AAT2_ARATH
ID AAT2_ARATH Reviewed; 405 AA.
AC P46645;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2002, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic isozyme 1;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN Name=ASP2; Synonyms=AAT2; OrderedLocusNames=At5g19550; ORFNames=T20D1.70;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=7894512; DOI=10.1046/j.1365-313x.1995.07010061.x;
RA Schultz C.J., Coruzzi G.M.;
RT "The aspartate aminotransferase gene family of Arabidopsis encodes
RT isoenzymes localized to three distinct subcellular compartments.";
RL Plant J. 7:61-75(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 327-405.
RC STRAIN=cv. Columbia; TISSUE=Leaf;
RX PubMed=8580968; DOI=10.1046/j.1365-313x.1996.09010101.x;
RA Cooke R., Raynal M., Laudie M., Grellet F., Delseny M., Morris P.-C.,
RA Guerrier D., Giraudat J., Quigley F., Clabault G., Li Y.-F., Mache R.,
RA Krivitzky M., Gy I.J.-J., Kreis M., Lecharny A., Parmentier Y., Marbach J.,
RA Fleck J., Clement B., Philipps G., Herve C., Bardet C., Tremousaygue D.,
RA Lescure B., Lacomme C., Roby D., Jourjon M.-F., Chabrier P.,
RA Charpenteau J.-L., Desprez T., Amselem J., Chiapello H., Hoefte H.;
RT "Further progress towards a catalogue of all Arabidopsis genes: analysis of
RT a set of 5000 non-redundant ESTs.";
RL Plant J. 9:101-124(1996).
RN [5]
RP FUNCTION.
RX PubMed=9611168; DOI=10.1093/genetics/149.2.491;
RA Schultz C.J., Hsu M., Miesak B., Coruzzi G.M.;
RT "Arabidopsis mutants define an in vivo role for isoenzymes of aspartate
RT aminotransferase in plant nitrogen assimilation.";
RL Genetics 149:491-499(1998).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9535706; DOI=10.1006/prep.1997.0845;
RA Wilkie S.E., Warren M.J.;
RT "Recombinant expression, purification, and characterization of three
RT isoenzymes of aspartate aminotransferase from Arabidopsis thaliana.";
RL Protein Expr. Purif. 12:381-389(1998).
RN [7]
RP FUNCTION, MUTAGENESIS OF PRO-46; PRO-71; GLY-254 AND SER-306, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=12068109; DOI=10.1104/pp.005090;
RA Miesak B.H., Coruzzi G.M.;
RT "Molecular and physiological analysis of Arabidopsis mutants defective in
RT cytosolic or chloroplastic aspartate aminotransferase.";
RL Plant Physiol. 129:650-660(2002).
RN [8]
RP INDUCTION BY PATHOGEN, AND DISRUPTION PHENOTYPE.
RX PubMed=21676488; DOI=10.1016/j.jplph.2011.05.012;
RA Brauc S., De Vooght E., Claeys M., Hofte M., Angenon G.;
RT "Influence of over-expression of cytosolic aspartate aminotransferase on
RT amino acid metabolism and defence responses against Botrytis cinerea
RT infection in Arabidopsis thaliana.";
RL J. Plant Physiol. 168:1813-1819(2011).
RN [9]
RP FUNCTION, MUTAGENESIS OF ALA-250; LYS-251; GLU-258; ARG-259 AND PRO-292,
RP DISRUPTION PHENOTYPE, DEVELOPMENTAL STAGE, AND SUBUNIT.
RC STRAIN=cv. Columbia;
RX PubMed=21511809; DOI=10.1093/mp/ssr033;
RA Leasure C.D., Tong H.Y., Hou X.W., Shelton A., Minton M., Esquerra R.,
RA Roje S., Hellmann H., He Z.H.;
RT "root uv-b sensitive mutants are suppressed by specific mutations in
RT ASPARTATE AMINOTRANSFERASE2 and by exogenous vitamin B6.";
RL Mol. Plant 4:759-770(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Important for the metabolism of amino acids and Krebs-cycle
CC related organic acids. Involved in plant nitrogen metabolism of Asp and
CC Asp-derived amino acids and in the synthesis of Asp/Asn for seed
CC storage (PubMed:12068109). May be involved in the assessment of the
CC pyridoxal phosphate levels in the cell (PubMed:21511809).
CC {ECO:0000269|PubMed:12068109, ECO:0000269|PubMed:7894512,
CC ECO:0000269|PubMed:9535706, ECO:0000269|PubMed:9611168,
CC ECO:0000303|PubMed:21511809}.
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:9535706};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.38 mM for L-aspartate {ECO:0000269|PubMed:9535706};
CC KM=0.10 mM for 2-oxoglutarate {ECO:0000269|PubMed:9535706};
CC KM=12.8 mM for L-glutamate {ECO:0000269|PubMed:9535706};
CC KM=0.027 mM for oxaloacetate {ECO:0000269|PubMed:9535706};
CC Note=kcat is 217 sec(-1) for the forward reaction. kcat is 574 sec(-
CC 1) for the reverse reaction. {ECO:0000269|PubMed:9535706};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21511809}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Highly expressed during early germination.
CC {ECO:0000269|PubMed:21511809}.
CC -!- INDUCTION: Up-regulated upon pathogen infection.
CC {ECO:0000269|PubMed:21676488}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype, but slight modification of
CC the amino acid composition. Growth defect, when grown in vitro.
CC {ECO:0000269|PubMed:12068109, ECO:0000269|PubMed:21511809,
CC ECO:0000269|PubMed:21676488}.
CC -!- MISCELLANEOUS: Several mutations in ASP2, but not all, suppress the
CC root UV-B sensitive (rus) phenotype. A loss of ASP2 activity is not
CC sufficient for this suppression. {ECO:0000269|PubMed:21511809}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U15033; AAA79370.1; -; mRNA.
DR EMBL; AF296830; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92724.1; -; Genomic_DNA.
DR EMBL; Z26740; CAA81411.1; -; mRNA.
DR RefSeq; NP_197456.1; NM_121960.5.
DR AlphaFoldDB; P46645; -.
DR SMR; P46645; -.
DR BioGRID; 17351; 9.
DR STRING; 3702.AT5G19550.1; -.
DR iPTMnet; P46645; -.
DR PaxDb; P46645; -.
DR PRIDE; P46645; -.
DR ProteomicsDB; 244375; -.
DR EnsemblPlants; AT5G19550.1; AT5G19550.1; AT5G19550.
DR GeneID; 832075; -.
DR Gramene; AT5G19550.1; AT5G19550.1; AT5G19550.
DR KEGG; ath:AT5G19550; -.
DR Araport; AT5G19550; -.
DR TAIR; locus:2180826; AT5G19550.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P46645; -.
DR OMA; WDQNKRQ; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P46645; -.
DR SABIO-RK; P46645; -.
DR PRO; PR:P46645; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; P46645; baseline and differential.
DR Genevisible; P46645; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006103; P:2-oxoglutarate metabolic process; ISS:UniProtKB.
DR GO; GO:0006531; P:aspartate metabolic process; ISS:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0071456; P:cellular response to hypoxia; HEP:TAIR.
DR GO; GO:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IMP:TAIR.
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 Acetylation; Aminotransferase; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..405
FT /note="Aspartate aminotransferase, cytoplasmic isozyme 1"
FT /id="PRO_0000123872"
FT BINDING 37
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 134
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 187
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT BINDING 379
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 251
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P23542"
FT MUTAGEN 46
FT /note="P->L: In aat2-4; loss of activity."
FT /evidence="ECO:0000269|PubMed:12068109"
FT MUTAGEN 71
FT /note="P->L: In aat2-2; loss of activity and growth defect
FT when grown in vitro."
FT /evidence="ECO:0000269|PubMed:12068109"
FT MUTAGEN 250
FT /note="A->V: In asp2-12; loss of pyridoxal phosphate
FT binding and loss of activity."
FT /evidence="ECO:0000269|PubMed:21511809"
FT MUTAGEN 251
FT /note="K->A: Loss of activity."
FT /evidence="ECO:0000269|PubMed:21511809"
FT MUTAGEN 254
FT /note="G->R: In aat2-1; loss of activity."
FT /evidence="ECO:0000269|PubMed:12068109"
FT MUTAGEN 258
FT /note="E->K: In asp2-13; loss of pyridoxal phosphate
FT binding and loss of activity."
FT /evidence="ECO:0000269|PubMed:21511809"
FT MUTAGEN 259
FT /note="R->H: In asp2-14; loss of pyridoxal phosphate
FT binding and loss of activity."
FT /evidence="ECO:0000269|PubMed:21511809"
FT MUTAGEN 292
FT /note="P->L: In asp2-11; loss of pyridoxal phosphate
FT binding and loss of activity."
FT /evidence="ECO:0000269|PubMed:21511809"
FT MUTAGEN 306
FT /note="S->N: In aat2-5; loss of activity."
FT /evidence="ECO:0000269|PubMed:12068109"
FT CONFLICT 250
FT /note="A -> T (in Ref. 1; AAA79370)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 405 AA; 44267 MW; A53C5DF1B176F632 CRC64;
MDSVFSNVAR APEDPILGVT VAYNNDPSPV KINLGVGAYR TEEGKPLVLD VVRKAEQQLV
NDPSRVKEYI PIVGISDFNK LSAKLILGAD SPAITESRVT TVQCLSGTGS LRVGAEFLKT
HYHQSVIYIP KPTWGNHPKV FNLAGLSVEY FRYYDPATRG LDFKGLLEDL GAAPSGAIVL
LHACAHNPTG VDPTSEQWEQ IRQLMRSKSL LPFFDSAYQG FASGSLDTDA QSVRTFVADG
GECLIAQSYA KNMGLYGERV GALSIVCKSA DVASKVESQV KLVVRPMYSS PPIHGASIVA
TILKSSDMYN NWTIELKEMA DRIKSMRQQL FEAIQARGTP GDWSHIIKQI GMFTFTGLNK
EQVEFMTKEF HIYMTSDGRI SMAGLSSKTV PHLADAMHAA VTRLG
