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P09053

- AVTA_ECOLI

UniProt

P09053 - AVTA_ECOLI

Protein

Valine--pyruvate aminotransferase

Gene

avtA

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (11 Oct 2004)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of alanine.2 Publications

    Catalytic activityi

    L-valine + pyruvate = 3-methyl-2-oxobutanoate + L-alanine.

    Cofactori

    Pyridoxal phosphate.

    GO - Molecular functioni

    1. pyridoxal phosphate binding Source: InterPro
    2. transaminase activity Source: EcoCyc
    3. valine-pyruvate transaminase activity Source: EcoCyc

    GO - Biological processi

    1. cellular amino acid catabolic process Source: EcoCyc
    2. D-alanine biosynthetic process Source: UniProtKB
    3. pyruvate metabolic process Source: EcoCyc
    4. valine biosynthetic process Source: EcoCyc

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.
    ECOL316407:JW5652-MONOMER.
    MetaCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Valine--pyruvate aminotransferase (EC:2.6.1.66)
    Alternative name(s):
    Alanine--valine transaminase
    Transaminase C
    Gene namesi
    Name:avtA
    Ordered Locus Names:b3572, JW5652
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG10107. avtA.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 417417Valine--pyruvate aminotransferasePRO_0000123941Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei249 – 2491N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP09053.
    PRIDEiP09053.

    Expressioni

    Inductioni

    Modestly repressed by alanine and leucine via Lrp. Amino acid limitation causes repression by promoting the accumulation of L-alanine or L-leucine or both. AvtA is also repressed by L-alpha-aminobutyric acid and other nonprotein amino acids which are structurally similar to L-alanine.2 Publications

    Gene expression databases

    GenevestigatoriP09053.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    IntActiP09053. 1 interaction.
    STRINGi511145.b3572.

    Structurei

    3D structure databases

    ProteinModelPortaliP09053.
    SMRiP09053. Positions 15-415.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG3977.
    HOGENOMiHOG000269357.
    KOiK00835.
    OMAiHQCLRMN.
    OrthoDBiEOG6QCD62.
    PhylomeDBiP09053.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProiIPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00155. Aminotran_1_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF53383. SSF53383. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P09053-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTFSLFGDKF TRHSGITLLM EDLNDGLRTP GAIMLGGGNP AQIPEMQDYF    50
    QTLLTDMLES GKATDALCNY DGPQGKTELL TLLAGMLREK LGWDIEPQNI 100
    ALTNGSQSAF FYLFNLFAGR RADGRVKKVL FPLAPEYIGY ADAGLEEDLF 150
    VSARPNIELL PEGQFKYHVD FEHLHIGEET GMICVSRPTN PTGNVITDEE 200
    LLKLDALANQ HGIPLVIDNA YGVPFPGIIF SEARPLWNPN IVLCMSLSKL 250
    GLPGSRCGII IANEKIITAI TNMNGIISLA PGGIGPAMMC EMIKRNDLLR 300
    LSETVIKPFY YQRVQETIAI IRRYLPENRC LIHKPEGAIF LWLWFKDLPI 350
    TTKQLYQRLK ARGVLMVPGH NFFPGLDKPW PHTHQCMRMN YVPEPEKIEA 400
    GVKILAEEIE RAWAESH 417
    Length:417
    Mass (Da):46,711
    Last modified:October 11, 2004 - v3
    Checksum:i55A0CA53F0E697A2
    GO

    Sequence cautioni

    The sequence CAA68546.1 differs from that shown. Reason:

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti208 – 2081A → G in AAB18549. (PubMed:8041620)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00490 Genomic DNA. Translation: CAA68546.1. Sequence problems.
    U00039 Genomic DNA. Translation: AAB18549.1.
    U00096 Genomic DNA. Translation: AAT48193.1.
    AP009048 Genomic DNA. Translation: BAE77721.1.
    PIRiS47793.
    RefSeqiYP_026231.1. NC_000913.3.
    YP_491862.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAT48193; AAT48193; b3572.
    BAE77721; BAE77721; BAE77721.
    GeneIDi12930377.
    948087.
    KEGGiecj:Y75_p3603.
    eco:b3572.
    PATRICi32122620. VBIEscCol129921_3687.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00490 Genomic DNA. Translation: CAA68546.1 . Sequence problems.
    U00039 Genomic DNA. Translation: AAB18549.1 .
    U00096 Genomic DNA. Translation: AAT48193.1 .
    AP009048 Genomic DNA. Translation: BAE77721.1 .
    PIRi S47793.
    RefSeqi YP_026231.1. NC_000913.3.
    YP_491862.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P09053.
    SMRi P09053. Positions 15-415.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P09053. 1 interaction.
    STRINGi 511145.b3572.

    Proteomic databases

    PaxDbi P09053.
    PRIDEi P09053.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT48193 ; AAT48193 ; b3572 .
    BAE77721 ; BAE77721 ; BAE77721 .
    GeneIDi 12930377.
    948087.
    KEGGi ecj:Y75_p3603.
    eco:b3572.
    PATRICi 32122620. VBIEscCol129921_3687.

    Organism-specific databases

    EchoBASEi EB0105.
    EcoGenei EG10107. avtA.

    Phylogenomic databases

    eggNOGi COG3977.
    HOGENOMi HOG000269357.
    KOi K00835.
    OMAi HQCLRMN.
    OrthoDBi EOG6QCD62.
    PhylomeDBi P09053.

    Enzyme and pathway databases

    BioCyci EcoCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.
    ECOL316407:JW5652-MONOMER.
    MetaCyc:VALINE-PYRUVATE-AMINOTRANSFER-MONOMER.

    Miscellaneous databases

    PROi P09053.

    Gene expression databases

    Genevestigatori P09053.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    InterProi IPR004839. Aminotransferase_I/II.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    Pfami PF00155. Aminotran_1_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53383. SSF53383. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Rapid sequencing of cloned DNA using a transposon for bidirectional priming: sequence of the Escherichia coli K-12 avtA gene."
      Liu L., Whalen W., Das A., Berg C.M.
      Nucleic Acids Res. 15:9461-9469(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: K12.
    2. "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes."
      Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R.
      Nucleic Acids Res. 22:2576-2586(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. Cited for: SEQUENCE REVISION TO 208.
    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. "Transamination in Escherichia coli."
      Rudman D., Meister A.
      J. Biol. Chem. 200:591-604(1953) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS AN AMINOTRANSFERASE.
    7. "Gratuitous repression of avtA in Escherichia coli and Salmonella typhimurium."
      Whalen W.A., Berg C.M.
      J. Bacteriol. 158:571-574(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION.
    8. "Genetics and regulation of the major enzymes of alanine synthesis in Escherichia coli."
      Kim S.H., Schneider B.L., Reitzer L.
      J. Bacteriol. 192:5304-5311(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ALANINE BIOSYNTHESIS, INDUCTION.

    Entry informationi

    Entry nameiAVTA_ECOLI
    AccessioniPrimary (citable) accession number: P09053
    Secondary accession number(s): Q2M7N5, Q6BF21
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: October 11, 2004
    Last modified: October 1, 2014
    This is version 109 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3