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UniProtKB/Swiss-Prot entry P13029


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CATA_ECOLI
Primary accession number P13029
Secondary accession number Q2M8N8
Integrated into Swiss-Prot on January 1, 1990
Sequence was last modified on October 1, 1993 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 97)
Name and origin of the protein
Protein name Peroxidase/catalase HPI
Synonyms EC 1.11.1.6
EC 1.11.1.7
Catalase-peroxidase
Hydroperoxidase I
Gene name
Name: katG
OrderedLocusNames: b3942, JW3914
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=3045098 [NCBI, ExPASy, EBI, Israel, Japan]
Triggs-Raine B.L., Doble B.W., Mulvey M.R., Sorby P.A., Loewen P.C.;
"Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli.";
J. Bacteriol. 170:4415-4419(1988).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-339.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.15.3391; PubMed=8346018 [NCBI, ExPASy, EBI, Israel, Japan]
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes.";
Nucleic Acids Res. 21:3391-3398(1993).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 309-726.
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1093/nar/21.23.5408; PubMed=8265357 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes.";
Nucleic Acids Res. 21:5408-5417(1993).
[6]
BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND HEME-BINDING.
PubMed=374409 [NCBI, ExPASy, EBI, Israel, Japan]
Claiborne A., Fridovich I.;
"Purification of the o-dianisidine peroxidase from Escherichia coli B.";
J. Biol. Chem. 254:4245-4252(1979).
[7]
COVALENT BOND.
DOI=10.1074/jbc.M304053200; PubMed=12832453 [NCBI, ExPASy, EBI, Israel, Japan]
Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T., Singh R., Switala J., Carpena X., Fita I., Loewen P.C.;
"Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry.";
J. Biol. Chem. 278:35687-35692(2003).
[8]
BIOPHYSICOCHEMICAL PROPERTIES.
DOI=10.1016/j.abb.2007.12.008; PubMed=18178143 [NCBI, ExPASy, EBI, Israel, Japan]
Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
"Comparative study of catalase-peroxidases (KatGs).";
Arch. Biochem. Biophys. 471:207-214(2008).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 422-726.
DOI=10.1107/S0907444904020621; PubMed=15388929 [NCBI, ExPASy, EBI, Israel, Japan]
Carpena X., Melik-Adamyan W., Loewen P.C., Fita I.;
"Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli.";
Acta Crystallogr. D 60:1824-1832(2004).
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 H2O2 = O2 + 2 H2O.
  • CATALYTIC ACTIVITY: Donor + H2O2 = oxidized donor + 2 H2O.
  • COFACTOR: Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=35 mM for H2O2 for the catalase reaction (at pH 5.5-6.0);
    KM=4.2 mM for H2O2 for the catalase reaction (at pH 7.0);
    KM=3.9 mM for H2O2 for the catalase reaction (at pH 7.5);
    KM=60 µM for H2O2 for the peroxidase reaction;
    KM=24 µM for ABTS for the peroxidase reaction;
    Vmax=3730 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0);
    Vmax=2220 µmol/min/mg enzyme for H2O2 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;
  • SUBUNIT: Homotetramer.
  • INDUCTION: By hydrogen peroxide.
  • PTM: The N-terminus is blocked.
  • PTM: The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme (By similarity).
  • SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.
  • SIMILARITY: Contains 1 HRM (heme regulatory motif) repeat.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M21516; AAA24040.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC76924.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE77368.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
L19201; AAB03074.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00006; AAC43048.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A65201; CSECHP.
RefSeq AP_003867.1; -.
NP_418377.1; -.
3D structure databases
PDB
1U2J; X-ray; 2.30 A; A/B/C/D/E/F/G/H=422-726.[ExPASy / RCSB / EBI]
1U2K; X-ray; 2.00 A; A=422-726.[ExPASy / RCSB / EBI]
1U2L; X-ray; 2.30 A; A/B=422-726.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1U2J; -.
1U2K; -.
1U2L; -.
ModBase P13029.
Protein-protein interaction databases
DIP DIP:10053N; -.
IntAct P13029; -.
Protein family/group databases
PeroxiBase 2394; EcoCP01_K-12.
Enzyme and pathway databases
BioCyc EcoCyc:HYDROPEROXIDI-MON; -.
MetaCyc:HYDROPEROXIDI-MON; -.
2D gel databases
SWISS-2DPAGE P13029; -.
Organism-specific databases
EchoBASE EB0506; -.
EcoGene EG10511; katG.
Ontologies
GO
GO:0005829; Cellular component: cytosol (inferred from direct assay from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR000763; Catalase_proxase.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.
Pfam PF00141; peroxidase; 2.
Pfam graphical view of domain structure.
PRINTS PR00460; BPEROXIDASE.
PR00458; PEROXIDASE.
TIGRFAMs TIGR00198; cat_per_HPI; 1.
PROSITE PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS P13029.
Genome annotation databases
GeneID 948431; -.
GenomeReviews U00096_GR; b3942.
AP009048_GR; JW3914.
KEGG ecj:JW3914; -.
eco:b3942; -.
Phylogenomic databases
HOGENOM P13029; -.
Genome annotation databases
CMR P13029; b3942.
Other
ProtoNet P13029.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   726  726     Peroxidase/catalase HPI. PRO_0000055564
REPEAT   15    20  6     HRM. 
ACT_SITE   106   106        Proton acceptor (By similarity). 
METAL   267   267        Iron (heme axial ligand). 
SITE   102   102  1     Transition state stabilizer (By similarity). 
CROSSLNK   105   226        Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252). 
CROSSLNK   226   252        Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105). 
CONFLICT   621   621        A -> G (in Ref. 1; AAA24040). 
HELIX   447   458  12      
HELIX   464   475  12      
TURN   480   483  4      
HELIX   491   493  3      
HELIX   497   499  3      
HELIX   501   503  3      
HELIX   506   509  4      
HELIX   510   520  11      
HELIX   525   541  17      
TURN   542   545  4      
HELIX   561   563  3      
HELIX   566   570  5      
STRAND   575   577  3      
TURN   578   581  4      
HELIX   591   601  11      
HELIX   606   619  14      
STRAND   623   625  3      
HELIX   641   647  7      
STRAND   651   657  7      
STRAND   663   667  5      
TURN   668   670  3      
STRAND   673   677  5      
HELIX   679   686  8      
HELIX   688   698  11      
HELIX   703   718  16      
TURN   719   721  3      
Sequence information
Length: 726 AA [This is the length of the unprocessed precursor] Molecular weight: 80024 Da [This is the MW of the unprocessed precursor] CRC64: 24D32EBED5DE9BD6 [This is a checksum on the sequence]
        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 

P13029 in FASTA format

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View entry in raw text format (no links)
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