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Protein

Catalase-peroxidase

Gene

katG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity.3 Publications

Catalytic activityi

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

Cofactori

heme b1 PublicationNote: Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.1 Publication

Kineticsi

  1. KM=35 mM for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. KM=4.2 mM for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. KM=3.9 mM for H2O2 for the catalase reaction (at pH 7.5)2 Publications
  4. KM=60 µM for H2O2 for the peroxidase reaction2 Publications
  5. KM=24 µM for ABTS for the peroxidase reaction2 Publications
  1. Vmax=3730 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0)2 Publications
  2. Vmax=2220 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0)2 Publications
  3. Vmax=18 µmol/min/mg enzyme for ABTS for the peroxidase reaction2 Publications

pH dependencei

Optimum pH is 4.25 for the peroxidase reaction and 7.5 for the catalase reaction.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei102 – 1021Transition state stabilizerUniRule annotation
Active sitei106 – 1061Proton acceptorUniRule annotation
Metal bindingi267 – 2671Iron (heme axial ligand)

GO - Molecular functioni

  • catalase activity Source: EcoCyc
  • heme binding Source: EcoCyc
  • identical protein binding Source: EcoCyc
  • metal ion binding Source: UniProtKB-KW
  • oxidoreductase activity Source: EcoliWiki
  • peroxidase activity Source: EcoCyc

GO - Biological processi

  • cellular oxidant detoxification Source: GOC
  • cellular response to hydrogen peroxide Source: EcoCyc
  • hydrogen peroxide catabolic process Source: EcoCyc
  • response to oxidative stress Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciEcoCyc:HYDROPEROXIDI-MONOMER.
ECOL316407:JW3914-MONOMER.
MetaCyc:HYDROPEROXIDI-MONOMER.

Protein family/group databases

PeroxiBasei2394. EcoCP01_K-12.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Hydroperoxidase I1 Publication
Short name:
HPI1 Publication
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:b3942, JW3914
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10511. katG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extracellular region Source: GO_Central
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Cells are more sensitive to killing by nalidixic acid, the effect is mitigated by pretreatment with 2,2'-bipyridyl and thiourea, both of which inhibit hydroxyl radical accumulation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 726726Catalase-peroxidasePRO_0000055564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki105 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252)1 Publication
Cross-linki226 ↔ 252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105)1 Publication

Post-translational modificationi

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

Proteomic databases

EPDiP13029.
PaxDbiP13029.
PRIDEiP13029.

2D gel databases

SWISS-2DPAGEP13029.

Expressioni

Inductioni

By hydrogen peroxide.

Interactioni

Subunit structurei

Homotetramer.1 Publication

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263062. 10 interactions.
DIPiDIP-10053N.
IntActiP13029. 11 interactions.
MINTiMINT-1304887.
STRINGi511145.b3942.

Structurei

Secondary structure

1
726
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi429 – 4313Combined sources
Helixi447 – 45812Combined sources
Turni459 – 4613Combined sources
Helixi464 – 47512Combined sources
Turni480 – 4834Combined sources
Helixi491 – 4933Combined sources
Helixi497 – 4993Combined sources
Helixi501 – 5033Combined sources
Helixi506 – 52015Combined sources
Helixi525 – 54319Combined sources
Helixi561 – 5633Combined sources
Helixi566 – 5705Combined sources
Beta strandi575 – 5773Combined sources
Turni578 – 5814Combined sources
Helixi591 – 60111Combined sources
Helixi606 – 61914Combined sources
Beta strandi623 – 6253Combined sources
Helixi641 – 6477Combined sources
Beta strandi651 – 6577Combined sources
Beta strandi662 – 6676Combined sources
Turni668 – 6703Combined sources
Beta strandi673 – 6786Combined sources
Helixi679 – 6868Combined sources
Helixi688 – 69710Combined sources
Beta strandi699 – 7013Combined sources
Helixi703 – 71816Combined sources
Turni719 – 7213Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U2JX-ray2.30A/B/C/D/E/F/G/H422-726[»]
1U2KX-ray2.00A422-726[»]
1U2LX-ray2.30A/B422-726[»]
ProteinModelPortaliP13029.
SMRiP13029. Positions 30-725.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP13029.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
InParanoidiP13029.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.
PhylomeDBiP13029.

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.

P13029-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS
60 70 80 90 100
NRSNPLGEDF DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF
110 120 130 140 150
IRMAWHGAGT YRSIDGRGGA GRGQQRFAPL NSWPDNVSLD KARRLLWPIK
160 170 180 190 200
QKYGQKISWA DLFILAGNVA LENSGFRTFG FGAGREDVWE PDLDVNWGDE
210 220 230 240 250
KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS AAAAIRATFG
260 270 280 290 300
NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST
310 320 330 340 350
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF
360 370 380 390 400
EAVDAPEIIP DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF
410 420 430 440 450
NEAFARAWFK LTHRDMGPKS RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI
460 470 480 490 500
IDLKFAIADS GLSVSELVSV AWASASTFRG GDKRGGANGA RLALMPQRDW
510 520 530 540 550
DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA ASAAGLSIHV
560 570 580 590 600
PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ
610 620 630 640 650
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR
660 670 680 690 700
YEWKATDESK ELFEGRDRET GEVKFTASRA DLVFGSNSVL RAVAEVYASS
710 720
DAHEKFVKDF VAAWVKVMNL DRFDLL
Length:726
Mass (Da):80,024
Last modified:October 1, 1993 - v2
Checksum:i24D32EBED5DE9BD6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti621 – 6211A → G in AAA24040 (PubMed:3045098).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21516 Genomic DNA. Translation: AAA24040.1.
U00096 Genomic DNA. Translation: AAC76924.1.
AP009048 Genomic DNA. Translation: BAE77368.1.
L19201 Genomic DNA. Translation: AAB03074.1.
U00006 Genomic DNA. Translation: AAC43048.1.
PIRiA65201. CSECHP.
RefSeqiNP_418377.1. NC_000913.3.
WP_001295695.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC76924; AAC76924; b3942.
BAE77368; BAE77368; BAE77368.
GeneIDi948431.
KEGGiecj:JW3914.
eco:b3942.
PATRICi32123405. VBIEscCol129921_4063.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21516 Genomic DNA. Translation: AAA24040.1.
U00096 Genomic DNA. Translation: AAC76924.1.
AP009048 Genomic DNA. Translation: BAE77368.1.
L19201 Genomic DNA. Translation: AAB03074.1.
U00006 Genomic DNA. Translation: AAC43048.1.
PIRiA65201. CSECHP.
RefSeqiNP_418377.1. NC_000913.3.
WP_001295695.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U2JX-ray2.30A/B/C/D/E/F/G/H422-726[»]
1U2KX-ray2.00A422-726[»]
1U2LX-ray2.30A/B422-726[»]
ProteinModelPortaliP13029.
SMRiP13029. Positions 30-725.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263062. 10 interactions.
DIPiDIP-10053N.
IntActiP13029. 11 interactions.
MINTiMINT-1304887.
STRINGi511145.b3942.

Protein family/group databases

PeroxiBasei2394. EcoCP01_K-12.

2D gel databases

SWISS-2DPAGEP13029.

Proteomic databases

EPDiP13029.
PaxDbiP13029.
PRIDEiP13029.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC76924; AAC76924; b3942.
BAE77368; BAE77368; BAE77368.
GeneIDi948431.
KEGGiecj:JW3914.
eco:b3942.
PATRICi32123405. VBIEscCol129921_4063.

Organism-specific databases

EchoBASEiEB0506.
EcoGeneiEG10511. katG.

Phylogenomic databases

eggNOGiENOG4105C1X. Bacteria.
COG0376. LUCA.
HOGENOMiHOG000218110.
InParanoidiP13029.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.
PhylomeDBiP13029.

Enzyme and pathway databases

BioCyciEcoCyc:HYDROPEROXIDI-MONOMER.
ECOL316407:JW3914-MONOMER.
MetaCyc:HYDROPEROXIDI-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP13029.
PROiP13029.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli."
    Triggs-Raine B.L., Doble B.W., Mulvey M.R., Sorby P.A., Loewen P.C.
    J. Bacteriol. 170:4415-4419(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
    Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
    Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-339.
    Strain: K12 / MG1655 / ATCC 47076.
  5. "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes."
    Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.
    Nucleic Acids Res. 21:5408-5417(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 309-726.
    Strain: K12 / MG1655 / ATCC 47076.
  6. "Purification of the o-dianisidine peroxidase from Escherichia coli B."
    Claiborne A., Fridovich I.
    J. Biol. Chem. 254:4245-4252(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, HEME-BINDING, COFACTOR.
  7. "Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry."
    Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T., Singh R., Switala J., Carpena X., Fita I., Loewen P.C.
    J. Biol. Chem. 278:35687-35692(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT BOND.
  8. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
  9. "YihE kinase is a central regulator of programmed cell death in bacteria."
    Dorsey-Oresto A., Lu T., Mosel M., Wang X., Salz T., Drlica K., Zhao X.
    Cell Rep. 3:528-537(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    Strain: K12 / MG1655 / ATCC 47076.
  10. "Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli."
    Carpena X., Melik-Adamyan W., Loewen P.C., Fita I.
    Acta Crystallogr. D 60:1824-1832(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 422-726.

Entry informationi

Entry nameiKATG_ECOLI
AccessioniPrimary (citable) accession number: P13029
Secondary accession number(s): Q2M8N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1993
Last modified: March 16, 2016
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.