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Protein

Catalase-peroxidase 2

Gene

katG2

Organism
Legionella pneumophila (strain Lens)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity.UniRule annotation

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bUniRule annotationNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei104 – 1041Transition state stabilizerUniRule annotation
Active sitei108 – 1081Proton acceptorUniRule annotation
Metal bindingi270 – 2701Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-262-MONOMER.

Protein family/group databases

PeroxiBasei2397. LpnCP01_Lens.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidase 2UniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CP 2UniRule annotation
Alternative name(s):
Peroxidase/catalase 2UniRule annotation
Gene namesi
Name:katG2UniRule annotation
Ordered Locus Names:lpl0250
OrganismiLegionella pneumophila (strain Lens)
Taxonomic identifieri297245 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesLegionellaceaeLegionella
Proteomesi
  • UP000002517 Componenti: Chromosome

Organism-specific databases

LegioListilpl0250.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2727UniRule annotationAdd
BLAST
Chaini28 – 749722Catalase-peroxidase 2PRO_0000354819Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki107 ↔ 229Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255)UniRule annotation
Cross-linki229 ↔ 255Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107)UniRule annotation

Post-translational modificationi

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.UniRule annotation

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ5WZY1.
SMRiQ5WZY1. Positions 34-740.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiMSTRWEK.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5WZY1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFKRTIPLFA AFTLAISPSI FPNYAHAQED KPKTNQYWWP KMLDLSPLRQ
60 70 80 90 100
PNATSNPMGE KFNYAEEFNS LDLNAVIEDL KKLMTTSQDW WPADYGNYGP
110 120 130 140 150
LFIRMSWHAA GTYRIYDGRG GANGGFQRFA PQNSWPDNAN LDKARRLLWP
160 170 180 190 200
IKQKYGRKIS WADLLVLAGN VAMESMGFKT IGFAGGREDA WEAININWGT
210 220 230 240 250
EGKWLESKRQ DKVGKLEKPL AATVMGLIYV NPEGPNGVPD PLAAAEKIRE
260 270 280 290 300
TFGRMAMNDE ETVALIAGGH AFGKTHGAAS GKYLGPAPEA AGIEEQGFGW
310 320 330 340 350
KNSYGSGKGK DTITSGLEGA WTVTPTHWSH NYLQNLFNFN WVKTKSPGGA
360 370 380 390 400
IQWVPENSNA SSMVPDAFDP SKRHAPVMLT TDLALKFDPV YSKIAKRFLD
410 420 430 440 450
NPKEFDDAFA RAWFKLIHRD MGPRSRYLGS LVPKEIMIWQ DPVPPVDYKL
460 470 480 490 500
VDANDIANLK GKILNSGLTT PELVKTAWAS ASTFRGTDMR GGANGARIRL
510 520 530 540 550
APQKDWPAND PQELAKVLKT LESIQNNFNN AQADGKKISL ADLIVLGGNA
560 570 580 590 600
AIEQAAKQAG YDIIVPFTPG RTDATQGMTD VKSFEVLEPK ADGFRNYFDK
610 620 630 640 650
SNNMSPPEML VDKASLLKLS VPEMTVLVGG MRVLNANTGQ NQYGVFTDKP
660 670 680 690 700
GTLNNDFFIN LLSMSTEWKK SSETEGIYEG YDRKTGKLKW KATSVDLIFG
710 720 730 740
ANSELRAVAE AYATDDAKDK FIQDFVNAWV KVMTADRFDI KAANANINS
Length:749
Mass (Da):82,899
Last modified:November 23, 2004 - v1
Checksum:iF679F6E45F67F5D0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH14481.1.
RefSeqiWP_011214515.1. NC_006369.1.

Genome annotation databases

EnsemblBacteriaiCAH14481; CAH14481; lpl0250.
KEGGilpf:lpl0250.
PATRICi22313959. VBILegPne33733_0330.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR628337 Genomic DNA. Translation: CAH14481.1.
RefSeqiWP_011214515.1. NC_006369.1.

3D structure databases

ProteinModelPortaliQ5WZY1.
SMRiQ5WZY1. Positions 34-740.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei2397. LpnCP01_Lens.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAH14481; CAH14481; lpl0250.
KEGGilpf:lpl0250.
PATRICi22313959. VBILegPne33733_0330.

Organism-specific databases

LegioListilpl0250.

Phylogenomic databases

HOGENOMiHOG000218110.
KOiK03782.
OMAiMSTRWEK.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciLPNE297245:GJD4-262-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Lens.

Entry informationi

Entry nameiKATG2_LEGPL
AccessioniPrimary (citable) accession number: Q5WZY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: November 23, 2004
Last modified: November 11, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.