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P77434

- ALAC_ECOLI

UniProt

P77434 - ALAC_ECOLI

Protein

Glutamate-pyruvate aminotransferase AlaC

Gene

alaC

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 105 (01 Oct 2014)
      Sequence version 1 (01 Feb 1997)
      Previous versions | rss
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    Functioni

    Involved in the biosynthesis of alanine.2 Publications

    Catalytic activityi

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

    Cofactori

    Pyridoxal phosphate.Curated

    Kineticsi

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

    GO - Molecular functioni

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

    GO - Biological processi

    1. alanine biosynthetic process Source: EcoliWiki
    2. D-alanine biosynthetic process Source: UniProtKB
    3. L-alanine biosynthetic process from pyruvate Source: EcoCyc

    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: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG14198. alaC.

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0436.
    HOGENOMiHOG000223051.
    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

    MADTRPERRF TRIDRLPPYV FNITAELKMA ARRRGEDIID FSMGNPDGAT    50
    PPHIVEKLCT VAQRPDTHGY STSRGIPRLR RAISRWYQDR YDVEIDPESE 100
    AIVTIGSKEG LAHLMLATLD HGDTVLVPNP SYPIHIYGAV IAGAQVRSVP 150
    LVEGVDFFNE LERAIRESYP KPKMMILGFP SNPTAQCVEL EFFEKVVALA 200
    KRYDVLVVHD LAYADIVYDG WKAPSIMQVP GARDVAVEFF TLSKSYNMAG 250
    WRIGFMVGNK TLVSALARIK SYHDYGTFTP LQVAAIAALE GDQQCVRDIA 300
    EQYKRRRDVL VKGLHEAGWM VEMPKASMYV WAKIPEPYAA MGSLEFAKKL 350
    LNEAKVCVSP GIGFGDYGDT HVRFALIENR DRIRQAIRGI KAMFRADGLL 400
    PASSKHIHEN AE 412
    Length:412
    Mass (Da):46,216
    Last modified:February 1, 1997 - v1
    Checksum:iF0F62F84344E588E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75438.1.
    AP009048 Genomic DNA. Translation: BAA16249.1.
    PIRiH65011.
    RefSeqiNP_416880.1. NC_000913.3.
    YP_490621.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC75438; AAC75438; b2379.
    BAA16249; BAA16249; BAA16249.
    GeneIDi12931937.
    946850.
    KEGGiecj:Y75_p2346.
    eco:b2379.
    PATRICi32120137. VBIEscCol129921_2477.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U00096 Genomic DNA. Translation: AAC75438.1 .
    AP009048 Genomic DNA. Translation: BAA16249.1 .
    PIRi H65011.
    RefSeqi NP_416880.1. NC_000913.3.
    YP_490621.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P77434.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-12010N.
    IntActi P77434. 8 interactions.
    STRINGi 511145.b2379.

    Proteomic databases

    PaxDbi P77434.
    PRIDEi P77434.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC75438 ; AAC75438 ; b2379 .
    BAA16249 ; BAA16249 ; BAA16249 .
    GeneIDi 12931937.
    946850.
    KEGGi ecj:Y75_p2346.
    eco:b2379.
    PATRICi 32120137. VBIEscCol129921_2477.

    Organism-specific databases

    EchoBASEi EB3950.
    EcoGenei EG14198. alaC.

    Phylogenomic databases

    eggNOGi COG0436.
    HOGENOMi HOG000223051.
    KOi K14261.
    OMAi RGSIPKP.
    OrthoDBi EOG6W721W.
    PhylomeDBi P77434.

    Enzyme and pathway databases

    BioCyci EcoCyc:G7242-MONOMER.
    ECOL316407:JW2376-MONOMER.
    MetaCyc:G7242-MONOMER.

    Miscellaneous databases

    PROi P77434.

    Gene expression databases

    Genevestigatori P77434.

    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. "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: October 1, 2014
    This is version 105 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