ECMDB

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:

Phenylalanine metabolism PW000921
Tryptophan metabolism PW000815

KEGG Pathways:

Glyoxylate and dicarboxylate metabolism ec00630
Methane metabolism ec00680
Phenylalanine metabolism ec00360
Phenylpropanoid biosynthesis ec00940
Tryptophan metabolism ec00380

KEGG Reactions:

2.0

↔

2.0

1.0

2.0Hydrogen peroxide ↔ 2.0Water + 1.0Oxygen
ReactionCard

1.0

↔

1.0

2.0

1.0Methanol + 1.0Hydrogen peroxide ↔ 1.0Formaldehyde + 2.0Water
ReactionCard

1.0

↔

1.02-Phenylacetamide

1.0

1.0L-Phenylalanine + 1.0Oxygen ↔ 1.02-Phenylacetamide + 1.0Carbon dioxide
ReactionCard

1.0Coniferyl alcohol

↔

1.0Guaiacyl lignin

1.0Coniferyl alcohol ↔ 1.0Guaiacyl lignin
ReactionCard

2.0

4.0

↔

1.0

2.0

2.03-Hydroxyanthranilic acid + 4.0Oxygen ↔ 1.0Cinnavalininate + 2.0Superoxide anion + 2.0Hydrogen peroxide + 2.0Hydrogen ion
ReactionCard

1.0Sinapyl alcohol

↔

1.0Syringyl lignin

1.0Sinapyl alcohol ↔ 1.0Syringyl lignin
ReactionCard

1.04-Coumaryl alcohol

↔

1.0p-Hydroxyphenyl lignin

1.04-Coumaryl alcohol ↔ 1.0p-Hydroxyphenyl lignin
ReactionCard

1.05-Hydroxyconiferyl alcohol

↔

1.05-Hydroxy-guaiacyl lignin

1.05-Hydroxyconiferyl alcohol ↔ 1.05-Hydroxy-guaiacyl lignin
ReactionCard

1.0Reduced acceptor

1.0

↔

1.0Acceptor

1.0

1.0Reduced acceptor + 1.0Hydrogen peroxide ↔ 1.0Acceptor + 1.0Water + 1.0Oxygen
ReactionCard

SMPDB Reactions:

1.0L-Phenylalanine

1.0

↔

1.0

1.0Sinapyl alcohol

1.0L-Phenylalanine + 1.0Oxygen + 1.0L-Phenylalanine ↔ 1.0Carbon dioxide + 1.0Sinapyl alcohol
ReactionCard

EcoCyc Reactions:

2.0

↔

2.0

1.0

2.0Hydrogen peroxide ↔ 2.0Water + 1.0Oxygen
ReactionCard

Complex Reactions:

1.0Donor

1.0

→

1.0oxidized donor

2.0

1.0Donor + 1.0Hydrogen peroxide → 1.0oxidized donor + 2.0Water
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB01476	3-Hydroxyanthranilic acid	MetaboCard
ECMDB04030	Carbon dioxide	MetaboCard
ECMDB21005	Cinnavalininate	MetaboCard
ECMDB01426	Formaldehyde	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB21232	Hydrogen peroxide	MetaboCard
ECMDB00159	L-Phenylalanine	MetaboCard
ECMDB01333	Manganese	MetaboCard
ECMDB01875	Methanol	MetaboCard
ECMDB04124	Oxygen	MetaboCard
ECMDB01491	Pyridoxal 5'-phosphate	MetaboCard
ECMDB21285	Superoxide anion	MetaboCard
ECMDB00494	Water	MetaboCard

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 Orientation

Clockwise

Centisome Percentage:

89.05

Left Sequence End

4131858

Right Sequence End

4134038

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:

peroxidase (PF00141 )

Protein Residues:

726

Protein Molecular Weight:

80023

Protein Theoretical pI:

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:

Resource	Link
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

Catalase-peroxidase (P13029)