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Protein

Glutamate-pyruvate aminotransferase AlaA

Gene

alaA

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

Functioni

Involved in the biosynthesis of alanine.1 Publication

Catalytic activityi

L-alanine + 2-oxoglutarate = pyruvate + L-glutamate.

Cofactori

Kineticsi

  1. KM=0.55 mM for pyruvate (at 37 degrees Celsius and pH 8.5)1 Publication
  2. KM=4.9 mM for alanine (at 37 degrees Celsius and pH 8.5)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411Substrate; via amide nitrogenBy similarity
    Binding sitei179 – 1791SubstrateBy similarity
    Binding sitei378 – 3781SubstrateBy similarity

    GO - Molecular functioni

    • L-alanine:2-oxoglutarate aminotransferase activity Source: UniProtKB
    • pyridoxal phosphate binding Source: InterPro
    • transaminase activity Source: EcoliWiki

    GO - Biological processi

    • alanine biosynthetic process Source: EcoliWiki
    • cellular response to DNA damage stimulus Source: EcoCyc
    • D-alanine biosynthetic process Source: UniProtKB
    • L-alanine biosynthetic process from pyruvate Source: EcoCyc
    • response to antibiotic Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:G7184-MONOMER.
    ECOL316407:JW2287-MONOMER.
    MetaCyc:G7184-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-pyruvate aminotransferase AlaA (EC:2.6.1.2)
    Gene namesi
    Name:alaA
    Synonyms:yfbQ
    Ordered Locus Names:b2290, JW2287
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14101. alaA.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 405405Glutamate-pyruvate aminotransferase AlaAPRO_0000123866Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei240 – 2401N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP0A959.
    PRIDEiP0A959.

    Expressioni

    Inductioni

    Modestly repressed by alanine and leucine via Lrp.1 Publication

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-11970N.
    IntActiP0A959. 10 interactions.
    STRINGi511145.b2290.

    Structurei

    Secondary structure

    1
    405
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 103Combined sources
    Helixi20 – 3011Combined sources
    Helixi44 – 463Combined sources
    Helixi52 – 6110Combined sources
    Helixi62 – 643Combined sources
    Helixi75 – 8612Combined sources
    Turni87 – 893Combined sources
    Helixi95 – 973Combined sources
    Beta strandi98 – 1036Combined sources
    Helixi104 – 11310Combined sources
    Beta strandi121 – 1277Combined sources
    Helixi130 – 1389Combined sources
    Beta strandi142 – 1487Combined sources
    Helixi150 – 1523Combined sources
    Helixi158 – 1636Combined sources
    Beta strandi169 – 1779Combined sources
    Turni179 – 1813Combined sources
    Helixi187 – 19913Combined sources
    Beta strandi203 – 2075Combined sources
    Turni209 – 2124Combined sources
    Helixi223 – 2264Combined sources
    Beta strandi232 – 2387Combined sources
    Turni239 – 2424Combined sources
    Helixi245 – 2473Combined sources
    Beta strandi250 – 2567Combined sources
    Helixi259 – 2613Combined sources
    Helixi262 – 27413Combined sources
    Helixi281 – 2844Combined sources
    Helixi285 – 2906Combined sources
    Helixi297 – 3004Combined sources
    Helixi305 – 31915Combined sources
    Beta strandi329 – 3346Combined sources
    Helixi340 – 3434Combined sources
    Helixi348 – 35912Combined sources
    Beta strandi360 – 3623Combined sources
    Helixi366 – 3694Combined sources
    Beta strandi372 – 3809Combined sources
    Helixi385 – 40016Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CVQX-ray2.11A/B1-405[»]
    ProteinModelPortaliP0A959.
    SMRiP0A959. Positions 1-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223042.
    InParanoidiP0A959.
    KOiK14260.
    OMAiRIVFLPH.
    OrthoDBiEOG6X9MJ6.
    PhylomeDBiP0A959.

    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.

    P0A959-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA
    60 70 80 90 100
    PDEILVDVIR NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI
    110 120 130 140 150
    GNGVSELIVQ AMQALLNSGD EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE
    160 170 180 190 200
    SSDWFPDLDD IRAKITPRTR GIVIINPNNP TGAVYSKELL MEIVEIARQH
    210 220 230 240 250
    NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK TYRVAGFRQG
    260 270 280 290 300
    WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI
    310 320 330 340 350
    TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK
    360 370 380 390 400
    MVLDFLLQEK VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS

    GYHQL
    Length:405
    Mass (Da):45,517
    Last modified:July 19, 2005 - v1
    Checksum:i6A5E78876CC3C388
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75350.1.
    AP009048 Genomic DNA. Translation: BAA16127.1.
    PIRiH65000.
    RefSeqiNP_416793.1. NC_000913.3.
    WP_000074527.1. NZ_CP010445.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75350; AAC75350; b2290.
    BAA16127; BAA16127; BAA16127.
    GeneIDi946772.
    KEGGieco:b2290.
    PATRICi32119949. VBIEscCol129921_2384.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75350.1.
    AP009048 Genomic DNA. Translation: BAA16127.1.
    PIRiH65000.
    RefSeqiNP_416793.1. NC_000913.3.
    WP_000074527.1. NZ_CP010445.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4CVQX-ray2.11A/B1-405[»]
    ProteinModelPortaliP0A959.
    SMRiP0A959. Positions 1-404.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-11970N.
    IntActiP0A959. 10 interactions.
    STRINGi511145.b2290.

    Proteomic databases

    PaxDbiP0A959.
    PRIDEiP0A959.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75350; AAC75350; b2290.
    BAA16127; BAA16127; BAA16127.
    GeneIDi946772.
    KEGGieco:b2290.
    PATRICi32119949. VBIEscCol129921_2384.

    Organism-specific databases

    EchoBASEiEB3854.
    EcoGeneiEG14101. alaA.

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223042.
    InParanoidiP0A959.
    KOiK14260.
    OMAiRIVFLPH.
    OrthoDBiEOG6X9MJ6.
    PhylomeDBiP0A959.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7184-MONOMER.
    ECOL316407:JW2287-MONOMER.
    MetaCyc:G7184-MONOMER.

    Miscellaneous databases

    PROiP0A959.

    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.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features."
      Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T.
      , Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.
      DNA Res. 4:91-113(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. "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 AS AN AMINOTRANSFERASE AND IN ALANINE BIOSYNTHESIS, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INDUCTION, NOMENCLATURE.

    Entry informationi

    Entry nameiALAA_ECOLI
    AccessioniPrimary (citable) accession number: P0A959
    Secondary accession number(s): P77727
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2005
    Last sequence update: July 19, 2005
    Last modified: July 22, 2015
    This is version 84 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, 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.