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P0AB80

- ILVE_ECOLI

UniProt

P0AB80 - ILVE_ECOLI

Protein

Branched-chain-amino-acid aminotransferase

Gene

ilvE

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 83 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Acts on leucine, isoleucine and valine.

    Catalytic activityi

    L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate.
    L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate.
    L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate.

    Cofactori

    Pyridoxal phosphate.

    Pathwayi

    GO - Molecular functioni

    1. branched-chain-amino-acid transaminase activity Source: EcoCyc
    2. identical protein binding Source: EcoCyc
    3. L-isoleucine transaminase activity Source: UniProtKB-EC
    4. L-leucine transaminase activity Source: UniProtKB-EC
    5. L-valine transaminase activity Source: UniProtKB-EC

    GO - Biological processi

    1. aspartate biosynthetic process Source: EcoliWiki
    2. isoleucine biosynthetic process Source: UniProtKB-UniPathway
    3. leucine biosynthetic process Source: EcoCyc
    4. valine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Branched-chain amino acid biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
    ECOL316407:JW5606-MONOMER.
    MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
    UniPathwayiUPA00047; UER00058.
    UPA00048; UER00073.
    UPA00049; UER00062.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Branched-chain-amino-acid aminotransferase (EC:2.6.1.42)
    Short name:
    BCAT
    Alternative name(s):
    Transaminase B
    Gene namesi
    Name:ilvE
    Ordered Locus Names:b3770, JW5606
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10497. ilvE.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed
    Chaini2 – 309308Branched-chain-amino-acid aminotransferasePRO_0000103262Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei160 – 1601N6-(pyridoxal phosphate)lysine

    Proteomic databases

    PaxDbiP0AB80.
    PRIDEiP0AB80.

    2D gel databases

    SWISS-2DPAGEP0AB80.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AB80.

    Interactioni

    Subunit structurei

    Homohexamer.

    Protein-protein interaction databases

    DIPiDIP-10022N.
    STRINGi511145.b3770.

    Structurei

    Secondary structure

    1
    309
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 115
    Beta strandi14 – 174
    Helixi18 – 203
    Helixi28 – 325
    Beta strandi35 – 373
    Beta strandi40 – 434
    Beta strandi48 – 525
    Helixi54 – 6815
    Helixi76 – 8914
    Beta strandi93 – 10311
    Beta strandi108 – 1114
    Beta strandi118 – 1258
    Helixi135 – 1384
    Beta strandi140 – 1445
    Turni152 – 1543
    Beta strandi157 – 1593
    Helixi162 – 1643
    Helixi165 – 17713
    Beta strandi181 – 1866
    Beta strandi190 – 1956
    Beta strandi198 – 2047
    Beta strandi207 – 2104
    Helixi213 – 2153
    Helixi221 – 23212
    Beta strandi237 – 2393
    Helixi246 – 2494
    Beta strandi251 – 2577
    Turni258 – 2603
    Beta strandi261 – 2688
    Helixi274 – 2763
    Helixi280 – 29011
    Turni291 – 2944
    Beta strandi295 – 2973
    Beta strandi304 – 3063

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A3GX-ray2.50A/B/C2-309[»]
    1I1KX-ray2.10A/B/C1-309[»]
    1I1LX-ray2.40A/B/C1-309[»]
    1I1MX-ray2.40A/B/C1-309[»]
    1IYDX-ray2.15A/B/C1-309[»]
    1IYEX-ray1.82A/B/C1-309[»]
    ProteinModelPortaliP0AB80.
    SMRiP0AB80. Positions 5-308.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP0AB80.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0115.
    HOGENOMiHOG000276706.
    KOiK00826.
    OMAiFPWGSYL.
    OrthoDBiEOG67MF3R.
    PhylomeDBiP0AB80.

    Family and domain databases

    InterProiIPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005785. B_amino_transI.
    [Graphical view]
    PANTHERiPTHR11825. PTHR11825. 1 hit.
    PfamiPF01063. Aminotran_4. 1 hit.
    [Graphical view]
    SUPFAMiSSF56752. SSF56752. 1 hit.
    TIGRFAMsiTIGR01122. ilvE_I. 1 hit.
    PROSITEiPS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P0AB80-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTTKKADYIW FNGEMVRWED AKVHVMSHAL HYGTSVFEGI RCYDSHKGPV    50
    VFRHREHMQR LHDSAKIYRF PVSQSIDELM EACRDVIRKN NLTSAYIRPL 100
    IFVGDVGMGV NPPAGYSTDV IIAAFPWGAY LGAEALEQGI DAMVSSWNRA 150
    APNTIPTAAK AGGNYLSSLL VGSEARRHGY QEGIALDVNG YISEGAGENL 200
    FEVKDGVLFT PPFTSSALPG ITRDAIIKLA KELGIEVREQ VLSRESLYLA 250
    DEVFMSGTAA EITPVRSVDG IQVGEGRCGP VTKRIQQAFF GLFTGETEDK 300
    WGWLDQVNQ 309
    Length:309
    Mass (Da):34,094
    Last modified:January 23, 2007 - v2
    Checksum:iE8A2B953168CD09D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti151 – 1511A → R in AAA67573. (PubMed:1379743)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02413 Genomic DNA. Translation: CAA26262.1.
    M32253 Genomic DNA. Translation: AAA24022.1.
    M10313 Genomic DNA. Translation: AAB59052.1.
    X04890 Genomic DNA. Translation: CAA28575.1.
    M87049 Genomic DNA. Translation: AAA67573.1.
    U00096 Genomic DNA. Translation: AAT48207.1.
    AP009048 Genomic DNA. Translation: BAE77527.1.
    V00290 Genomic DNA. Translation: CAA23559.1.
    PIRiE65180. XNECV.
    RefSeqiYP_026247.1. NC_000913.3.
    YP_491668.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAT48207; AAT48207; b3770.
    BAE77527; BAE77527; BAE77527.
    GeneIDi12932278.
    948278.
    KEGGiecj:Y75_p3405.
    eco:b3770.
    PATRICi32123035. VBIEscCol129921_3887.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X02413 Genomic DNA. Translation: CAA26262.1 .
    M32253 Genomic DNA. Translation: AAA24022.1 .
    M10313 Genomic DNA. Translation: AAB59052.1 .
    X04890 Genomic DNA. Translation: CAA28575.1 .
    M87049 Genomic DNA. Translation: AAA67573.1 .
    U00096 Genomic DNA. Translation: AAT48207.1 .
    AP009048 Genomic DNA. Translation: BAE77527.1 .
    V00290 Genomic DNA. Translation: CAA23559.1 .
    PIRi E65180. XNECV.
    RefSeqi YP_026247.1. NC_000913.3.
    YP_491668.1. NC_007779.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A3G X-ray 2.50 A/B/C 2-309 [» ]
    1I1K X-ray 2.10 A/B/C 1-309 [» ]
    1I1L X-ray 2.40 A/B/C 1-309 [» ]
    1I1M X-ray 2.40 A/B/C 1-309 [» ]
    1IYD X-ray 2.15 A/B/C 1-309 [» ]
    1IYE X-ray 1.82 A/B/C 1-309 [» ]
    ProteinModelPortali P0AB80.
    SMRi P0AB80. Positions 5-308.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-10022N.
    STRINGi 511145.b3770.

    2D gel databases

    SWISS-2DPAGE P0AB80.

    Proteomic databases

    PaxDbi P0AB80.
    PRIDEi P0AB80.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT48207 ; AAT48207 ; b3770 .
    BAE77527 ; BAE77527 ; BAE77527 .
    GeneIDi 12932278.
    948278.
    KEGGi ecj:Y75_p3405.
    eco:b3770.
    PATRICi 32123035. VBIEscCol129921_3887.

    Organism-specific databases

    EchoBASEi EB0492.
    EcoGenei EG10497. ilvE.

    Phylogenomic databases

    eggNOGi COG0115.
    HOGENOMi HOG000276706.
    KOi K00826.
    OMAi FPWGSYL.
    OrthoDBi EOG67MF3R.
    PhylomeDBi P0AB80.

    Enzyme and pathway databases

    UniPathwayi UPA00047 ; UER00058 .
    UPA00048 ; UER00073 .
    UPA00049 ; UER00062 .
    BioCyci EcoCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.
    ECOL316407:JW5606-MONOMER.
    MetaCyc:BRANCHED-CHAINAMINOTRANSFER-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P0AB80.
    PROi P0AB80.

    Gene expression databases

    Genevestigatori P0AB80.

    Family and domain databases

    InterProi IPR001544. Aminotrans_IV.
    IPR018300. Aminotrans_IV_CS.
    IPR005785. B_amino_transI.
    [Graphical view ]
    PANTHERi PTHR11825. PTHR11825. 1 hit.
    Pfami PF01063. Aminotran_4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56752. SSF56752. 1 hit.
    TIGRFAMsi TIGR01122. ilvE_I. 1 hit.
    PROSITEi PS00770. AA_TRANSFER_CLASS_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Branched-chain amino acid aminotransferase of Escherichia coli: nucleotide sequence of the ilvE gene and the deduced amino acid sequence."
      Kuramitsu S., Ogawa T., Ogawa H., Kagamiyama H.
      J. Biochem. 97:993-999(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "The complete nucleotide sequence of the ilvGMEDA operon of Escherichia coli K-12."
      Lawther R.P., Wek R.C., Lopes J.M., Pereira R., Taillon B.E., Hatfield G.W.
      Nucleic Acids Res. 15:2137-2155(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    3. "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes."
      Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.
      Science 257:771-778(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    5. Cited for: SEQUENCE REVISION TO 151.
    6. "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.
    7. "The nucleotide sequence preceding and including the beginning of the ilvE gene of the ilvGEDA operon of Escherichia coli K12."
      Lawther R.P., Nichols B.P., Zurawski G., Hatfield G.W.
      Nucleic Acids Res. 7:2289-2301(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-81.
      Strain: K12.
    8. "DNA topology-mediated regulation of transcription initiation from the tandem promoters of the ilvGMEDA operon of Escherichia coli."
      Pagel J.M., Winkelman J.W., Adams C.W., Hatfield G.W.
      J. Mol. Biol. 224:919-935(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
    9. "Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties."
      Inoue K., Kuramitsu S., Aki K., Watanabe Y., Takagi T., Nishigai M., Ikaiu A., Kagamiyama H.
      J. Biochem. 104:777-784(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: PYRIDOXAL PHOSPHATE AT LYS-160.
    10. "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.
    11. "Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5-A resolution."
      Okada K., Hirotsu K., Sato M., Hyashi H., Kagamiyama H.
      J. Biochem. 121:637-641(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

    Entry informationi

    Entry nameiILVE_ECOLI
    AccessioniPrimary (citable) accession number: P0AB80
    Secondary accession number(s): P00510, Q2M879, Q47299
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 83 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3