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P0A959

- ALAA_ECOLI

UniProt

P0A959 - ALAA_ECOLI

Protein

Glutamate-pyruvate aminotransferase AlaA

Gene

alaA

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 77 (01 Oct 2014)
      Sequence version 1 (19 Jul 2005)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of alanine.1 Publication

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.By similarity

    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

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

    GO - Biological processi

    1. alanine biosynthetic process Source: EcoliWiki
    2. cellular response to DNA damage stimulus Source: EcoCyc
    3. D-alanine biosynthetic process Source: UniProtKB
    4. L-alanine biosynthetic process from pyruvate Source: EcoCyc
    5. response to antibiotic Source: EcoCyc

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG14101. alaA.

    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 – 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

    Gene expression databases

    GenevestigatoriP0A959.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

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

    Structurei

    3D structure databases

    ProteinModelPortaliP0A959.
    SMRiP0A959. Positions 6-405.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223042.
    KOiK14260.
    OMAiYQARDMR.
    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

    MSPIEKSSKL ENVCYDIRGP VLKEAKRLEE EGNKVLKLNI GNPAPFGFDA    50
    PDEILVDVIR NLPTAQGYCD SKGLYSARKA IMQHYQARGM RDVTVEDIYI 100
    GNGVSELIVQ AMQALLNSGD EMLVPAPDYP LWTAAVSLSS GKAVHYLCDE 150
    SSDWFPDLDD IRAKITPRTR GIVIINPNNP TGAVYSKELL MEIVEIARQH 200
    NLIIFADEIY DKILYDDAEH HSIAPLAPDL LTITFNGLSK TYRVAGFRQG 250
    WMVLNGPKKH AKGYIEGLEM LASMRLCANV PAQHAIQTAL GGYQSISEFI 300
    TPGGRLYEQR NRAWELINDI PGVSCVKPRG ALYMFPKIDA KRFNIHDDQK 350
    MVLDFLLQEK VLLVQGTAFN WPWPDHFRIV TLPRVDDIEL SLSKFARFLS 400
    GYHQL 405
    Length:405
    Mass (Da):45,517
    Last modified:July 19, 2005 - v1
    Checksum:i6A5E78876CC3C388
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75350.1.
    AP009048 Genomic DNA. Translation: BAA16127.1.
    PIRiH65000.
    RefSeqiNP_416793.1. NC_000913.3.
    YP_490532.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75350; AAC75350; b2290.
    BAA16127; BAA16127; BAA16127.
    GeneIDi12933976.
    946772.
    KEGGiecj:Y75_p2256.
    eco:b2290.
    PATRICi32119949. VBIEscCol129921_2384.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75350.1 .
    AP009048 Genomic DNA. Translation: BAA16127.1 .
    PIRi H65000.
    RefSeqi NP_416793.1. NC_000913.3.
    YP_490532.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0A959.
    SMRi P0A959. Positions 6-405.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-11970N.
    IntActi P0A959. 10 interactions.
    STRINGi 511145.b2290.

    Proteomic databases

    PaxDbi P0A959.
    PRIDEi P0A959.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75350 ; AAC75350 ; b2290 .
    BAA16127 ; BAA16127 ; BAA16127 .
    GeneIDi 12933976.
    946772.
    KEGGi ecj:Y75_p2256.
    eco:b2290.
    PATRICi 32119949. VBIEscCol129921_2384.

    Organism-specific databases

    EchoBASEi EB3854.
    EcoGenei EG14101. alaA.

    Phylogenomic databases

    eggNOGi COG0436.
    HOGENOMi HOG000223042.
    KOi K14260.
    OMAi YQARDMR.
    OrthoDBi EOG6X9MJ6.
    PhylomeDBi P0A959.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7184-MONOMER.
    ECOL316407:JW2287-MONOMER.
    MetaCyc:G7184-MONOMER.

    Miscellaneous databases

    PROi P0A959.

    Gene expression databases

    Genevestigatori P0A959.

    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. "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: October 1, 2014
    This is version 77 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

    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