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P21179

- CATE_ECOLI

UniProt

P21179 - CATE_ECOLI

Protein

Catalase HPII

Gene

katE

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 146 (01 Oct 2014)
      Sequence version 1 (01 May 1991)
      Previous versions | rss
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    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

    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

    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.
    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

    MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT    50
    APGSLKAPDT RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR 100
    GPTLLEDFIL REKITHFDHE RIPERIVHAR GSAAHGYFQP YKSLSDITKA 150
    DFLSDPNKIT PVFVRFSTVQ GGAGSADTVR DIRGFATKFY TEEGIFDLVG 200
    NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW DYVSLQPETL 250
    HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA 300
    SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD 350
    FDLLDPTKLI PEELVPVQRV GKMVLNRNPD NFFAENEQAA FHPGHIVPGL 400
    DFTNDPLLQG RLFSYTDTQI SRLGGPNFHE IPINRPTCPY HNFQRDGMHR 450
    MGIDTNPANY EPNSINDNWP RETPPGPKRG GFESYQERVE GNKVRERSPS 500
    FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR ERVVDQLAHI 550
    DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YAIPDGDVKG 600
    RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI 650
    AATFAGAPSL TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD 700
    ARKFKATIKI ADQGEEGIVE ADSADGSFMD ELLTLMAAHR VWSRIPKIDK 750
    IPA 753
    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.
    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

    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 1, 2014
    This is version 146 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