ID   AATC_YEAST              Reviewed;         418 AA.
AC   P23542; D6VY29;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   27-MAR-2024, entry version 211.
DE   RecName: Full=Aspartate aminotransferase, cytoplasmic;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=AAT2; Synonyms=ASP5; OrderedLocusNames=YLR027C; ORFNames=L1746;
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=9169871;
RA   Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA   Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA   Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA   Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA   Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA   Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA   Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA   Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA   Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA   Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA   Zollner A., Hani J., Hoheisel J.D.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL   Nature 387:87-90(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   PROTEIN SEQUENCE OF 2-418.
RX   PubMed=2199266; DOI=10.1042/bst0180256;
RA   Cronin V.B., Doyle J.M., Doonan S.;
RT   "Amino acid sequences of aspartate aminotransferases: the cytosolic
RT   isoenzymes from yeast and from human liver.";
RL   Biochem. Soc. Trans. 18:256-256(1990).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-418, ACETYLATION AT SER-2, AND ENZYME ACTIVITY.
RX   PubMed=1859361; DOI=10.1042/bj2770335;
RA   Cronin V.B., Maras B., Barra D., Doonan S.;
RT   "The amino acid sequence of the aspartate aminotransferase from baker's
RT   yeast (Saccharomyces cerevisiae).";
RL   Biochem. J. 277:335-340(1991).
RN   [5]
RP   CRYSTALLIZATION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   PubMed=6811576; DOI=10.1093/oxfordjournals.jbchem.a133929;
RA   Yagi T., Kagamiyama H., Nozaki M.;
RT   "Aspartate: 2-oxoglutarate aminotransferase from bakers' yeast:
RT   crystallization and characterization.";
RL   J. Biochem. 92:35-43(1982).
RN   [6]
RP   ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
RX   PubMed=9288922; DOI=10.1111/j.1432-1033.1997.00972.x;
RA   Verleur N., Elgersma Y., Van Roermund C.W., Tabak H.F., Wanders R.J.;
RT   "Cytosolic aspartate aminotransferase encoded by the AAT2 gene is targeted
RT   to the peroxisomes in oleate-grown Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 247:972-980(1997).
RN   [7]
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA   Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA   Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT   "Analysis of phosphorylation sites on proteins from Saccharomyces
RT   cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN   [9]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RP   X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH PYRODOXAL PHOSPHATE
RP   AND MALEIC ACID, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-255, AND SUBUNIT.
RX   PubMed=9655342; DOI=10.1002/pro.5560070614;
RA   Jeffery C.J., Barry T., Doonan S., Petsko G.A., Ringe D.;
RT   "Crystal structure of Saccharomyces cerevisiae cytosolic aspartate
RT   aminotransferase.";
RL   Protein Sci. 7:1380-1387(1998).
CC   -!- FUNCTION: Plays a key role in amino acid metabolism.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate;
CC         Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1;
CC         Evidence={ECO:0000269|PubMed:1859361, ECO:0000269|PubMed:6811576,
CC         ECO:0000269|PubMed:9288922};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000269|PubMed:6811576, ECO:0000269|PubMed:9655342};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.11 mM for L-aspartate {ECO:0000269|PubMed:6811576};
CC         KM=20 mM for L-glutamate {ECO:0000269|PubMed:6811576};
CC         KM=0.006 mM for oxaloacetate {ECO:0000269|PubMed:6811576};
CC         KM=0.16 mM for 2-oxoglutarate {ECO:0000269|PubMed:6811576};
CC       pH dependence:
CC         Optimum pH is 8-9. {ECO:0000269|PubMed:6811576};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:6811576,
CC       ECO:0000269|PubMed:9655342}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9288922}.
CC       Peroxisome {ECO:0000269|PubMed:9288922}. Note=Targeted to peroxisomes
CC       in cells grown in oleate.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes.
CC   -!- MISCELLANEOUS: Present with 7700 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. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA97550.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; Z73199; CAA97550.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006945; DAA09345.1; -; Genomic_DNA.
DR   PIR; S64854; S64854.
DR   RefSeq; NP_013127.2; NM_001181914.1.
DR   PDB; 1YAA; X-ray; 2.05 A; A/B/C/D=2-412.
DR   PDBsum; 1YAA; -.
DR   AlphaFoldDB; P23542; -.
DR   SMR; P23542; -.
DR   BioGRID; 31301; 216.
DR   DIP; DIP-2897N; -.
DR   IntAct; P23542; 18.
DR   MINT; P23542; -.
DR   STRING; 4932.YLR027C; -.
DR   iPTMnet; P23542; -.
DR   MaxQB; P23542; -.
DR   PaxDb; 4932-YLR027C; -.
DR   PeptideAtlas; P23542; -.
DR   EnsemblFungi; YLR027C_mRNA; YLR027C; YLR027C.
DR   GeneID; 850714; -.
DR   KEGG; sce:YLR027C; -.
DR   AGR; SGD:S000004017; -.
DR   SGD; S000004017; AAT2.
DR   VEuPathDB; FungiDB:YLR027C; -.
DR   eggNOG; KOG1412; Eukaryota.
DR   GeneTree; ENSGT00950000183082; -.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; P23542; -.
DR   OMA; SWAIRYF; -.
DR   OrthoDB; 1123851at2759; -.
DR   BioCyc; MetaCyc:YLR027C-MONOMER; -.
DR   BioCyc; YEAST:YLR027C-MONOMER; -.
DR   Reactome; R-SCE-70263; Gluconeogenesis.
DR   Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
DR   BioGRID-ORCS; 850714; 3 hits in 10 CRISPR screens.
DR   EvolutionaryTrace; P23542; -.
DR   PRO; PR:P23542; -.
DR   Proteomes; UP000002311; Chromosome XII.
DR   RNAct; P23542; Protein.
DR   GO; GO:0005829; C:cytosol; IDA:SGD.
DR   GO; GO:0005777; C:peroxisome; IDA:SGD.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:SGD.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006532; P:aspartate biosynthetic process; IMP:SGD.
DR   GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR   GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II.
DR   InterPro; IPR000796; Asp_trans.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF55; GLUTAMATE OXALOACETATE TRANSAMINASE 1, ISOFORM B; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00799; TRANSAMINASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Aminotransferase; Cytoplasm;
KW   Direct protein sequencing; Peroxisome; Phosphoprotein; Pyridoxal phosphate;
KW   Reference proteome; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1859361,
FT                   ECO:0000269|PubMed:2199266, ECO:0007744|PubMed:22814378"
FT   CHAIN           2..418
FT                   /note="Aspartate aminotransferase, cytoplasmic"
FT                   /id="PRO_0000123875"
FT   BINDING         38
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000269|PubMed:9655342"
FT   BINDING         135
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000269|PubMed:9655342"
FT   BINDING         188
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000269|PubMed:9655342"
FT   BINDING         387
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000269|PubMed:9655342"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000269|PubMed:1859361,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         255
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000269|PubMed:9655342"
FT   MOD_RES         389
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17287358"
FT   CONFLICT        95
FT                   /note="F -> L (in Ref. 3; AA sequence and 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        413..414
FT                   /note="TI -> AT (in Ref. 3; AA sequence and 4; AA
FT                   sequence)"
FT                   /evidence="ECO:0000305"
FT   TURN            3..8
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           18..25
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           51..61
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           77..88
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           93..96
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          100..106
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           107..122
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          128..133
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           138..143
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            144..146
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          149..153
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            157..160
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           164..173
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          179..183
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            188..190
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           196..208
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          212..218
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            220..222
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          223..225
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           227..230
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           232..240
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            241..244
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          247..252
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            254..256
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           260..262
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          264..270
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           277..293
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           301..312
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           314..345
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           353..356
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          359..363
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           368..378
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   STRAND          386..389
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           390..392
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   TURN            395..397
FT                   /evidence="ECO:0007829|PDB:1YAA"
FT   HELIX           398..411
FT                   /evidence="ECO:0007829|PDB:1YAA"
SQ   SEQUENCE   418 AA;  46058 MW;  D25F40F6C6DD2B33 CRC64;
     MSATLFNNIE LLPPDALFGI KQRYGQDQRA TKVDLGIGAY RDDNGKPWVL PSVKAAEKLI
     HNDSSYNHEY LGITGLPSLT SNAAKIIFGT QSDAFQEDRV ISVQSLSGTG ALHISAKFFS
     KFFPDKLVYL SKPTWANHMA IFENQGLKTA TYPYWANETK SLDLNGFLNA IQKAPEGSIF
     VLHSCAHNPT GLDPTSEQWV QIVDAIASKN HIALFDTAYQ GFATGDLDKD AYAVRLGVEK
     LSTVSPVFVC QSFAKNAGMY GERVGCFHLA LTKQAQNKTI KPAVTSQLAK IIRSEVSNPP
     AYGAKIVAKL LETPELTEQW HKDMVTMSSR ITKMRHALRD HLVKLGTPGN WDHIVNQCGM
     FSFTGLTPQM VKRLEETHAV YLVASGRASI AGLNQGNVEY VAKAIDEVVR FYTIEAKL
//