Catalase-peroxidase - Escherichia coli (strain K12)

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P13029 (KATG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 126. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Catalase-peroxidase
Short name=CP
EC=1.11.1.21

Alternative name(s):
Hydroperoxidase I
Short name=HPI
Peroxidase/catalase

Gene names

Name:	katG
Ordered Locus Names:	b3942, JW3914

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	726 AA.
Sequence status	Complete.
Protein existence	Evidence 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. HAMAP MF_01961
Catalytic activity	Donor + H₂O₂ = oxidized donor + 2 H₂O. HAMAP MF_01961 2 H₂O₂ = O₂ + 2 H₂O. HAMAP MF_01961
Cofactor	Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer. Ref.6
Subunit structure	Homotetramer. Ref.6
Induction	By hydrogen peroxide. HAMAP MF_01961
Post-translational modification	The N-terminus is blocked. HAMAP MF_01961 The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Biophysicochemical properties	Kinetic parameters: K_M=35 mM for H₂O₂ for the catalase reaction (at pH 5.5-6.0) Ref.6 Ref.8 K_M=4.2 mM for H₂O₂ for the catalase reaction (at pH 7.0) K_M=3.9 mM for H₂O₂ for the catalase reaction (at pH 7.5) K_M=60 µM for H₂O₂ for the peroxidase reaction K_M=24 µM for ABTS for the peroxidase reaction V_max=3730 µmol/min/mg enzyme for H₂O₂ for the catalase reaction (at pH 5.5-6.0) V_max=2220 µmol/min/mg enzyme for H₂O₂ for the catalase reaction (at pH 7.0) V_max=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 process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 726

726

Catalase-peroxidase HAMAP MF_01961

PRO_0000055564

Sites

Active site

106

Proton acceptor By similarity

Metal binding

267

Iron (heme axial ligand)

Site

102

Transition state stabilizer By similarity

Amino acid modifications

Cross-link

105 ↔ 226

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252) HAMAP MF_01961

Cross-link

226 ↔ 252

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105) HAMAP MF_01961

Experimental info

Sequence conflict

621

A → G in AAA24040. Ref.1

Secondary structure

726

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P13029 [UniParc].

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

FASTA

726

80,024

        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' referencesShow '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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

PIR

CSECHP. A65201.

RefSeq

NP_418377.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U2J	X-ray	2.30	A/B/C/D/E/F/G/H	422-726	[»]
1U2K	X-ray	2.00	A	422-726	[»]
1U2L	X-ray	2.30	A/B	422-726	[»]

ProteinModelPortal

P13029.

SMR

P13029. Positions 30-725.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-10053N.

IntAct

P13029. 12 interactions.

MINT

MINT-1304887.

Protein family/group databases

PeroxiBase

2394. EcoCP01_K-12.

2D gel databases

SWISS-2DPAGE

P13029.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004229; EBESCP00000004229; EBESCG00000003452.
EBESCT00000015460; EBESCP00000014751; EBESCG00000014520.

GeneID

948431.

GenomeReviews

Gene locus JW3914 in contig AP009048_GR.
Gene locus b3942 in contig U00096_GR.

KEGG

ecj:JW3914.
eco:b3942.

PATRIC

32123405. VBIEscCol129921_4063.

Organism-specific databases

EchoBASE

EB0506.

EcoGene

EG10511. katG.

Phylogenomic databases

eggNOG

COG0376.

GeneTree

EBGT00050000011618.

HOGENOM

HBG285610.

OMA

KRHAPSM.

PhylomeDB

P13029.

ProtClustDB

PRK15061.

Enzyme and pathway databases

BioCyc

EcoCyc:HYDROPEROXIDI-MONOMER.
MetaCyc:HYDROPEROXIDI-MONOMER.

Gene expression databases

Genevestigator

P13029.

Family and domain databases

HAMAP

MF_01961. Catal-peroxid.
[Tree]

InterPro

IPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

K03782.

Pfam

PF00141. peroxidase. 2 hits.
[Graphical view]

PRINTS

PR00460. BPEROXIDASE.
PR00458. PEROXIDASE.

SUPFAM

SSF48113. Peroxidase_super. 2 hits.

TIGRFAMs

TIGR00198. Cat_per_HPI. 1 hit.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KATG_ECOLI

Accession

Primary (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:	January 25, 2012
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

2D gel databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents