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P17649

- GABAT_YEAST

UniProt

P17649 - GABAT_YEAST

Protein

4-aminobutyrate aminotransferase

Gene

UGA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Required for the degradation of gamma-aminobutyric acid (GABA), which is important for utilization of GABA as nitrogen source and for oxidative stress tolerance. Deaminates GABA to succinate semialdehyde, which in turn is converted to succinate by the succinate-semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine (BAL).3 Publications

    Catalytic activityi

    4-aminobutanoate + 2-oxoglutarate = succinate semialdehyde + L-glutamate.

    Cofactori

    Pyridoxal phosphate.

    pH dependencei

    Optimum pH is 8.3.1 Publication

    GO - Molecular functioni

    1. 4-aminobutyrate transaminase activity Source: SGD
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. gamma-aminobutyric acid catabolic process Source: SGD

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:YGR019W-MONOMER.
    YEAST:YGR019W-MONOMER.
    ReactomeiREACT_189231. Degradation of GABA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-aminobutyrate aminotransferase (EC:2.6.1.19)
    Alternative name(s):
    GABA aminotransferase
    Short name:
    GABA-AT
    Gamma-amino-N-butyrate transaminase
    Short name:
    GABA transaminase
    Gene namesi
    Name:UGA1
    Ordered Locus Names:YGR019W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome VII

    Organism-specific databases

    CYGDiYGR019w.
    SGDiS000003251. UGA1.

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytosol Source: SGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 4714714-aminobutyrate aminotransferasePRO_0000120382Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei326 – 3261N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    MaxQBiP17649.
    PaxDbiP17649.
    PeptideAtlasiP17649.

    Expressioni

    Inductioni

    Subject to nitrogen catabolite repression. Expression is low in the presence of the preferred nitrogen sources, and up-regulated by GABA.1 Publication

    Gene expression databases

    GenevestigatoriP17649.

    Interactioni

    Subunit structurei

    Homodimer and homotetramer.1 Publication

    Protein-protein interaction databases

    BioGridi33261. 36 interactions.
    IntActiP17649. 2 interactions.
    MINTiMINT-4486784.

    Structurei

    3D structure databases

    ProteinModelPortaliP17649.
    SMRiP17649. Positions 15-461.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0160.
    GeneTreeiENSGT00550000074885.
    HOGENOMiHOG000020208.
    KOiK13524.
    OMAiHIEENEW.
    OrthoDBiEOG744TK4.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProiIPR004631. 4NH2But_aminotransferase_euk.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PANTHERiPTHR11986. PTHR11986. 1 hit.
    PTHR11986:SF6. PTHR11986:SF6. 1 hit.
    PfamiPF00202. Aminotran_3. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR00699. GABAtrns_euk. 1 hit.
    PROSITEiPS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P17649-1 [UniParc]FASTAAdd to Basket

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    MSICEQYYPE EPTKPTVKTE SIPGPESQKQ LKELGEVFDT RPAYFLADYE    50
    KSLGNYITDV DGNTYLDLYA QISSIALGYN NPALIKAAQS PEMIRALVDR 100
    PALGNFPSKD LDKILKQILK SAPKGQDHVW SGLSGADANE LAFKAAFIYY 150
    RAKQRGYDAD FSEKENLSVM DNDAPGAPHL AVLSFKRAFH GRLFASGSTT 200
    CSKPIHKLDF PAFHWPHAEY PSYQYPLDEN SDANRKEDDH CLAIVEELIK 250
    TWSIPVAALI IEPIQSEGGD NHASKYFLQK LRDITLKYNV VYIIDEVQTG 300
    VGATGKLWCH EYADIQPPVD LVTFSKKFQS AGYFFHDPKF IPNKPYRQFN 350
    TWCGEPARMI IAGAIGQEIS DKKLTEQCSR VGDYLFKKLE GLQKKYPENF 400
    QNLRGKGRGT FIAWDLPTGE KRDLLLKKLK LNGCNVGGCA VHAVRLRPSL 450
    TFEEKHADIF IEALAKSVNE L 471
    Length:471
    Mass (Da):52,946
    Last modified:October 1, 1996 - v2
    Checksum:i33D446778A891F63
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti240 – 2401H → R in CAA36833. (PubMed:2190186)Curated
    Sequence conflicti240 – 2401H → R in ABF58895. (PubMed:17355287)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52600 Genomic DNA. Translation: CAA36833.1.
    DQ512723 Genomic DNA. Translation: ABF58895.1.
    Z72804 Genomic DNA. Translation: CAA97002.1.
    AY692904 Genomic DNA. Translation: AAT92923.1.
    BK006941 Genomic DNA. Translation: DAA08115.1.
    PIRiS64310.
    RefSeqiNP_011533.3. NM_001181148.3.

    Genome annotation databases

    EnsemblFungiiYGR019W; YGR019W; YGR019W.
    GeneIDi852902.
    KEGGisce:YGR019W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X52600 Genomic DNA. Translation: CAA36833.1 .
    DQ512723 Genomic DNA. Translation: ABF58895.1 .
    Z72804 Genomic DNA. Translation: CAA97002.1 .
    AY692904 Genomic DNA. Translation: AAT92923.1 .
    BK006941 Genomic DNA. Translation: DAA08115.1 .
    PIRi S64310.
    RefSeqi NP_011533.3. NM_001181148.3.

    3D structure databases

    ProteinModelPortali P17649.
    SMRi P17649. Positions 15-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 33261. 36 interactions.
    IntActi P17649. 2 interactions.
    MINTi MINT-4486784.

    Proteomic databases

    MaxQBi P17649.
    PaxDbi P17649.
    PeptideAtlasi P17649.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YGR019W ; YGR019W ; YGR019W .
    GeneIDi 852902.
    KEGGi sce:YGR019W.

    Organism-specific databases

    CYGDi YGR019w.
    SGDi S000003251. UGA1.

    Phylogenomic databases

    eggNOGi COG0160.
    GeneTreei ENSGT00550000074885.
    HOGENOMi HOG000020208.
    KOi K13524.
    OMAi HIEENEW.
    OrthoDBi EOG744TK4.

    Enzyme and pathway databases

    BioCyci MetaCyc:YGR019W-MONOMER.
    YEAST:YGR019W-MONOMER.
    Reactomei REACT_189231. Degradation of GABA.

    Miscellaneous databases

    NextBioi 972583.
    PROi P17649.

    Gene expression databases

    Genevestigatori P17649.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 2 hits.
    InterProi IPR004631. 4NH2But_aminotransferase_euk.
    IPR005814. Aminotrans_3.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view ]
    PANTHERi PTHR11986. PTHR11986. 1 hit.
    PTHR11986:SF6. PTHR11986:SF6. 1 hit.
    Pfami PF00202. Aminotran_3. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000521. Transaminase_4ab_Lys_Orn. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR00699. GABAtrns_euk. 1 hit.
    PROSITEi PS00600. AA_TRANSFER_CLASS_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of the yeast UGA1 gene encoding GABA transaminase."
      Andre B., Jauniaux J.-C.
      Nucleic Acids Res. 18:3049-3049(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Sigma 1278B.
    2. "A gene duplication led to specialized gamma-aminobutyrate and beta-alanine aminotransferase in yeast."
      Andersen G., Andersen B., Dobritzsch D., Schnackerz K.D., Piskur J.
      FEBS J. 274:1804-1817(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT.
      Strain: ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632.
    3. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
      Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
      Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
      Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
      , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
      Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    7. "Mutations affecting the enzymes involved in the utilization of 4-aminobutyric acid as nitrogen source by the yeast Saccharomyces cerevisiae."
      Ramos F., El Guezzar M., Grenson M., Wiame J.-M.
      Eur. J. Biochem. 149:401-404(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
    8. Cited for: SUBCELLULAR LOCATION.
    9. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    10. "New insights into gamma-aminobutyric acid catabolism: evidence for gamma-hydroxybutyric acid and polyhydroxybutyrate synthesis in Saccharomyces cerevisiae."
      Bach B., Meudec E., Lepoutre J.-P., Rossignol T., Blondin B., Dequin S., Camarasa C.
      Appl. Environ. Microbiol. 75:4231-4239(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INDUCTION.

    Entry informationi

    Entry nameiGABAT_YEAST
    AccessioniPrimary (citable) accession number: P17649
    Secondary accession number(s): A5H0J7, D6VUF4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 573 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome VII
      Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

    External Data

    Dasty 3