GABAT_YEAST
ID GABAT_YEAST Reviewed; 471 AA.
AC P17649; A5H0J7; D6VUF4;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=4-aminobutyrate aminotransferase;
DE EC=2.6.1.19 {ECO:0000269|PubMed:17355287, ECO:0000305|PubMed:3888627};
DE AltName: Full=GABA aminotransferase;
DE Short=GABA-AT;
DE AltName: Full=Gamma-amino-N-butyrate transaminase;
DE Short=GABA transaminase;
GN Name=UGA1; OrderedLocusNames=YGR019W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sigma 1278B;
RX PubMed=2190186; DOI=10.1093/nar/18.10.3049;
RA Andre B., Jauniaux J.-C.;
RT "Nucleotide sequence of the yeast UGA1 gene encoding GABA transaminase.";
RL Nucleic Acids Res. 18:3049-3049(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND COFACTOR.
RC STRAIN=ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632;
RX PubMed=17355287; DOI=10.1111/j.1742-4658.2007.05729.x;
RA Andersen G., Andersen B., Dobritzsch D., Schnackerz K.D., Piskur J.;
RT "A gene duplication led to specialized gamma-aminobutyrate and beta-alanine
RT aminotransferase in yeast.";
RL FEBS J. 274:1804-1817(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9290212;
RX DOI=10.1002/(sici)1097-0061(19970915)13:11<1077::aid-yea152>3.0.co;2-y;
RA Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.;
RT "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae
RT chromosome VII.";
RL Yeast 13:1077-1090(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169869;
RA Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J.,
RA Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M.,
RA Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L.,
RA Coblenz A., Coglievina M., Coissac E., Defoor E., Del Bino S., Delius H.,
RA Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P.,
RA Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M.,
RA Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A.,
RA Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K.,
RA Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P.,
RA Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E.,
RA Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K.,
RA Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A.,
RA Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S.,
RA Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M.,
RA Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C.,
RA Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M.,
RA Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M.,
RA Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y.,
RA Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L.,
RA Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D.,
RA Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F.,
RA Zaccaria P., Zimmermann M., Zollner A., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.";
RL Nature 387:81-84(1997).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=3888627; DOI=10.1111/j.1432-1033.1985.tb08939.x;
RA Ramos F., El Guezzar M., Grenson M., Wiame J.-M.;
RT "Mutations affecting the enzymes involved in the utilization of 4-
RT aminobutyric acid as nitrogen source by the yeast Saccharomyces
RT cerevisiae.";
RL Eur. J. Biochem. 149:401-404(1985).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=11914276; DOI=10.1101/gad.970902;
RA Kumar A., Agarwal S., Heyman J.A., Matson S., Heidtman M., Piccirillo S.,
RA Umansky L., Drawid A., Jansen R., Liu Y., Cheung K.-H., Miller P.,
RA Gerstein M., Roeder G.S., Snyder M.;
RT "Subcellular localization of the yeast proteome.";
RL Genes Dev. 16:707-719(2002).
RN [9]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [10]
RP FUNCTION, AND INDUCTION.
RX PubMed=19411412; DOI=10.1128/aem.00051-09;
RA Bach B., Meudec E., Lepoutre J.-P., Rossignol T., Blondin B., Dequin S.,
RA Camarasa C.;
RT "New insights into gamma-aminobutyric acid catabolism: evidence for gamma-
RT hydroxybutyric acid and polyhydroxybutyrate synthesis in Saccharomyces
RT cerevisiae.";
RL Appl. Environ. Microbiol. 75:4231-4239(2009).
CC -!- FUNCTION: Required for the degradation of gamma-aminobutyric acid
CC (GABA), which is important for utilization of GABA as nitrogen source
CC and for oxidative stress tolerance. Deaminates GABA to succinate
CC semialdehyde, which in turn is converted to succinate by the succinate-
CC semialdehyde dehydrogenase UGA2. Cannot transaminate beta-alanine
CC (BAL). {ECO:0000269|PubMed:17355287, ECO:0000269|PubMed:19411412,
CC ECO:0000269|PubMed:3888627}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + 4-aminobutanoate = L-glutamate + succinate
CC semialdehyde; Xref=Rhea:RHEA:23352, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57706, ChEBI:CHEBI:59888; EC=2.6.1.19;
CC Evidence={ECO:0000269|PubMed:17355287, ECO:0000305|PubMed:3888627};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17355287};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.2 mM for 4-aminobutanoate {ECO:0000269|PubMed:17355287};
CC KM=0.22 mM for 2-oxoglutarate {ECO:0000269|PubMed:17355287};
CC Vmax=12.8 umol/min/mg enzyme {ECO:0000269|PubMed:17355287};
CC pH dependence:
CC Optimum pH is 8.3. {ECO:0000269|PubMed:3888627};
CC -!- SUBUNIT: Homodimer and homotetramer. {ECO:0000269|PubMed:17355287}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11914276}.
CC -!- INDUCTION: Subject to nitrogen catabolite repression. Expression is low
CC in the presence of the preferred nitrogen sources, and up-regulated by
CC GABA. {ECO:0000269|PubMed:19411412}.
CC -!- MISCELLANEOUS: Present with 573 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X52600; CAA36833.1; -; Genomic_DNA.
DR EMBL; DQ512723; ABF58895.1; -; Genomic_DNA.
DR EMBL; Z72804; CAA97002.1; -; Genomic_DNA.
DR EMBL; AY692904; AAT92923.1; -; Genomic_DNA.
DR EMBL; BK006941; DAA08115.1; -; Genomic_DNA.
DR PIR; S64310; S64310.
DR RefSeq; NP_011533.3; NM_001181148.3.
DR AlphaFoldDB; P17649; -.
DR SMR; P17649; -.
DR BioGRID; 33261; 67.
DR IntAct; P17649; 2.
DR STRING; 4932.YGR019W; -.
DR iPTMnet; P17649; -.
DR MaxQB; P17649; -.
DR PaxDb; P17649; -.
DR PRIDE; P17649; -.
DR EnsemblFungi; YGR019W_mRNA; YGR019W; YGR019W.
DR GeneID; 852902; -.
DR KEGG; sce:YGR019W; -.
DR SGD; S000003251; UGA1.
DR VEuPathDB; FungiDB:YGR019W; -.
DR eggNOG; KOG1405; Eukaryota.
DR GeneTree; ENSGT00550000074885; -.
DR HOGENOM; CLU_016922_12_0_1; -.
DR InParanoid; P17649; -.
DR OMA; HDPEIVP; -.
DR BioCyc; MetaCyc:YGR019W-MON; -.
DR BioCyc; YEAST:YGR019W-MON; -.
DR BRENDA; 2.6.1.19; 984.
DR Reactome; R-SCE-916853; Degradation of GABA.
DR PRO; PR:P17649; -.
DR Proteomes; UP000002311; Chromosome VII.
DR RNAct; P17649; protein.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IMP:SGD.
DR GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IMP:SGD.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004631; 4NH2But_aminotransferase_euk.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00699; GABAtrns_euk; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..471
FT /note="4-aminobutyrate aminotransferase"
FT /id="PRO_0000120382"
FT BINDING 135..136
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 192
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT BINDING 351
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT MOD_RES 326
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P80147"
FT CONFLICT 240
FT /note="H -> R (in Ref. 1; CAA36833 and 2; ABF58895)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 471 AA; 52946 MW; 33D446778A891F63 CRC64;
MSICEQYYPE EPTKPTVKTE SIPGPESQKQ LKELGEVFDT RPAYFLADYE KSLGNYITDV
DGNTYLDLYA QISSIALGYN NPALIKAAQS PEMIRALVDR PALGNFPSKD LDKILKQILK
SAPKGQDHVW SGLSGADANE LAFKAAFIYY RAKQRGYDAD FSEKENLSVM DNDAPGAPHL
AVLSFKRAFH GRLFASGSTT CSKPIHKLDF PAFHWPHAEY PSYQYPLDEN SDANRKEDDH
CLAIVEELIK TWSIPVAALI IEPIQSEGGD NHASKYFLQK LRDITLKYNV VYIIDEVQTG
VGATGKLWCH EYADIQPPVD LVTFSKKFQS AGYFFHDPKF IPNKPYRQFN TWCGEPARMI
IAGAIGQEIS DKKLTEQCSR VGDYLFKKLE GLQKKYPENF QNLRGKGRGT FIAWDLPTGE
KRDLLLKKLK LNGCNVGGCA VHAVRLRPSL TFEEKHADIF IEALAKSVNE L
