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Reviewed, UniProtKB/Swiss-Prot P21179 (CATE_ECOLI)

Last modified June 16, 2009. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 HPII
    EC=1.11.1.6
Alternative name(s):
    Hydroxyperoxidase II
Gene names
Name: katE
Ordered Locus Names: b1732, JW1721
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm Probable.

Induction

By entry into stationary phase.

Sequence similarities

Belongs to the catalase family. HPII subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   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: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 753753Catalase HPII
PRO_0000084971

Sites

Active site1281 By similarity
Active site2011 By similarity
Metal binding4151Iron (heme axial ligand)

Amino acid modifications

Cross-link392 ↔ 4153'-histidyl-3-tyrosine (His-Tyr)

Secondary structure

....................................................................................................................... 753
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21179-1 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 1F034E4866A70FB9

FASTA75384,163
        10         20         30         40         50         60 
MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT APGSLKAPDT 

        70         80         90        100        110        120 
RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR GPTLLEDFIL REKITHFDHE 

       130        140        150        160        170        180 
RIPERIVHAR GSAAHGYFQP YKSLSDITKA DFLSDPNKIT PVFVRFSTVQ GGAGSADTVR 

       190        200        210        220        230        240 
DIRGFATKFY TEEGIFDLVG NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW 

       250        260        270        280        290        300 
DYVSLQPETL HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA 

       310        320        330        340        350        360 
SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD FDLLDPTKLI 

       370        380        390        400        410        420 
PEELVPVQRV GKMVLNRNPD NFFAENEQAA FHPGHIVPGL DFTNDPLLQG RLFSYTDTQI 

       430        440        450        460        470        480 
SRLGGPNFHE IPINRPTCPY HNFQRDGMHR MGIDTNPANY EPNSINDNWP RETPPGPKRG 

       490        500        510        520        530        540 
GFESYQERVE GNKVRERSPS FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR 

       550        560        570        580        590        600 
ERVVDQLAHI DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YAIPDGDVKG 

       610        620        630        640        650        660 
RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI AATFAGAPSL 

       670        680        690        700        710        720 
TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD ARKFKATIKI ADQGEEGIVE 

       730        740        750 
ADSADGSFMD ELLTLMAAHR VWSRIPKIDK IPA 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII."
von Ossowski I., Mulvey M.R., Leco P.A., Borys A., Loewen P.C.
J. Bacteriol. 173:514-520(1991) [PubMed: 1987146] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10.
Strain: K12.
[2]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]"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.
[4]"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005."
Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L.
Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract]
Cited for: SEQUENCE REVISION TO 198.
[5]"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.
[6]"Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli."
Bravo J., Fita I., Ferrer J.C., Ens W., Hillar A., Switala J., Loewen P.C.
Protein Sci. 6:1016-1023(1997) [PubMed: 9144772] [Abstract]
Cited for: CROSS-LINK 392-HIS--TYR-415.
[7]"Crystal structure of catalase HPII from Escherichia coli."
Bravo J., Verdaguer N., Tormo J., Betzel C., Switala J., Loewen P.C., Fita I.
Structure 3:491-502(1995) [PubMed: 7663946] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[8]"Role of the lateral channel in catalase HPII of Escherichia coli."
Sevinc M.S., Mate M.J., Switala J., Fita I., Loewen P.C.
Protein Sci. 8:490-498(1999) [PubMed: 10091651] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[9]"Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli."
Melik-Adamyan W.R., Bravo J., Carpena X., Switala J., Mate M.J., Fita I., Loewen P.C.
Proteins 44:270-281(2001) [PubMed: 11455600] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

M55161 Genomic DNA. Translation: AAA24039.1.
U00096 Genomic DNA. Translation: AAT48137.1.
AP009048 Genomic DNA. Translation: BAA15513.1.
PIRA39129.
RefSeqAP_002351.1.
YP_025308.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CF9X-ray1.80A/B/C/D1-753[»]
1GG9X-ray1.89A/B/C/D1-753[»]
1GGEX-ray1.89A/B/C/D1-753[»]
1GGFX-ray2.28A/B/C/D1-753[»]
1GGHX-ray2.15A/B/C/D1-753[»]
1GGJX-ray1.92A/B/C/D1-753[»]
1GGKX-ray2.26A/B/C/D1-753[»]
1IPHX-ray2.80A/B/C/D1-753[»]
1P7YX-ray2.40A/B/C/D1-753[»]
1P7ZX-ray2.21A/B/C/D1-753[»]
1P80X-ray1.65A/B/C/D1-753[»]
1P81X-ray1.81A/B/C/D1-753[»]
1QF7X-ray2.20A/B/C/D1-753[»]
1QWSX-ray1.90A/B/C/D1-753[»]
1YE9X-ray2.80A/B/C/D/I/J/K/L75-300[»]
E/F/G/H/M/N/O/P309-567[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:10052N.

Protein family/group databases

PeroxiBase5321. EcoKatE.

2-D gel databases

SWISS-2DPAGEP21179.

Genome annotation databases

GeneID946234.
GenomeReviewsGene locus JW1721 in contig AP009048_GR.
Gene locus b1732 in contig U00096_GR.
KEGGecj:JW1721.
eco:b1732.

Organism-specific databases

EchoBASEEB0504.
EcoGeneEG10509. katE.
CMRSearch...

Phylogenomic databases

HOGENOMP21179.
OMAP21179. FCFEVGK.

Enzyme and pathway databases

BioCycEcoCyc:HYDROPEROXIDII-MON.
MetaCyc:HYDROPEROXIDII-MON.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATE_ECOLI
AccessionPrimary (citable) accession number: P21179
Secondary accession number(s): P76906, P78066, P78168
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: June 16, 2009
This is version 96 of the entry and version 1 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

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