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Protein

Catalase-peroxidase

Gene

katG

Organism
Methylibium petroleiphilum (strain PM1)
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
Sitei88 – 881Transition state stabilizerUniRule annotation
Active sitei92 – 921Proton acceptorUniRule annotation
Metal bindingi256 – 2561Iron (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

BioCyciMPET420662:GHBE-3785-MONOMER.

Protein family/group databases

PeroxiBasei2346. MpetCP01.

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:Mpe_A3740
OrganismiMethylibium petroleiphilum (strain PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
Proteomesi
  • UP000000366 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 715715Catalase-peroxidasePRO_0000354832Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki91 ↔ 215Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-241)UniRule annotation
Cross-linki215 ↔ 241Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91)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

PRIDEiA2SMA4.

Interactioni

Subunit structurei

Homodimer or homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi420662.Mpe_A3740.

Structurei

3D structure databases

ProteinModelPortaliA2SMA4.
SMRiA2SMA4. Positions 16-715.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A2SMA4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATESKCPFN HAAGGGTTNQ DWWPSQLRLE LLNQHSSKSD PLGAGFDYAE
60 70 80 90 100
EFKKLDYFAL KKDLLALMTD SQDWWPADFG HYGPQFVRMA WHAAGTYRTA
110 120 130 140 150
DGRGGGGRGQ QRFAPLNSWP DNVNIDKSRR LLWPIKQKYG QRISWADLLI
160 170 180 190 200
LTGNVALESM GFRTFGFAGG REDVWEPDND VNWGNETTWL ATDKRFTGDR
210 220 230 240 250
DLDQPLAATH MGLIYVNPEG PNASGDPLAA AKDIRATFGR MAMDDEEIVA
260 270 280 290 300
LIAGGHTFGK AHGAAPESHK GPEPEGAPLE AQGLGWTSSF GSGHGKDTVS
310 320 330 340 350
SGLEVTWTTT PARWSNDFFE HLFKFEWELT QSPAGAKQWT AKDAPEIIPD
360 370 380 390 400
AHVPGKKLKP TMLTTDLTLR VDPEFEKISR RFLDNPQGFA DAFARAWFKL
410 420 430 440 450
THRDMGPKVR YLGPEVPKEE LLWQDPLPPA TLPAPNAADV AELKAKIAAS
460 470 480 490 500
GLTVAQLVAT AWASASTFRG GDKRGGANGA RLRLAPQKDW EANTPGELAK
510 520 530 540 550
VLATLETLQK ASGKFSLADV IVLAGGVGVE QAAKAAGVGI EVPFAPGRVD
560 570 580 590 600
ATQEQTDVES FAFLEPVADG FRNYFKGPGS VPVEHLLVDK AQLLTLTAPE
610 620 630 640 650
MTVLVGGLRV LGANAGGSRH GVFTDRPGVL TPDFFVNLLD MRTTWQPANG
660 670 680 690 700
VYEGKDRQTG QQKWTATRVD LAFGSNAVLR ALAEVYASAD GQTKFVHDFV
710
AAWTKVMNLD RYDLA
Length:715
Mass (Da):77,828
Last modified:March 6, 2007 - v1
Checksum:iFEF5A0F70B124663
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM96693.1.
RefSeqiWP_011831313.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM96693; ABM96693; Mpe_A3740.
KEGGimpt:Mpe_A3740.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM96693.1.
RefSeqiWP_011831313.1. NC_008825.1.

3D structure databases

ProteinModelPortaliA2SMA4.
SMRiA2SMA4. Positions 16-715.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420662.Mpe_A3740.

Protein family/group databases

PeroxiBasei2346. MpetCP01.

Proteomic databases

PRIDEiA2SMA4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM96693; ABM96693; Mpe_A3740.
KEGGimpt:Mpe_A3740.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.

Enzyme and pathway databases

BioCyciMPET420662:GHBE-3785-MONOMER.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
    Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
    J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PM1.

Entry informationi

Entry nameiKATG_METPP
AccessioniPrimary (citable) accession number: A2SMA4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: March 6, 2007
Last modified: December 9, 2015
This is version 61 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.