ID   ALAT_YEAST              Reviewed;         507 AA.
AC   P52892; D6VS97; Q66RF8;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 167.
DE   RecName: Full=Probable alanine aminotransferase;
DE            EC=2.6.1.2;
DE   AltName: Full=Glutamate pyruvate transaminase;
DE            Short=GPT;
DE   AltName: Full=Glutamic--alanine transaminase;
DE   AltName: Full=Glutamic--pyruvic transaminase;
GN   Name=ALT2; OrderedLocusNames=YDR111C; ORFNames=YD9727.07C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
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   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [5]
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).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-alanine = L-glutamate + pyruvate;
CC         Xref=Rhea:RHEA:19453, ChEBI:CHEBI:15361, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:57972; EC=2.6.1.2;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- PATHWAY: Amino-acid degradation; L-alanine degradation via transaminase
CC       pathway; pyruvate from L-alanine: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 3480 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. Alanine aminotransferase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; Z48758; CAA88665.1; -; Genomic_DNA.
DR   EMBL; AY723777; AAU09694.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11957.1; -; Genomic_DNA.
DR   PIR; S52677; S52677.
DR   RefSeq; NP_010396.1; NM_001180419.1.
DR   AlphaFoldDB; P52892; -.
DR   SMR; P52892; -.
DR   BioGRID; 32169; 70.
DR   DIP; DIP-4931N; -.
DR   IntAct; P52892; 2.
DR   MINT; P52892; -.
DR   STRING; 4932.YDR111C; -.
DR   iPTMnet; P52892; -.
DR   MaxQB; P52892; -.
DR   PaxDb; P52892; -.
DR   PRIDE; P52892; -.
DR   EnsemblFungi; YDR111C_mRNA; YDR111C; YDR111C.
DR   GeneID; 851690; -.
DR   KEGG; sce:YDR111C; -.
DR   SGD; S000002518; ALT2.
DR   VEuPathDB; FungiDB:YDR111C; -.
DR   eggNOG; KOG0258; Eukaryota.
DR   GeneTree; ENSGT00940000172095; -.
DR   HOGENOM; CLU_014254_3_0_1; -.
DR   InParanoid; P52892; -.
DR   OMA; LDEEHAW; -.
DR   BioCyc; YEAST:YDR111C-MON; -.
DR   Reactome; R-SCE-8964540; Alanine metabolism.
DR   UniPathway; UPA00528; UER00586.
DR   PRO; PR:P52892; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; P52892; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008483; F:transaminase activity; ISS:SGD.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0042853; P:L-alanine catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   InterPro; IPR045088; ALAT1/2-like.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11751; PTHR11751; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
PE   1: Evidence at protein level;
KW   Aminotransferase; Cytoplasm; Nucleus; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   CHAIN           1..507
FT                   /note="Probable alanine aminotransferase"
FT                   /id="PRO_0000123937"
FT   MOD_RES         327
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        420
FT                   /note="K -> E (in Ref. 3; AAU09694)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   507 AA;  56770 MW;  CB4DCD137CF26085 CRC64;
     MTMTHQQDLK GVFTAKDLDF KPAGKITKKD LNTGVTKAEY AVRGAIPTRA DELKEELKKN
     PEVLPFDDII NANIGNPQQL DQKPLTFTRQ VLAILEYPEI LRVGHNELAS LNLFSRDALE
     RAERLLNDIG GSIGAYSHSQ GVPGIRQTVA DFITRRDGGE PATPEDIYLT TGASSAATSL
     LSLLCKDSQT GLLIPIPQYP LYTASASLFN AQVLPYYLDE ESNWSTNSDE IEKVVQDALK
     KQIRPSVLIV INPGNPTGAV LSEETIARIC LIAAKYGITI ISDEVYQENI FNDVKFHSMK
     KVLRKLQHLY PGKFDNVQLA SLHSISKGFM DECGQRGGYM EIIGFSQEIR DALFKLMSIS
     ICSVVTGQAV VDLMVKPPQP GDESYEQDHD ERLKIFHEMR TRANLLYETF KELEGIECQK
     PQGAMYLFPR LVLPKKALCE SERLGIEPDE FYCTSLLEST GICTVPGSGF GQRPGTYHVR
     TTFLAPGTKW IQDWKEFHQD FFSKYRN