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P21179

- CATE_ECOLI

UniProt

P21179 - CATE_ECOLI

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Protein

Catalase HPII

Gene

katE

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Heme group.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei128 – 1281PROSITE-ProRule annotation
Active sitei201 – 2011PROSITE-ProRule annotation
Metal bindingi415 – 4151Iron (heme axial ligand)

GO - Molecular functioni

  1. catalase activity Source: EcoCyc
  2. heme binding Source: EcoliWiki
  3. identical protein binding Source: IntAct
  4. iron ion binding Source: EcoliWiki

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. hydrogen peroxide catabolic process Source: EcoliWiki
  3. hyperosmotic response Source: EcoCyc
  4. 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10509. katE.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: EcoliWiki
  2. cytosol Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 753753Catalase HPIIPRO_0000084971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki392 ↔ 4153'-histidyl-3-tyrosine (His-Tyr)

Proteomic databases

PaxDbiP21179.
PRIDEiP21179.

2D gel databases

SWISS-2DPAGEP21179.

Expressioni

Inductioni

By entry into stationary phase.

Gene expression databases

GenevestigatoriP21179.

Interactioni

Subunit structurei

Homotetramer.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi850594. 1 interaction.
DIPiDIP-10052N.
IntActiP21179. 11 interactions.
MINTiMINT-1247982.
STRINGi511145.b1732.

Structurei

Secondary structure

1
753
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi19 – 224
Beta strandi32 – 343
Turni45 – 473
Helixi53 – 564
Helixi63 – 675
Helixi68 – 703
Beta strandi87 – 893
Beta strandi95 – 984
Helixi108 – 11811
Beta strandi126 – 1283
Beta strandi130 – 14213
Turni145 – 1473
Helixi151 – 1533
Beta strandi160 – 1678
Beta strandi169 – 1713
Beta strandi179 – 1813
Beta strandi184 – 1918
Beta strandi194 – 20512
Helixi211 – 2133
Helixi214 – 2218
Turni225 – 2273
Helixi237 – 2459
Helixi247 – 2493
Helixi250 – 2578
Helixi259 – 2613
Beta strandi262 – 2643
Helixi266 – 2683
Beta strandi277 – 2804
Beta strandi286 – 29510
Helixi304 – 31310
Helixi317 – 32812
Beta strandi333 – 34210
Helixi343 – 3453
Beta strandi349 – 3513
Turni362 – 3643
Beta strandi368 – 37710
Helixi382 – 3854
Turni386 – 3883
Helixi406 – 42318
Helixi428 – 4303
Helixi432 – 4343
Beta strandi459 – 4624
Turni465 – 4684
Beta strandi477 – 4793
Beta strandi488 – 4958
Helixi499 – 5013
Helixi506 – 5149
Helixi517 – 53216
Helixi537 – 54812
Helixi552 – 56110
Helixi568 – 5714
Helixi586 – 5883
Beta strandi590 – 5934
Beta strandi602 – 6065
Beta strandi609 – 6113
Helixi613 – 62513
Beta strandi629 – 64113
Beta strandi647 – 6493
Turni654 – 6563
Helixi659 – 6613
Beta strandi663 – 6675
Helixi672 – 6743
Turni675 – 6773
Helixi679 – 69012
Beta strandi695 – 6984
Helixi699 – 70810
Beta strandi718 – 7236
Helixi726 – 73712
Helixi742 – 7443
Helixi745 – 7484
Beta strandi749 – 7513

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP21179.
SMRiP21179. Positions 28-753.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21179.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family. HPII subfamily.Curated

Phylogenomic databases

eggNOGiCOG0753.
HOGENOMiHOG000087851.
InParanoidiP21179.
KOiK03781.
OMAiESFGDHF.
OrthoDBiEOG6P5Z9F.
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:
EMBL
GenBank
DDBJ
Links Updated
M55161 Genomic DNA. Translation: AAA24039.1.
U00096 Genomic DNA. Translation: AAT48137.1.
AP009048 Genomic DNA. Translation: BAA15513.1.
PIRiA39129.
RefSeqiYP_025308.1. NC_000913.3.
YP_489993.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAT48137; AAT48137; b1732.
BAA15513; BAA15513; BAA15513.
GeneIDi12934065.
946234.
KEGGiecj:Y75_p1707.
eco:b1732.
PATRICi32118771. VBIEscCol129921_1803.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55161 Genomic DNA. Translation: AAA24039.1 .
U00096 Genomic DNA. Translation: AAT48137.1 .
AP009048 Genomic DNA. Translation: BAA15513.1 .
PIRi A39129.
RefSeqi YP_025308.1. NC_000913.3.
YP_489993.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1CF9 X-ray 1.80 A/B/C/D 1-753 [» ]
1GG9 X-ray 1.89 A/B/C/D 1-753 [» ]
1GGE X-ray 1.89 A/B/C/D 1-753 [» ]
1GGF X-ray 2.28 A/B/C/D 1-753 [» ]
1GGH X-ray 2.15 A/B/C/D 1-753 [» ]
1GGJ X-ray 1.92 A/B/C/D 1-753 [» ]
1GGK X-ray 2.26 A/B/C/D 1-753 [» ]
1IPH X-ray 2.80 A/B/C/D 1-753 [» ]
1P7Y X-ray 2.40 A/B/C/D 1-753 [» ]
1P7Z X-ray 2.21 A/B/C/D 1-753 [» ]
1P80 X-ray 1.65 A/B/C/D 1-753 [» ]
1P81 X-ray 1.81 A/B/C/D 1-753 [» ]
1QF7 X-ray 2.20 A/B/C/D 1-753 [» ]
1QWS X-ray 1.90 A/B/C/D 1-753 [» ]
1YE9 X-ray 2.80 A/B/C/D/I/J/K/L 75-300 [» ]
E/F/G/H/M/N/O/P 309-567 [» ]
3P9P X-ray 1.50 A/B/C/D 1-753 [» ]
3P9Q X-ray 1.48 A/B/C/D 1-753 [» ]
3P9R X-ray 1.90 A/B/C/D 1-753 [» ]
3P9S X-ray 1.90 A/B/C/D 1-753 [» ]
3PQ2 X-ray 1.79 A/B/C/D 1-753 [» ]
3PQ3 X-ray 1.79 A/B/C/D 1-753 [» ]
3PQ4 X-ray 1.79 A/B/C/D 1-753 [» ]
3PQ5 X-ray 1.80 A/B/C/D 1-753 [» ]
3PQ6 X-ray 1.80 A/B/C/D 1-753 [» ]
3PQ7 X-ray 1.80 A/B/C/D 1-753 [» ]
3PQ8 X-ray 1.80 A/B/C/D 1-753 [» ]
3TTT X-ray 1.58 A/B/C/D 1-753 [» ]
3TTU X-ray 1.89 A/B/C/D 1-753 [» ]
3TTV X-ray 1.45 A/B/C/D 1-753 [» ]
3TTW X-ray 1.62 A/B/C/D 1-753 [» ]
3TTX X-ray 1.74 A/B/C/D 1-753 [» ]
3VU3 X-ray 2.85 A 1-753 [» ]
4BFL X-ray 1.64 A/B/C/D 1-753 [» ]
4ENP X-ray 1.50 A/B/C/D 1-753 [» ]
4ENQ X-ray 1.90 A/B/C/D 1-753 [» ]
4ENR X-ray 1.60 A/B/C/D 1-753 [» ]
4ENS X-ray 1.60 A/B/C/D 1-753 [» ]
4ENT X-ray 1.70 A/B/C/D 1-753 [» ]
4ENU X-ray 1.70 A/B/C/D 1-753 [» ]
4ENV X-ray 1.70 A/B/C/D 1-753 [» ]
4ENW X-ray 1.90 A/B/C/D 1-753 [» ]
ProteinModelPortali P21179.
SMRi P21179. Positions 28-753.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 850594. 1 interaction.
DIPi DIP-10052N.
IntActi P21179. 11 interactions.
MINTi MINT-1247982.
STRINGi 511145.b1732.

Protein family/group databases

PeroxiBasei 5321. EcoKat05.

2D gel databases

SWISS-2DPAGE P21179.

Proteomic databases

PaxDbi P21179.
PRIDEi P21179.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT48137 ; AAT48137 ; b1732 .
BAA15513 ; BAA15513 ; BAA15513 .
GeneIDi 12934065.
946234.
KEGGi ecj:Y75_p1707.
eco:b1732.
PATRICi 32118771. VBIEscCol129921_1803.

Organism-specific databases

EchoBASEi EB0504.
EcoGenei EG10509. katE.

Phylogenomic databases

eggNOGi COG0753.
HOGENOMi HOG000087851.
InParanoidi P21179.
KOi K03781.
OMAi ESFGDHF.
OrthoDBi EOG6P5Z9F.
PhylomeDBi P21179.

Enzyme and pathway databases

BioCyci EcoCyc:HYDROPEROXIDII-MONOMER.
ECOL316407:JW1721-MONOMER.
MetaCyc:HYDROPEROXIDII-MONOMER.
SABIO-RK P21179.

Miscellaneous databases

EvolutionaryTracei P21179.
PROi P21179.

Gene expression databases

Genevestigatori P21179.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
3.40.50.880. 1 hit.
InterProi IPR018028. 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 ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038927. Catalase_clade2. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF52317. SSF52317. 1 hit.
SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. 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).

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: October 29, 2014
This is version 147 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

External Data

Dasty 3