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Protein

Catalase-peroxidase

Gene

katG

Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6))
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)DescriptionActionsGraphical viewLength
Sitei93Transition state stabilizerUniRule annotation1
Active sitei97Proton acceptorUniRule annotation1
Metal bindingi265Iron (heme axial ligand)UniRule annotation1

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

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:Lcho_0281
OrganismiLeptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6))
Taxonomic identifieri395495 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesLeptothrix
Proteomesi
  • UP000001693 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003548261 – 723Catalase-peroxidaseAdd BLAST723

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki96 ↔ 224Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-250)UniRule annotation
Cross-linki224 ↔ 250Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96)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

Proteomic databases

PRIDEiB1Y7V8.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi395495.Lcho_0281.

Structurei

3D structure databases

ProteinModelPortaliB1Y7V8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B1Y7V8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPKTSAGQC PVMHGANTTA AQSNTAWWPN ALNLDILHQH DTKTNPLGEG
60 70 80 90 100
YRYREAVKQL DVAALKADLT ALMTRSQPWW PADWGHYGGL MIRMAWHAAG
110 120 130 140 150
SYRVADGRGG AGTGNQRFAP LNSWPDNANL DKARRLLWPI KKKYGAKISW
160 170 180 190 200
ADLIVLAGNV AYESMGLKTY GFAFGREDIW HPEKDIYWGS EKAWLAPTGG
210 220 230 240 250
EGSRYSGQRD LENPLAAVMM GLIYVNPEGV DGQPDPLKTA QDVRVTFARM
260 270 280 290 300
AMDDEETVAL TAGGHTVGKS HGNGSAANLG PAPEGADVHE QGLGWNNHSS
310 320 330 340 350
RGIGRDTVTS GIEGAWTTHP TQWDNGYFKL LLGYDWELKK SPAGAWQWEP
360 370 380 390 400
VGIKEDDKPV DVEDPSIRLN PIMTDADMAM KMDPAYRRIS ERFAADQAYF
410 420 430 440 450
SEVFARAWFK LTHRDLGPKS RYIGPEIPAE DLLWQDPVPV GPTAYDVGAV
460 470 480 490 500
KSRIATSGLS VGELVATAWD SARTWRGSDY RGGANGARIR LAPQKDWAGN
510 520 530 540 550
EPERLARVLA VLEPIAAAAG ASVADVIVLA GNVGVELAAK AAGFDVTVPF
560 570 580 590 600
APGRGDATQA QTDVESFEVL EPVADGFRNW QQRSFAVQPE EMLLDRAQLM
610 620 630 640 650
GLSAPEMTVL VGGLRVLGAN HGGSKHGVFT DRVGALTNDF FVTLTDMAHA
660 670 680 690 700
WVPTGRNSYE IRERASGVVK YTATRADLVF GSNSVLRAYA EVYAQDDSRE
710 720
KFVRDFVAAW VKVMNADRYE LQG
Length:723
Mass (Da):78,888
Last modified:May 20, 2008 - v1
Checksum:iD01F682DA9F5BA77
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001013 Genomic DNA. Translation: ACB32556.1.
RefSeqiWP_012345318.1. NC_010524.1.

Genome annotation databases

EnsemblBacteriaiACB32556; ACB32556; Lcho_0281.
KEGGilch:Lcho_0281.
PATRICi22390833. VBILepCho83238_0286.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001013 Genomic DNA. Translation: ACB32556.1.
RefSeqiWP_012345318.1. NC_010524.1.

3D structure databases

ProteinModelPortaliB1Y7V8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi395495.Lcho_0281.

Proteomic databases

PRIDEiB1Y7V8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACB32556; ACB32556; Lcho_0281.
KEGGilch:Lcho_0281.
PATRICi22390833. VBILepCho83238_0286.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiIAEVYAC.
OrthoDBiPOG091H05R1.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid. 1 hit.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiKATG_LEPCP
AccessioniPrimary (citable) accession number: B1Y7V8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: May 20, 2008
Last modified: November 2, 2016
This is version 55 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, Reference 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.