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Reviewed, UniProtKB/Swiss-Prot P13029 (KATG_ECOLI)

Last modified November 25, 2008. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase
    Hydroperoxidase I
      Short name=HPI
Gene names
Name: katG
Ordered Locus Names: b3942, JW3914
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length726 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

2 H(2)O(2) = O(2) + 2 H(2)O.

Donor + H(2)O(2) = oxidized donor + 2 H(2)O.

Cofactor

Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.

Subunit structure

Homotetramer.

Induction

By hydrogen peroxide.

Post-translational modification

The N-terminus is blocked.

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

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=35 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)

KM=4.2 mM for H(2)O(2) for the catalase reaction (at pH 7.0)

KM=3.9 mM for H(2)O(2) for the catalase reaction (at pH 7.5)

KM=60 µM for H(2)O(2) for the peroxidase reaction

KM=24 µM for ABTS for the peroxidase reaction

Vmax=3730 µmol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)

Vmax=2220 µmol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 7.0)

Vmax=18 µmol/min/mg enzyme for ABTS for the peroxidase reaction

pH dependence:

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

Ontologies

Keywords

   Biological processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Complete proteome
Direct protein sequencing

Gene Ontology (GO)

   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytosol

Inferred from direct assay. Source: UniProtKB

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 726726Catalase-peroxidase
PRO_0000055564

Sites

Active site1061Proton acceptor By similarity
Metal binding2671Iron (heme axial ligand)
Site1021Transition state stabilizer By similarity

Amino acid modifications

Cross-link105 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252)
Cross-link226 ↔ 252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105)

Experimental info

Sequence conflict6211A → G in AAA24040. Ref.1

Secondary structure

................................................ 726
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P13029-1 [UniParc].

Last modified October 1, 1993. Version 2.
Checksum: 24D32EBED5DE9BD6

FASTA72680,024
        10         20         30         40         50         60 
MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF 

        70         80         90        100        110        120 
DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA 

       130        140        150        160        170        180 
GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG 

       190        200        210        220        230        240 
FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS 

       250        260        270        280        290        300 
AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST 

       310        320        330        340        350        360 
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP 

       370        380        390        400        410        420 
DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS 

       430        440        450        460        470        480 
RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG 

       490        500        510        520        530        540 
GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA 

       550        560        570        580        590        600 
ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ 

       610        620        630        640        650        660 
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK 

       670        680        690        700        710        720 
ELFEGRDRET GEVKFTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL 


DRFDLL 

« Hide

References

« Hide 'large scale' references
[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: 3045098] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract]
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: 16738553] [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: 8346018] [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: 8265357] [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: 374409] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, HEME-BINDING.
[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: 12832453] [Abstract]
Cited for: COVALENT BOND.
[8]"Comparative study of catalase-peroxidases (KatGs)."
Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.
Arch. Biochem. Biophys. 471:207-214(2008) [PubMed: 18178143] [Abstract]
Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
[9]"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: 15388929] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 422-726.

Cross-references

Sequence databases

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.
PIRCSECHP. A65201.
RefSeqAP_003867.1.
NP_418377.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1U2JX-ray2.30A/B/C/D/E/F/G/H422-726[»]
1U2KX-ray2.00A422-726[»]
1U2LX-ray2.30A/B422-726[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:10053N.

Protein family/group databases

PeroxiBase2394. EcoCP01_K-12.

2-D gel databases

SWISS-2DPAGEP13029.

Genome annotation databases

GeneID948431.
GenomeReviewsGene locus b3942 in contig U00096_GR.
Gene locus JW3914 in contig AP009048_GR.
KEGGecj:JW3914.
eco:b3942.

Organism-specific databases

EchoBASEEB0506.
EcoGeneEG10511. katG.
CMRSearch...

Phylogenomic databases

HOGENOMP13029.

Enzyme and pathway databases

BioCycEcoCyc:HYDROPEROXIDI-MON.
MetaCyc:HYDROPEROXIDI-MON.

Family and domain databases

HAMAPMF_01961.
[Tree]
InterProIPR000763. Catalase_proxase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[Graphical view]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
TIGRFAMsTIGR00198. cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_ECOLI
AccessionPrimary (citable) accession number: P13029
Secondary accession number(s): Q2M8N8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: October 1, 1993
Last modified: November 25, 2008
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

UniProtKB secondary accession numbers

Index of UniProtKB secondary accession numbers

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents