1 [UniParc].

Last modified November 23, 2004. Version 1.
Checksum: F679F6E45F67F5D0

FASTA74982,899
        10         20         30         40         50         60 
MFKRTIPLFA AFTLAISPSI FPNYAHAQED KPKTNQYWWP KMLDLSPLRQ PNATSNPMGE 

        70         80         90        100        110        120 
KFNYAEEFNS LDLNAVIEDL KKLMTTSQDW WPADYGNYGP LFIRMSWHAA GTYRIYDGRG 

       130        140        150        160        170        180 
GANGGFQRFA PQNSWPDNAN LDKARRLLWP IKQKYGRKIS WADLLVLAGN VAMESMGFKT 

       190        200        210        220        230        240 
IGFAGGREDA WEAININWGT EGKWLESKRQ DKVGKLEKPL AATVMGLIYV NPEGPNGVPD 

       250        260        270        280        290        300 
PLAAAEKIRE TFGRMAMNDE ETVALIAGGH AFGKTHGAAS GKYLGPAPEA AGIEEQGFGW 

       310        320        330        340        350        360 
KNSYGSGKGK DTITSGLEGA WTVTPTHWSH NYLQNLFNFN WVKTKSPGGA IQWVPENSNA 

       370        380        390        400        410        420 
SSMVPDAFDP SKRHAPVMLT TDLALKFDPV YSKIAKRFLD NPKEFDDAFA RAWFKLIHRD 

       430        440        450        460        470        480 
MGPRSRYLGS LVPKEIMIWQ DPVPPVDYKL VDANDIANLK GKILNSGLTT PELVKTAWAS 

       490        500        510        520        530        540 
ASTFRGTDMR GGANGARIRL APQKDWPAND PQELAKVLKT LESIQNNFNN AQADGKKISL 

       550        560        570        580        590        600 
ADLIVLGGNA AIEQAAKQAG YDIIVPFTPG RTDATQGMTD VKSFEVLEPK ADGFRNYFDK 

       610        620        630        640        650        660 
SNNMSPPEML VDKASLLKLS VPEMTVLVGG MRVLNANTGQ NQYGVFTDKP GTLNNDFFIN 

       670        680        690        700        710        720 
LLSMSTEWKK SSETEGIYEG YDRKTGKLKW KATSVDLIFG ANSELRAVAE AYATDDAKDK 

       730        740 
FIQDFVNAWV KVMTADRFDI KAANANINS

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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].

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR628337 Genomic DNA. Translation: CAH14481.1.
RefSeqYP_125617.1.

3D structure databases

HSSPHSSP built from PDB template 1ITK based on UniProtKB O59651.
SMRQ5WZY1. Positions 34-740.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ5WZY1.

Protein family/group databases

PeroxiBase2397. LpnCP01_Lens.

Genome annotation databases

GeneID3113546.
GenomeReviewsGene locus lpl0250 in contig CR628337_GR.
KEGGlpf:lpl0250.
NMPDRfig|297245.3.peg.221.

Organism-specific databases

LegioListlpl0250.
CMRSearch...

Phylogenomic databases

eggNOGCOG0376.
HOGENOMHBG285610.
OMAKNKCGKG.
PhylomeDBQ5WZY1.

Enzyme and pathway databases

BioCycLPNE297245:LPL0250-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]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
TIGRFAMsTIGR00198. cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameKATG2_LEGPL
AccessionPrimary (citable) accession number: Q5WZY1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 23, 2004
Last modified: February 9, 2010
This is version 45 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)

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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