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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)DescriptionActionsGraphical viewLength
Sitei102Transition state stabilizerUniRule annotation1
Active sitei106Proton acceptorUniRule annotation1
Metal bindingi267Iron (heme axial ligand)1

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 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
ChainiPRO_00000555641 – 726Catalase-peroxidaseAdd BLAST726

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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 interactors.
DIPiDIP-10053N.
IntActiP13029. 11 interactors.
MINTiMINT-1304887.
STRINGi511145.b3942.

Structurei

Secondary structure

1726
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi429 – 431Combined sources3
Helixi447 – 458Combined sources12
Turni459 – 461Combined sources3
Helixi464 – 475Combined sources12
Turni480 – 483Combined sources4
Helixi491 – 493Combined sources3
Helixi497 – 499Combined sources3
Helixi501 – 503Combined sources3
Helixi506 – 520Combined sources15
Helixi525 – 543Combined sources19
Helixi561 – 563Combined sources3
Helixi566 – 570Combined sources5
Beta strandi575 – 577Combined sources3
Turni578 – 581Combined sources4
Helixi591 – 601Combined sources11
Helixi606 – 619Combined sources14
Beta strandi623 – 625Combined sources3
Helixi641 – 647Combined sources7
Beta strandi651 – 657Combined sources7
Beta strandi662 – 667Combined sources6
Turni668 – 670Combined sources3
Beta strandi673 – 678Combined sources6
Helixi679 – 686Combined sources8
Helixi688 – 697Combined sources10
Beta strandi699 – 701Combined sources3
Helixi703 – 718Combined sources16
Turni719 – 721Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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.
OMAiIAEVYAC.
PhylomeDBiP13029.

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.
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)DescriptionActionsGraphical viewLength
Sequence conflicti621A → G in AAA24040 (PubMed:3045098).Curated1

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
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263062. 10 interactors.
DIPiDIP-10053N.
IntActiP13029. 11 interactors.
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.
OMAiIAEVYAC.
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. 1 hit.
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...

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: November 2, 2016
This is version 161 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.