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P21179 (CATE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length753 AA.
Sequence statusComplete.
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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-549879,EBI-549879

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 [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] [Europe PMC] [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] [Europe PMC] [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 277:1453-1462(1997) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55161 Genomic DNA. Translation: AAA24039.1.
U00096 Genomic DNA. Translation: AAT48137.1.
AP009048 Genomic DNA. Translation: BAA15513.1.
PIRA39129.
RefSeqYP_025308.1. NC_000913.3.
YP_489993.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
3P9PX-ray1.50A/B/C/D1-753[»]
3P9QX-ray1.48A/B/C/D1-753[»]
3P9RX-ray1.90A/B/C/D1-753[»]
3P9SX-ray1.90A/B/C/D1-753[»]
3PQ2X-ray1.79A/B/C/D1-753[»]
3PQ3X-ray1.79A/B/C/D1-753[»]
3PQ4X-ray1.79A/B/C/D1-753[»]
3PQ5X-ray1.80A/B/C/D1-753[»]
3PQ6X-ray1.80A/B/C/D1-753[»]
3PQ7X-ray1.80A/B/C/D1-753[»]
3PQ8X-ray1.80A/B/C/D1-753[»]
3TTTX-ray1.58A/B/C/D1-753[»]
3TTUX-ray1.89A/B/C/D1-753[»]
3TTVX-ray1.45A/B/C/D1-753[»]
3TTWX-ray1.62A/B/C/D1-753[»]
3TTXX-ray1.74A/B/C/D1-753[»]
3VU3X-ray2.85A1-753[»]
4BFLX-ray1.64A/B/C/D1-753[»]
4ENPX-ray1.50A/B/C/D1-753[»]
4ENQX-ray1.90A/B/C/D1-753[»]
4ENRX-ray1.60A/B/C/D1-753[»]
4ENSX-ray1.60A/B/C/D1-753[»]
4ENTX-ray1.70A/B/C/D1-753[»]
4ENUX-ray1.70A/B/C/D1-753[»]
4ENVX-ray1.70A/B/C/D1-753[»]
4ENWX-ray1.90A/B/C/D1-753[»]
ProteinModelPortalP21179.
SMRP21179. Positions 28-753.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid850594. 1 interaction.
DIPDIP-10052N.
IntActP21179. 11 interactions.
MINTMINT-1247982.
STRING511145.b1732.

Protein family/group databases

PeroxiBase5321. EcoKat05.

2D gel databases

SWISS-2DPAGEP21179.

Proteomic databases

PaxDbP21179.
PRIDEP21179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT48137; AAT48137; b1732.
BAA15513; BAA15513; BAA15513.
GeneID12934065.
946234.
KEGGecj:Y75_p1707.
eco:b1732.
PATRIC32118771. VBIEscCol129921_1803.

Organism-specific databases

EchoBASEEB0504.
EcoGeneEG10509. katE.

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087851.
KOK03781.
OMAESFGDHF.
OrthoDBEOG6P5Z9F.
PhylomeDBP21179.

Enzyme and pathway databases

BioCycEcoCyc:HYDROPEROXIDII-MONOMER.
ECOL316407:JW1721-MONOMER.
MetaCyc:HYDROPEROXIDII-MONOMER.
SABIO-RKP21179.

Gene expression databases

GenevestigatorP21179.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024712. Catalase_clade2.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
IPR029062. Class_I_gatase-like.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038927. Catalase_clade2. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP21179.
PROP21179.

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: July 9, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene