AATC_YEAST
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 03-AUG-2022, entry version 205.
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; 204.
DR DIP; DIP-2897N; -.
DR IntAct; P23542; 18.
DR MINT; P23542; -.
DR STRING; 4932.YLR027C; -.
DR iPTMnet; P23542; -.
DR MaxQB; P23542; -.
DR PaxDb; P23542; -.
DR PRIDE; P23542; -.
DR EnsemblFungi; YLR027C_mRNA; YLR027C; YLR027C.
DR GeneID; 850714; -.
DR KEGG; sce:YLR027C; -.
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; WDQNKRQ; -.
DR BioCyc; MetaCyc:YLR027C-MON; -.
DR BioCyc; YEAST:YLR027C-MON; -.
DR Reactome; R-SCE-70263; Gluconeogenesis.
DR Reactome; R-SCE-8963693; Aspartate and asparagine metabolism.
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:0019266; P:asparagine biosynthetic process from oxaloacetate; IC:SGD.
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 Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 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
