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Protein

Isocitrate dehydrogenase [NADP]

Gene

icd

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

Functioni

Catalytic activityi

Isocitrate + NADP+ = 2-oxoglutarate + CO2 + NADPH.1 Publication

Cofactori

Mg2+, Mn2+Note: Binds 1 Mg(2+) or Mn2+ ion per subunit.

Enzyme regulationi

Inhibition of this enzyme by phosphorylation regulates the branch point between the Krebs cycle and the glyoxylate bypass, which is an alternate route that accumulates carbon for biosynthesis when acetate is the sole carbon source for growth.

Kineticsi

  1. KM=11.4 µM for isocitrate1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei104 – 1041NADP3 Publications
    Binding sitei113 – 1131Substrate1 Publication
    Binding sitei115 – 1151Substrate
    Binding sitei119 – 1191Substrate
    Binding sitei129 – 1291Substrate
    Binding sitei153 – 1531Substrate
    Sitei160 – 1601Critical for catalysis
    Sitei230 – 2301Critical for catalysis
    Metal bindingi307 – 3071Magnesium or manganese3 Publications
    Binding sitei352 – 3521NADP; via amide nitrogen and carbonyl oxygen3 Publications
    Binding sitei391 – 3911NADP3 Publications
    Binding sitei395 – 3951NADP3 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi339 – 3457NADP3 Publications

    GO - Molecular functioni

    • isocitrate dehydrogenase (NADP+) activity Source: UniProtKB
    • magnesium ion binding Source: InterPro
    • NAD binding Source: InterPro

    GO - Biological processi

    • electron transport chain Source: EcoliWiki
    • glyoxylate cycle Source: UniProtKB-KW
    • response to oxidative stress Source: EcoCyc
    • tricarboxylic acid cycle Source: UniProtKB-KW
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Glyoxylate bypass, Tricarboxylic acid cycle

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciEcoCyc:ISOCITDEH-SUBUNIT.
    ECOL316407:JW1122-MONOMER.
    MetaCyc:ISOCITDEH-SUBUNIT.
    BRENDAi1.1.1.42. 2026.
    SABIO-RKP08200.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Isocitrate dehydrogenase [NADP] (EC:1.1.1.42)
    Short name:
    IDH
    Alternative name(s):
    IDP
    NADP(+)-specific ICDH
    Oxalosuccinate decarboxylase
    Gene namesi
    Name:icd
    Synonyms:icdA, icdE
    Ordered Locus Names:b1136, JW1122
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG10489. icd.
    EG10009. icdC.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: EcoliWiki
    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi100 – 1001K → R or E: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi113 – 1131S → D or E: Reduced affinity for isocitrate. 1 Publication
    Mutagenesisi160 – 1601Y → F: Large decrease in activity and a small increase in substrate affinity. 2 Publications
    Mutagenesisi230 – 2301K → M: Decrease in activity and substrate affinity. 2 Publications
    Mutagenesisi242 – 2421K → E: Strongly impairs enzymatic activity. 1 Publication
    Mutagenesisi242 – 2421K → R: Impairs enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 416416Isocitrate dehydrogenase [NADP]PRO_0000083551Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei100 – 1001N6-succinyllysine1 Publication
    Modified residuei113 – 1131Phosphoserine1 Publication
    Modified residuei142 – 1421N6-acetyllysine1 Publication
    Modified residuei242 – 2421N6-succinyllysine1 Publication

    Post-translational modificationi

    Phosphorylation state of this enzyme is controlled by isocitrate dehydrogenase kinase/phosphatase (AceK).1 Publication
    Succinylation probably inhibits enzymatic activity.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    PaxDbiP08200.
    PRIDEiP08200.

    2D gel databases

    SWISS-2DPAGEP08200.

    Interactioni

    Subunit structurei

    Homodimer.4 Publications

    Protein-protein interaction databases

    DIPiDIP-10006N.
    IntActiP08200. 6 interactions.
    STRINGi511145.b1136.

    Structurei

    Secondary structure

    1
    416
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi15 – 173Combined sources
    Beta strandi20 – 223Combined sources
    Beta strandi25 – 328Combined sources
    Helixi38 – 5720Combined sources
    Beta strandi58 – 614Combined sources
    Beta strandi64 – 674Combined sources
    Helixi72 – 787Combined sources
    Helixi86 – 9510Combined sources
    Beta strandi96 – 1005Combined sources
    Beta strandi107 – 1093Combined sources
    Helixi114 – 1218Combined sources
    Beta strandi126 – 1327Combined sources
    Beta strandi140 – 1423Combined sources
    Helixi144 – 1463Combined sources
    Beta strandi148 – 1547Combined sources
    Helixi158 – 1614Combined sources
    Beta strandi163 – 1653Combined sources
    Helixi170 – 18112Combined sources
    Beta strandi196 – 1983Combined sources
    Helixi203 – 21917Combined sources
    Beta strandi223 – 2297Combined sources
    Turni231 – 2333Combined sources
    Turni235 – 2373Combined sources
    Helixi238 – 25316Combined sources
    Beta strandi256 – 2583Combined sources
    Beta strandi259 – 2624Combined sources
    Beta strandi264 – 2674Combined sources
    Turni269 – 2713Combined sources
    Beta strandi274 – 2818Combined sources
    Helixi282 – 29110Combined sources
    Helixi293 – 2953Combined sources
    Beta strandi298 – 3014Combined sources
    Helixi303 – 31614Combined sources
    Turni320 – 3223Combined sources
    Beta strandi326 – 3283Combined sources
    Beta strandi333 – 3364Combined sources
    Helixi343 – 3453Combined sources
    Turni346 – 3494Combined sources
    Helixi354 – 36613Combined sources
    Helixi370 – 38516Combined sources
    Beta strandi388 – 3903Combined sources
    Helixi391 – 3944Combined sources
    Beta strandi397 – 3993Combined sources
    Beta strandi401 – 4033Combined sources
    Helixi405 – 41410Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AI2X-ray1.90A1-416[»]
    1AI3X-ray1.90A1-416[»]
    1BL5X-ray2.50A3-416[»]
    1CW1X-ray2.10A1-416[»]
    1CW4X-ray2.10A1-416[»]
    1CW7X-ray2.60A1-416[»]
    1GROX-ray2.50A1-416[»]
    1GRPX-ray2.50A1-416[»]
    1HJ6X-ray2.00A1-416[»]
    1IDCX-ray2.50A1-416[»]
    1IDDX-ray2.50A1-416[»]
    1IDEX-ray2.50A1-416[»]
    1IDFX-ray2.50A1-416[»]
    1IKAX-ray2.70A1-416[»]
    1ISOX-ray1.90A1-416[»]
    1P8FX-ray1.85A1-416[»]
    1PB1X-ray1.70A1-416[»]
    1PB3X-ray1.70A1-416[»]
    1SJSX-ray2.42A1-416[»]
    3ICDX-ray2.50A1-416[»]
    3LCBX-ray2.90C/D1-416[»]
    4AJ3X-ray1.90A1-416[»]
    4AJAX-ray1.80A1-416[»]
    4AJBX-ray1.90A1-416[»]
    4AJCX-ray2.30A1-416[»]
    4AJRX-ray2.69A1-416[»]
    4AJSX-ray1.80A1-416[»]
    4BNPX-ray2.00A1-416[»]
    4ICDX-ray2.50A1-416[»]
    4P69X-ray3.30C/D2-416[»]
    5ICDX-ray2.50A1-416[»]
    6ICDX-ray2.80A1-416[»]
    7ICDX-ray2.40A1-416[»]
    8ICDX-ray2.50A1-416[»]
    9ICDX-ray2.50A1-416[»]
    ProteinModelPortaliP08200.
    SMRiP08200. Positions 1-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP08200.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0538.
    HOGENOMiHOG000021113.
    InParanoidiP08200.
    KOiK00031.
    OMAiFRDWGYE.
    OrthoDBiEOG6SNDTP.
    PhylomeDBiP08200.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004439. Isocitrate_DH_NADP_dimer_prok.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11835. PTHR11835. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00183. prok_nadp_idh. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P08200-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MESKVVVPAQ GKKITLQNGK LNVPENPIIP YIEGDGIGVD VTPAMLKVVD
    60 70 80 90 100
    AAVEKAYKGE RKISWMEIYT GEKSTQVYGQ DVWLPAETLD LIREYRVAIK
    110 120 130 140 150
    GPLTTPVGGG IRSLNVALRQ ELDLYICLRP VRYYQGTPSP VKHPELTDMV
    160 170 180 190 200
    IFRENSEDIY AGIEWKADSA DAEKVIKFLR EEMGVKKIRF PEHCGIGIKP
    210 220 230 240 250
    CSEEGTKRLV RAAIEYAIAN DRDSVTLVHK GNIMKFTEGA FKDWGYQLAR
    260 270 280 290 300
    EEFGGELIDG GPWLKVKNPN TGKEIVIKDV IADAFLQQIL LRPAEYDVIA
    310 320 330 340 350
    CMNLNGDYIS DALAAQVGGI GIAPGANIGD ECALFEATHG TAPKYAGQDK
    360 370 380 390 400
    VNPGSIILSA EMMLRHMGWT EAADLIVKGM EGAINAKTVT YDFERLMDGA
    410
    KLLKCSEFGD AIIENM
    Length:416
    Mass (Da):45,757
    Last modified:August 1, 1988 - v1
    Checksum:i9A02E707C3B4FDD9
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02799 Genomic DNA. Translation: AAA24006.1.
    U00096 Genomic DNA. Translation: AAC74220.1.
    AP009048 Genomic DNA. Translation: BAA35958.1.
    AF017587 Genomic DNA. Translation: AAC45887.1.
    PIRiA28482. DCECIS.
    RefSeqiNP_415654.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC74220; AAC74220; b1136.
    BAA35958; BAA35958; BAA35958.
    GeneIDi945702.
    KEGGiecj:Y75_p1106.
    eco:b1136.
    PATRICi32117521. VBIEscCol129921_1183.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    J02799 Genomic DNA. Translation: AAA24006.1.
    U00096 Genomic DNA. Translation: AAC74220.1.
    AP009048 Genomic DNA. Translation: BAA35958.1.
    AF017587 Genomic DNA. Translation: AAC45887.1.
    PIRiA28482. DCECIS.
    RefSeqiNP_415654.1. NC_000913.3.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AI2X-ray1.90A1-416[»]
    1AI3X-ray1.90A1-416[»]
    1BL5X-ray2.50A3-416[»]
    1CW1X-ray2.10A1-416[»]
    1CW4X-ray2.10A1-416[»]
    1CW7X-ray2.60A1-416[»]
    1GROX-ray2.50A1-416[»]
    1GRPX-ray2.50A1-416[»]
    1HJ6X-ray2.00A1-416[»]
    1IDCX-ray2.50A1-416[»]
    1IDDX-ray2.50A1-416[»]
    1IDEX-ray2.50A1-416[»]
    1IDFX-ray2.50A1-416[»]
    1IKAX-ray2.70A1-416[»]
    1ISOX-ray1.90A1-416[»]
    1P8FX-ray1.85A1-416[»]
    1PB1X-ray1.70A1-416[»]
    1PB3X-ray1.70A1-416[»]
    1SJSX-ray2.42A1-416[»]
    3ICDX-ray2.50A1-416[»]
    3LCBX-ray2.90C/D1-416[»]
    4AJ3X-ray1.90A1-416[»]
    4AJAX-ray1.80A1-416[»]
    4AJBX-ray1.90A1-416[»]
    4AJCX-ray2.30A1-416[»]
    4AJRX-ray2.69A1-416[»]
    4AJSX-ray1.80A1-416[»]
    4BNPX-ray2.00A1-416[»]
    4ICDX-ray2.50A1-416[»]
    4P69X-ray3.30C/D2-416[»]
    5ICDX-ray2.50A1-416[»]
    6ICDX-ray2.80A1-416[»]
    7ICDX-ray2.40A1-416[»]
    8ICDX-ray2.50A1-416[»]
    9ICDX-ray2.50A1-416[»]
    ProteinModelPortaliP08200.
    SMRiP08200. Positions 1-416.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-10006N.
    IntActiP08200. 6 interactions.
    STRINGi511145.b1136.

    2D gel databases

    SWISS-2DPAGEP08200.

    Proteomic databases

    PaxDbiP08200.
    PRIDEiP08200.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC74220; AAC74220; b1136.
    BAA35958; BAA35958; BAA35958.
    GeneIDi945702.
    KEGGiecj:Y75_p1106.
    eco:b1136.
    PATRICi32117521. VBIEscCol129921_1183.

    Organism-specific databases

    EchoBASEiEB0484.
    EcoGeneiEG10489. icd.
    EG10009. icdC.

    Phylogenomic databases

    eggNOGiCOG0538.
    HOGENOMiHOG000021113.
    InParanoidiP08200.
    KOiK00031.
    OMAiFRDWGYE.
    OrthoDBiEOG6SNDTP.
    PhylomeDBiP08200.

    Enzyme and pathway databases

    BioCyciEcoCyc:ISOCITDEH-SUBUNIT.
    ECOL316407:JW1122-MONOMER.
    MetaCyc:ISOCITDEH-SUBUNIT.
    BRENDAi1.1.1.42. 2026.
    SABIO-RKP08200.

    Miscellaneous databases

    EvolutionaryTraceiP08200.
    PROiP08200.

    Family and domain databases

    Gene3Di3.40.718.10. 1 hit.
    InterProiIPR019818. IsoCit/isopropylmalate_DH_CS.
    IPR001804. Isocitrate/isopropylmalate_DH.
    IPR004439. Isocitrate_DH_NADP_dimer_prok.
    IPR024084. IsoPropMal-DH-like_dom.
    [Graphical view]
    PANTHERiPTHR11835. PTHR11835. 1 hit.
    PfamiPF00180. Iso_dh. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00183. prok_nadp_idh. 1 hit.
    PROSITEiPS00470. IDH_IMDH. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Inactivation of isocitrate dehydrogenase by phosphorylation is mediated by the negative charge of the phosphate."
      Thorsness P.E., Koshland D.E. Jr.
      J. Biol. Chem. 262:10422-10425(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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. "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.
    5. "Evolutionary genetics of the isocitrate dehydrogenase gene (icd) in Escherichia coli and Salmonella enterica."
      Wang F.-S., Whittam T.S., Selander R.K.
      J. Bacteriol. 179:6551-6559(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 11-414.
      Strain: CH734.
    6. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
      Link A.J., Robison K., Church G.M.
      Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-12.
      Strain: K12 / EMG2.
    7. "Mutational analysis of the catalytic residues lysine 230 and tyrosine 160 in the NADP(+)-dependent isocitrate dehydrogenase from Escherichia coli."
      Lee M.E., Dyer D.H., Klein O.D., Bolduc J.M., Stoddard B.L., Koshland D.E. Jr.
      Biochemistry 34:378-384(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME KINETICS, MUTAGENESIS OF TYR-160 AND LYS-230.
    8. "Escherichia coli proteome analysis using the gene-protein database."
      VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
      Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY 2D-GEL.
    9. "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
      Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
      Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-142, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
    10. "Identification of lysine succinylation as a new post-translational modification."
      Zhang Z., Tan M., Xie Z., Dai L., Chen Y., Zhao Y.
      Nat. Chem. Biol. 7:58-63(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, SUCCINYLATION AT LYS-100 AND LYS-242, MUTAGENESIS OF LYS-100 AND LYS-242.
      Strain: K12.
    11. "Regulation of an enzyme by phosphorylation at the active site."
      Hurley J.H., Dean A.M., Sohl J.L., Koshland D.E. Jr., Stroud R.M.
      Science 249:1012-1016(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ISOCITRATE AND MAGNESIUM, PHOSPHORYLATION AT SER-113, MUTAGENESIS OF SER-113.
    12. "Mutagenesis and Laue structures of enzyme intermediates: isocitrate dehydrogenase."
      Bolduc J.M., Dyer D.H., Scott W.G., Singer P., Sweet R.M., Koshland D.E. Jr., Stoddard B.L.
      Science 268:1312-1318(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH ISOCITRATE; NADP AND MAGNESIUM, MUTAGENESIS OF TYR-160 AND LYS-230, BIOPHYSICOCHEMICAL PROPERTIES.
    13. "Structure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenase."
      Hurley J.H., Thorsness P.E., Ramalingam V., Helmers N.H., Koshland D.E. Jr., Stroud R.M.
      Proc. Natl. Acad. Sci. U.S.A. 86:8635-8639(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH NADP, SUBUNIT.
    14. "Active site water molecules revealed in the 2.1 A resolution structure of a site-directed mutant of isocitrate dehydrogenase."
      Cherbavaz D.B., Lee M.E., Stroud R.M., Koshland D.E. Jr.
      J. Mol. Biol. 295:377-385(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF MUTANT MET-230.
    15. "Structural basis for a change in substrate specificity: crystal structure of S113E isocitrate dehydrogenase in a complex with isopropylmalate, Mg2+, and NADP."
      Doyle S.A., Beernink P.T., Koshland D.E. Jr.
      Biochemistry 40:4234-4241(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANT GLU-113 IN COMPLEX WITH SUBSTRATE ANALOG; MAGNESIUM AND NADP.

    Entry informationi

    Entry nameiIDH_ECOLI
    AccessioniPrimary (citable) accession number: P08200
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: August 1, 1988
    Last modified: June 24, 2015
    This is version 151 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

    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 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.