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Protein

Catalase HPII

Gene

katE

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei128PROSITE-ProRule annotation1
Active sitei201PROSITE-ProRule annotation1
Metal bindingi415Iron (heme axial ligand)1

GO - Molecular functioni

  • catalase activity Source: CACAO
  • heme binding Source: EcoliWiki
  • identical protein binding Source: EcoCyc
  • iron ion binding Source: EcoliWiki

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • hydrogen peroxide catabolic process Source: EcoliWiki
  • hyperosmotic response Source: EcoCyc
  • response to hydrogen peroxide Source: GO_Central
  • response to oxidative stress Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

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

Protein family/group databases

PeroxiBasei5321. EcoKat05.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase HPII (EC:1.11.1.6)
Alternative name(s):
Hydroxyperoxidase II
Gene namesi
Name:katE
Ordered Locus Names:b1732, JW1721
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10509. katE.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: EcoliWiki
  • cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000849711 – 753Catalase HPIIAdd BLAST753

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki392 ↔ 4153'-histidyl-3-tyrosine (His-Tyr)

Proteomic databases

EPDiP21179.
PaxDbiP21179.
PRIDEiP21179.

2D gel databases

SWISS-2DPAGEP21179.

Expressioni

Inductioni

By entry into stationary phase.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-549879,EBI-549879

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4263059. 28 interactors.
850594. 1 interactor.
DIPiDIP-10052N.
IntActiP21179. 11 interactors.
MINTiMINT-1247982.
STRINGi511145.b1732.

Structurei

Secondary structure

1753
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi19 – 22Combined sources4
Beta strandi32 – 34Combined sources3
Turni45 – 47Combined sources3
Helixi53 – 56Combined sources4
Helixi63 – 67Combined sources5
Helixi68 – 70Combined sources3
Beta strandi87 – 89Combined sources3
Beta strandi95 – 98Combined sources4
Helixi108 – 118Combined sources11
Beta strandi126 – 128Combined sources3
Beta strandi130 – 142Combined sources13
Turni145 – 147Combined sources3
Helixi151 – 153Combined sources3
Beta strandi160 – 167Combined sources8
Beta strandi169 – 171Combined sources3
Beta strandi179 – 181Combined sources3
Beta strandi184 – 191Combined sources8
Beta strandi194 – 205Combined sources12
Helixi211 – 213Combined sources3
Helixi214 – 221Combined sources8
Turni225 – 227Combined sources3
Helixi237 – 245Combined sources9
Helixi247 – 249Combined sources3
Helixi250 – 257Combined sources8
Helixi259 – 261Combined sources3
Beta strandi262 – 264Combined sources3
Helixi266 – 268Combined sources3
Beta strandi277 – 280Combined sources4
Beta strandi286 – 295Combined sources10
Helixi304 – 313Combined sources10
Helixi317 – 328Combined sources12
Beta strandi333 – 342Combined sources10
Helixi343 – 345Combined sources3
Beta strandi349 – 351Combined sources3
Turni362 – 364Combined sources3
Beta strandi368 – 377Combined sources10
Helixi382 – 385Combined sources4
Turni386 – 388Combined sources3
Helixi406 – 423Combined sources18
Helixi428 – 430Combined sources3
Helixi432 – 434Combined sources3
Beta strandi459 – 462Combined sources4
Turni465 – 468Combined sources4
Beta strandi477 – 479Combined sources3
Beta strandi488 – 495Combined sources8
Helixi499 – 501Combined sources3
Helixi506 – 514Combined sources9
Helixi517 – 532Combined sources16
Helixi537 – 548Combined sources12
Helixi552 – 561Combined sources10
Helixi568 – 571Combined sources4
Helixi586 – 588Combined sources3
Beta strandi590 – 593Combined sources4
Beta strandi602 – 606Combined sources5
Beta strandi609 – 611Combined sources3
Helixi613 – 625Combined sources13
Beta strandi629 – 641Combined sources13
Beta strandi647 – 649Combined sources3
Turni654 – 656Combined sources3
Helixi659 – 661Combined sources3
Beta strandi663 – 667Combined sources5
Helixi672 – 674Combined sources3
Turni675 – 677Combined sources3
Helixi679 – 690Combined sources12
Beta strandi695 – 698Combined sources4
Helixi699 – 708Combined sources10
Beta strandi718 – 723Combined sources6
Helixi726 – 737Combined sources12
Helixi742 – 744Combined sources3
Helixi745 – 748Combined sources4
Beta strandi749 – 751Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BV2X-ray1.53P/Q/R/S1-753[»]
ProteinModelPortaliP21179.
SMRiP21179.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21179.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family. HPII subfamily.Curated

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.
HOGENOMiHOG000087851.
InParanoidiP21179.
KOiK03781.
OMAiHNEIPTG.
PhylomeDBiP21179.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P21179-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT
60 70 80 90 100
APGSLKAPDT RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR
110 120 130 140 150
GPTLLEDFIL REKITHFDHE RIPERIVHAR GSAAHGYFQP YKSLSDITKA
160 170 180 190 200
DFLSDPNKIT PVFVRFSTVQ GGAGSADTVR DIRGFATKFY TEEGIFDLVG
210 220 230 240 250
NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW DYVSLQPETL
260 270 280 290 300
HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA
310 320 330 340 350
SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD
360 370 380 390 400
FDLLDPTKLI PEELVPVQRV GKMVLNRNPD NFFAENEQAA FHPGHIVPGL
410 420 430 440 450
DFTNDPLLQG RLFSYTDTQI SRLGGPNFHE IPINRPTCPY HNFQRDGMHR
460 470 480 490 500
MGIDTNPANY EPNSINDNWP RETPPGPKRG GFESYQERVE GNKVRERSPS
510 520 530 540 550
FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR ERVVDQLAHI
560 570 580 590 600
DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YAIPDGDVKG
610 620 630 640 650
RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI
660 670 680 690 700
AATFAGAPSL TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD
710 720 730 740 750
ARKFKATIKI ADQGEEGIVE ADSADGSFMD ELLTLMAAHR VWSRIPKIDK

IPA
Length:753
Mass (Da):84,163
Last modified:May 1, 1991 - v1
Checksum:i1F034E4866A70FB9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55161 Genomic DNA. Translation: AAA24039.1.
U00096 Genomic DNA. Translation: AAT48137.1.
AP009048 Genomic DNA. Translation: BAA15513.1.
PIRiA39129.
RefSeqiWP_000077872.1. NZ_LN832404.1.
YP_025308.1. NC_000913.3.

Genome annotation databases

EnsemblBacteriaiAAT48137; AAT48137; b1732.
BAA15513; BAA15513; BAA15513.
GeneIDi946234.
KEGGiecj:JW1721.
eco:b1732.
PATRICi32118771. VBIEscCol129921_1803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55161 Genomic DNA. Translation: AAA24039.1.
U00096 Genomic DNA. Translation: AAT48137.1.
AP009048 Genomic DNA. Translation: BAA15513.1.
PIRiA39129.
RefSeqiWP_000077872.1. NZ_LN832404.1.
YP_025308.1. NC_000913.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5BV2X-ray1.53P/Q/R/S1-753[»]
ProteinModelPortaliP21179.
SMRiP21179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263059. 28 interactors.
850594. 1 interactor.
DIPiDIP-10052N.
IntActiP21179. 11 interactors.
MINTiMINT-1247982.
STRINGi511145.b1732.

Protein family/group databases

PeroxiBasei5321. EcoKat05.

2D gel databases

SWISS-2DPAGEP21179.

Proteomic databases

EPDiP21179.
PaxDbiP21179.
PRIDEiP21179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAT48137; AAT48137; b1732.
BAA15513; BAA15513; BAA15513.
GeneIDi946234.
KEGGiecj:JW1721.
eco:b1732.
PATRICi32118771. VBIEscCol129921_1803.

Organism-specific databases

EchoBASEiEB0504.
EcoGeneiEG10509. katE.

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.
HOGENOMiHOG000087851.
InParanoidiP21179.
KOiK03781.
OMAiHNEIPTG.
PhylomeDBiP21179.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiP21179.
PROiP21179.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038927. Catalase_clade2. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATE_ECOLI
AccessioniPrimary (citable) accession number: P21179
Secondary accession number(s): P76906, P78066, P78168
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 2, 2016
This is version 163 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.