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Protein

4-aminobutyrate aminotransferase

Gene

UGA1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 5'-phosphate1 Publication

Kineticsi

  1. KM=3.2 mM for 4-aminobutanoate1 Publication
  2. KM=0.22 mM for 2-oxoglutarate1 Publication
  1. Vmax=12.8 µmol/min/mg enzyme1 Publication

pH dependencei

Optimum pH is 8.3.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei192 – 1921SubstrateBy similarity
Binding sitei351 – 3511Pyridoxal phosphate; shared with dimeric partnerBy similarity

GO - Molecular functioni

  • 4-aminobutyrate transaminase activity Source: SGD
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • gamma-aminobutyric acid catabolic process Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

BioCyciMetaCyc:YGR019W-MONOMER.
YEAST:YGR019W-MONOMER.
BRENDAi2.6.1.19. 984.
ReactomeiREACT_313750. 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 Componenti: Chromosome VII

Organism-specific databases

CYGDiYGR019w.
EuPathDBiFungiDB:YGR019W.
SGDiS000003251. UGA1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: SGD
Complete GO annotation...

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. 38 interactions.
IntActiP17649. 2 interactions.
MINTiMINT-4486784.

Structurei

3D structure databases

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

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni135 – 1362Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00550000074885.
HOGENOMiHOG000020208.
InParanoidiP17649.
KOiK13524.
OMAiCHENDAL.
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

« Hide

        10         20         30         40         50
MSICEQYYPE EPTKPTVKTE SIPGPESQKQ LKELGEVFDT RPAYFLADYE
60 70 80 90 100
KSLGNYITDV DGNTYLDLYA QISSIALGYN NPALIKAAQS PEMIRALVDR
110 120 130 140 150
PALGNFPSKD LDKILKQILK SAPKGQDHVW SGLSGADANE LAFKAAFIYY
160 170 180 190 200
RAKQRGYDAD FSEKENLSVM DNDAPGAPHL AVLSFKRAFH GRLFASGSTT
210 220 230 240 250
CSKPIHKLDF PAFHWPHAEY PSYQYPLDEN SDANRKEDDH CLAIVEELIK
260 270 280 290 300
TWSIPVAALI IEPIQSEGGD NHASKYFLQK LRDITLKYNV VYIIDEVQTG
310 320 330 340 350
VGATGKLWCH EYADIQPPVD LVTFSKKFQS AGYFFHDPKF IPNKPYRQFN
360 370 380 390 400
TWCGEPARMI IAGAIGQEIS DKKLTEQCSR VGDYLFKKLE GLQKKYPENF
410 420 430 440 450
QNLRGKGRGT FIAWDLPTGE KRDLLLKKLK LNGCNVGGCA VHAVRLRPSL
460 470
TFEEKHADIF IEALAKSVNE L
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi33261. 38 interactions.
IntActiP17649. 2 interactions.
MINTiMINT-4486784.

Proteomic databases

MaxQBiP17649.
PaxDbiP17649.
PeptideAtlasiP17649.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYGR019w.
EuPathDBiFungiDB:YGR019W.
SGDiS000003251. UGA1.

Phylogenomic databases

eggNOGiCOG0160.
GeneTreeiENSGT00550000074885.
HOGENOMiHOG000020208.
InParanoidiP17649.
KOiK13524.
OMAiCHENDAL.
OrthoDBiEOG744TK4.

Enzyme and pathway databases

BioCyciMetaCyc:YGR019W-MONOMER.
YEAST:YGR019W-MONOMER.
BRENDAi2.6.1.19. 984.
ReactomeiREACT_313750. Degradation of GABA.

Miscellaneous databases

NextBioi972583.
PROiP17649.

Gene expression databases

GenevestigatoriP17649.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR.
    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: May 27, 2015
This is version 139 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

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.