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Protein

Glutamate-pyruvate aminotransferase AlaC

Gene

alaC

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biosynthesis of alanine.2 Publications

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=0.94 mM for pyruvate (at 37 degrees Celsius and pH 8.5)1 Publication

    GO - Molecular functioni

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

    GO - Biological processi

    • alanine biosynthetic process Source: EcoliWiki
    • D-alanine biosynthetic process Source: UniProtKB
    • L-alanine biosynthetic process from pyruvate Source: EcoCyc
    Complete GO annotation...

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciEcoCyc:G7242-MONOMER.
    ECOL316407:JW2376-MONOMER.
    MetaCyc:G7242-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutamate-pyruvate aminotransferase AlaC (EC:2.6.1.2)
    Gene namesi
    Name:alaC
    Synonyms:yfdZ
    Ordered Locus Names:b2379, JW2376
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG14198. alaC.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 412412Glutamate-pyruvate aminotransferase AlaCPRO_0000123926Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei244 – 2441N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    PaxDbiP77434.
    PRIDEiP77434.

    Expressioni

    Inductioni

    Activated by SgrR and modestly repressed by alanine and leucine via Lrp.2 Publications

    Gene expression databases

    GenevestigatoriP77434.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    DIPiDIP-12010N.
    IntActiP77434. 8 interactions.
    STRINGi511145.b2379.

    Structurei

    3D structure databases

    ProteinModelPortaliP77434.
    SMRiP77434. Positions 20-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223051.
    InParanoidiP77434.
    KOiK14261.
    OMAiRGSIPKP.
    OrthoDBiEOG6W721W.
    PhylomeDBiP77434.

    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.

    P77434-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MADTRPERRF TRIDRLPPYV FNITAELKMA ARRRGEDIID FSMGNPDGAT
    60 70 80 90 100
    PPHIVEKLCT VAQRPDTHGY STSRGIPRLR RAISRWYQDR YDVEIDPESE
    110 120 130 140 150
    AIVTIGSKEG LAHLMLATLD HGDTVLVPNP SYPIHIYGAV IAGAQVRSVP
    160 170 180 190 200
    LVEGVDFFNE LERAIRESYP KPKMMILGFP SNPTAQCVEL EFFEKVVALA
    210 220 230 240 250
    KRYDVLVVHD LAYADIVYDG WKAPSIMQVP GARDVAVEFF TLSKSYNMAG
    260 270 280 290 300
    WRIGFMVGNK TLVSALARIK SYHDYGTFTP LQVAAIAALE GDQQCVRDIA
    310 320 330 340 350
    EQYKRRRDVL VKGLHEAGWM VEMPKASMYV WAKIPEPYAA MGSLEFAKKL
    360 370 380 390 400
    LNEAKVCVSP GIGFGDYGDT HVRFALIENR DRIRQAIRGI KAMFRADGLL
    410
    PASSKHIHEN AE
    Length:412
    Mass (Da):46,216
    Last modified:February 1, 1997 - v1
    Checksum:iF0F62F84344E588E
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75438.1.
    AP009048 Genomic DNA. Translation: BAA16249.1.
    PIRiH65011.
    RefSeqiNP_416880.1. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC75438; AAC75438; b2379.
    BAA16249; BAA16249; BAA16249.
    GeneIDi946850.
    KEGGiecj:Y75_p2346.
    eco:b2379.
    PATRICi32120137. VBIEscCol129921_2477.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA. Translation: AAC75438.1.
    AP009048 Genomic DNA. Translation: BAA16249.1.
    PIRiH65011.
    RefSeqiNP_416880.1. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP77434.
    SMRiP77434. Positions 20-399.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    DIPiDIP-12010N.
    IntActiP77434. 8 interactions.
    STRINGi511145.b2379.

    Proteomic databases

    PaxDbiP77434.
    PRIDEiP77434.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC75438; AAC75438; b2379.
    BAA16249; BAA16249; BAA16249.
    GeneIDi946850.
    KEGGiecj:Y75_p2346.
    eco:b2379.
    PATRICi32120137. VBIEscCol129921_2477.

    Organism-specific databases

    EchoBASEiEB3950.
    EcoGeneiEG14198. alaC.

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223051.
    InParanoidiP77434.
    KOiK14261.
    OMAiRGSIPKP.
    OrthoDBiEOG6W721W.
    PhylomeDBiP77434.

    Enzyme and pathway databases

    BioCyciEcoCyc:G7242-MONOMER.
    ECOL316407:JW2376-MONOMER.
    MetaCyc:G7242-MONOMER.

    Miscellaneous databases

    PROiP77434.

    Gene expression databases

    GenevestigatoriP77434.

    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. "The novel transcription factor SgrR coordinates the response to glucose-phosphate stress."
      Vanderpool C.K., Gottesman S.
      J. Bacteriol. 189:2238-2248(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INDUCTION BY SGRR.
    5. "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.
    6. "Isolation of a mutant auxotrophic for L-alanine and identification of three major aminotransferases that synthesize L-alanine in Escherichia coli."
      Yoneyama H., Hori H., Lim S.J., Murata T., Ando T., Isogai E., Katsumata R.
      Biosci. Biotechnol. Biochem. 75:930-938(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN ALANINE BIOSYNTHESIS.

    Entry informationi

    Entry nameiALAC_ECOLI
    AccessioniPrimary (citable) accession number: P77434
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: February 1, 1997
    Last modified: May 27, 2015
    This is version 109 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

    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.