Identification
Name:Catalase-peroxidase
Synonyms:
  • CP
  • Hydroperoxidase I
  • HPI
  • Peroxidase/catalase
Gene Name:katG
Enzyme Class:
Biological Properties
General Function:Involved in catalase activity
Specific Function:Bifunctional enzyme with both catalase and broad- spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
2 Thumb2 Thumb+Thumb
Thumb+ThumbThumb+2 Thumb
Thumb+Thumb2-Phenylacetamide+Thumb
Coniferyl alcoholGuaiacyl lignin
Coniferyl alcohol ↔ Guaiacyl lignin
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2 Thumb+4 ThumbThumb+2 Thumb+2 Thumb+2 Thumb
Sinapyl alcoholSyringyl lignin
Sinapyl alcohol ↔ Syringyl lignin
ReactionCard
4-Coumaryl alcoholp-Hydroxyphenyl lignin
4-Coumaryl alcohol ↔ p-Hydroxyphenyl lignin
ReactionCard
5-Hydroxyconiferyl alcohol5-Hydroxy-guaiacyl lignin
5-Hydroxyconiferyl alcohol ↔ 5-Hydroxy-guaiacyl lignin
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Reduced acceptor+ThumbAcceptor+Thumb+Thumb
Reduced acceptor + Hydrogen peroxide ↔ Acceptor + Water + Oxygen
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SMPDB Reactions:
L-Phenylalanine+Thumb+ThumbThumb+Sinapyl alcohol
L-Phenylalanine + Oxygen + L-PhenylalanineCarbon dioxide + Sinapyl alcohol
ReactionCard
2 Thumb2 Thumb+Thumb
EcoCyc Reactions:
2 Thumb2 Thumb+Thumb
Complex Reactions:
Donor+Thumboxidized donor+2 Thumb
Donor + Hydrogen peroxide → oxidized donor + 2 Water
ReactionCard
2 ThumbThumb+2 Thumb
Metabolites:
ECMDB IDNameView
ECMDB014763-Hydroxyanthranilic acidMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21005CinnavalininateMetaboCard
ECMDB01426FormaldehydeMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21232Hydrogen peroxideMetaboCard
ECMDB00159L-PhenylalanineMetaboCard
ECMDB01333ManganeseMetaboCard
ECMDB01875MethanolMetaboCard
ECMDB04124OxygenMetaboCard
ECMDB01491Pyridoxal 5'-phosphateMetaboCard
ECMDB21285Superoxide anionMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
antioxidant activity
binding
catalase activity
cation binding
heme binding
ion binding
iron ion binding
metal ion binding
peroxidase activity
transition metal ion binding
Process
metabolic process
oxidation reduction
response to oxidative stress
response to stimulus
response to stress
Gene Properties
Blattner:b3942
Gene OrientationClockwise
Centisome Percentage:89.05
Left Sequence End4131858
Right Sequence End4134038
Gene Sequence:
>2181 bp
ATGAGCACGTCAGACGATATCCATAACACCACAGCCACTGGCAAATGCCCGTTCCATCAG
GGCGGTCACGACCAGAGTGCGGGGGCGGGCACAACCACTCGCGACTGGTGGCCAAATCAA
CTTCGTGTTGACCTGTTAAACCAACATTCTAATCGTTCTAACCCACTGGGTGAGGACTTT
GACTACCGCAAAGAATTCAGCAAATTAGATTACTACGGCCTGAAAAAAGATCTGAAAGCC
CTGTTGACAGAATCTCAACCGTGGTGGCCAGCCGACTGGGGCAGTTACGCCGGTCTGTTT
ATTCGTATGGCCTGGCACGGCGCGGGGACTTACCGTTCAATCGATGGACGCGGTGGCGCG
GGTCGTGGTCAGCAACGTTTTGCACCGCTGAACTCCTGGCCGGATAACGTAAGCCTCGAT
AAAGCGCGTCGCCTGTTGTGGCCAATCAAACAGAAATATGGTCAGAAAATCTCCTGGGCC
GACCTGTTTATCCTCGCGGGTAACGTGGCGCTAGAAAACTCCGGCTTCCGTACCTTCGGT
TTTGGTGCCGGTCGTGAAGACGTCTGGGAACCGGATCTGGATGTTAACTGGGGTGATGAA
AAAGCCTGGCTGACTCACCGTCATCCGGAAGCGCTGGCGAAAGCACCGCTGGGTGCAACC
GAGATGGGTCTGATTTACGTTAACCCGGAAGGCCCGGATCACAGCGGCGAACCGCTTTCT
GCGGCAGCAGCTATCCGCGCGACCTTCGGCAACATGGGCATGAACGACGAAGAAACCGTG
GCGCTGATTGCGGGTGGTCATACGCTGGGTAAAACCCACGGTGCCGGTCCGACATCAAAT
GTAGGTCCTGATCCAGAAGCTGCACCGATTGAAGAACAAGGTTTAGGTTGGGCGAGCACT
TACGGCAGCGGCGTTGGCGCAGATGCCATTACCTCTGGTCTGGAAGTAGTCTGGACCCAG
ACGCCGACCCAGTGGAGCAACTATTTCTTCGAGAACCTGTTCAAGTATGAGTGGGTACAG
ACCCGCAGCCCGGCTGGCGCAATCCAGTTCGAAGCGGTAGACGCACCGGAAATTATCCCG
GATCCGTTTGATCCGTCGAAGAAACGTAAACCGACAATGCTGGTGACCGACCTGACGCTG
CGTTTTGATCCTGAGTTCGAGAAGATCTCTCGTCGTTTCCTCAACGATCCGCAGGCGTTC
AACGAAGCCTTTGCCCGTGCCTGGTTCAAACTGACGCACAGGGATATGGGGCCGAAATCT
CGCTACATCGGGCCGGAAGTGCCGAAAGAAGATCTGATCTGGCAAGATCCGCTGCCGCAG
CCGATCTACAACCCGACCGAGCAGGACATTATCGATCTGAAATTCGCGATTGCGGATTCT
GGTCTGTCTGTTAGTGAGCTGGTATCGGTGGCCTGGGCATCTGCTTCTACCTTCCGTGGT
GGCGACAAACGCGGTGGTGCCAACGGTGCGCGTCTGGCATTAATGCCGCAGCGCGACTGG
GATGTGAACGCCGCAGCCGTTCGTGCTCTGCCTGTTCTGGAGAAAATCCAGAAAGAGTCT
GGTAAAGCCTCGCTGGCGGATATCATAGTGCTGGCTGGTGTGGTTGGTGTTGAGAAAGCC
GCAAGCGCCGCAGGTTTGAGCATTCATGTACCGTTTGCGCCGGGTCGCGTTGATGCGCGT
CAGGATCAGACTGACATTGAGATGTTTGAGCTGCTGGAGCCAATTGCTGACGGTTTCCGT
AACTATCGCGCTCGTCTGGACGTTTCCACCACCGAGTCACTGCTGATCGACAAAGCACAG
CAACTGACGCTGACCGCGCCGGAAATGACTGCGCTGGTGGGCGGCATGCGTGTACTGGGT
GCCAACTTCGATGGCAGCAAAAACGGCGTCTTCACTGACCGCGTTGGCGTATTGAGCAAT
GACTTCTTCGTGAACTTGCTGGATATGCGTTACGAGTGGAAAGCGACCGACGAATCGAAA
GAGCTGTTCGAAGGCCGTGACCGTGAAACCGGCGAAGTGAAATTTACGGCCAGCCGTGCG
GATCTGGTGTTTGGTTCTAACTCCGTCCTGCGTGCGGTGGCGGAAGTTTACGCCAGTAGC
GATGCCCACGAGAAGTTTGTTAAAGACTTCGTGGCGGCATGGGTGAAAGTGATGAACCTC
GACCGTTTCGACCTGCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:726
Protein Molecular Weight:80023
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Catalase-peroxidase
MSTSDDIHNTTATGKCPFHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDF
DYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYAGLFIRMAWHGAGTYRSIDGRGGA
GRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFG
FGAGREDVWEPDLDVNWGDEKAWLTHRHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLS
AAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWAST
YGSGVGADAITSGLEVVWTQTPTQWSNYFFENLFKYEWVQTRSPAGAIQFEAVDAPEIIP
DPFDPSKKRKPTMLVTDLTLRFDPEFEKISRRFLNDPQAFNEAFARAWFKLTHRDMGPKS
RYIGPEVPKEDLIWQDPLPQPIYNPTEQDIIDLKFAIADSGLSVSELVSVAWASASTFRG
GDKRGGANGARLALMPQRDWDVNAAAVRALPVLEKIQKESGKASLADIIVLAGVVGVEKA
ASAAGLSIHVPFAPGRVDARQDQTDIEMFELLEPIADGFRNYRARLDVSTTESLLIDKAQ
QLTLTAPEMTALVGGMRVLGANFDGSKNGVFTDRVGVLSNDFFVNLLDMRYEWKATDESK
ELFEGRDRETGEVKFTASRADLVFGSNSVLRAVAEVYASSDAHEKFVKDFVAAWVKVMNL
DRFDLL
References
External Links:
ResourceLink
Uniprot ID:P13029
Uniprot Name:KATG_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676118
Ecogene ID:EG10511
Ecocyc:EG10511
ColiBase:b3942
Kegg Gene:b3942
EchoBASE ID:EB0506
CCDB:KATG_ECOLI
BacMap:16131780
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "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. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Carpena, X., Melik-Adamyan, W., Loewen, P. C., Fita, I. (2004). "Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli." Acta Crystallogr D Biol Crystallogr 60:1824-1832. Pubmed: 15388929
  • Claiborne, A., Fridovich, I. (1979). "Purification of the o-dianisidine peroxidase from Escherichia coli B. Physicochemical characterization and analysis of its dual catalatic and peroxidatic activities." J Biol Chem 254:4245-4252. Pubmed: 374409
  • Donald, L. J., Krokhin, O. V., Duckworth, H. W., Wiseman, B., Deemagarn, T., Singh, R., Switala, J., Carpena, X., Fita, I., Loewen, P. C. (2003). "Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry." J Biol Chem 278:35687-35692. Pubmed: 12832453
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Plunkett, G. 3rd, Burland, V., Daniels, D. L., Blattner, F. R. (1993). "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. Pubmed: 8346018
  • Singh, R., Wiseman, B., Deemagarn, T., Jha, V., Switala, J., Loewen, P. C. (2008). "Comparative study of catalase-peroxidases (KatGs)." Arch Biochem Biophys 471:207-214. Pubmed: 18178143
  • Triggs-Raine, B. L., Doble, B. W., Mulvey, M. R., Sorby, P. A., Loewen, P. C. (1988). "Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli." J Bacteriol 170:4415-4419. Pubmed: 3045098