ID   AAT1_ARATH              Reviewed;         430 AA.
AC   P46643;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 177.
DE   RecName: Full=Aspartate aminotransferase, mitochondrial;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
DE   Flags: Precursor;
GN   Name=ASP1; OrderedLocusNames=At2g30970; ORFNames=F7F1.18;
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=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
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   [7]
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP   ANALYSIS].
RC   STRAIN=cv. Landsberg erecta;
RX   PubMed=14671022; DOI=10.1105/tpc.016055;
RA   Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA   Millar A.H.;
RT   "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT   signaling and regulatory components, provides assessment of targeting
RT   prediction programs, and indicates plant-specific mitochondrial proteins.";
RL   Plant Cell 16:241-256(2004).
RN   [9]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=18318836; DOI=10.1111/j.1742-4658.2008.06279.x;
RA   Funakoshi M., Sekine M., Katane M., Furuchi T., Yohda M., Yoshikawa T.,
RA   Homma H.;
RT   "Cloning and functional characterization of Arabidopsis thaliana D-amino
RT   acid aminotransferase--D-aspartate behavior during germination.";
RL   FEBS J. 275:1188-1200(2008).
CC   -!- FUNCTION: Amino acid aminotransferase important for the metabolism of
CC       amino acids and Krebs-cycle related organic acids. No activity with D-
CC       Asp or D-Ala as amino donors. In plants, it is involved in nitrogen
CC       metabolism and in aspects of carbon and energy metabolism.
CC       {ECO:0000269|PubMed:18318836, ECO:0000269|PubMed:7894512,
CC       ECO:0000269|PubMed:9535706, ECO:0000269|PubMed:9611168}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate;
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:18318836, ECO:0000269|PubMed:9535706};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 mM for L-aspartate {ECO:0000269|PubMed:18318836};
CC         KM=3 mM for L-aspartate {ECO:0000269|PubMed:9535706};
CC         KM=0.26 mM for 2-oxoglutarate {ECO:0000269|PubMed:9535706};
CC         KM=8.15 mM for L-glutamate {ECO:0000269|PubMed:9535706};
CC         KM=0.038 mM for oxaloacetate {ECO:0000269|PubMed:9535706};
CC         Note=kcat is 205 sec(-1) for the forward reaction. kcat is 319
CC         sec(-1) for the reverse reaction. {ECO:0000269|PubMed:9535706};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000269|PubMed:14671022}.
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}.
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DR   EMBL; U15026; AAA79369.1; -; mRNA.
DR   EMBL; AC004669; AAC20731.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08468.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC08469.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7036974.1; -; Genomic_DNA.
DR   EMBL; AY059912; AAL24394.1; -; mRNA.
DR   EMBL; AY128806; AAM91206.1; -; mRNA.
DR   PIR; H84714; H84714.
DR   RefSeq; NP_001118421.1; NM_001124949.1.
DR   RefSeq; NP_180654.1; NM_128651.5.
DR   AlphaFoldDB; P46643; -.
DR   SMR; P46643; -.
DR   BioGRID; 2997; 2.
DR   FunCoup; P46643; 3064.
DR   STRING; 3702.P46643; -.
DR   GlyGen; P46643; 1 site.
DR   MetOSite; P46643; -.
DR   PaxDb; 3702-P46643; -.
DR   ProteomicsDB; 244373; -.
DR   GeneID; 817648; -.
DR   KEGG; ath:AT2G30970; -.
DR   Araport; AT2G30970; -.
DR   TAIR; AT2G30970; ASP1.
DR   eggNOG; KOG1411; Eukaryota.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   InParanoid; P46643; -.
DR   OMA; GTWTHIT; -.
DR   PhylomeDB; P46643; -.
DR   SABIO-RK; P46643; -.
DR   CD-CODE; 4299E36E; Nucleolus.
DR   PRO; PR:P46643; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate transaminase 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:0006536; P:glutamate metabolic process; ISS:UniProtKB.
DR   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000015; Aspartate aminotransferase; 1.
DR   FunFam; 3.90.1150.10:FF:000001; Aspartate aminotransferase; 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_large.
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   NCBIfam; NF006719; PRK09257.1; 1.
DR   PANTHER; PTHR11879; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF54; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 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   Aminotransferase; Mitochondrion; Pyridoxal phosphate; Reference proteome;
KW   Transferase; Transit peptide.
FT   TRANSIT         1..28
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           29..430
FT                   /note="Aspartate aminotransferase, mitochondrial"
FT                   /id="PRO_0000001209"
FT   BINDING         65
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P23542"
FT   BINDING         160
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P23542"
FT   BINDING         213
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P23542"
FT   BINDING         405
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250|UniProtKB:P23542"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250|UniProtKB:P23542"
SQ   SEQUENCE   430 AA;  47758 MW;  A6525B958B0249EF CRC64;
     MALAMMIRNA ASKRGMTPIS GHFGGLRSMS SWWKSVEPAP KDPILGVTEA FLADPSPEKV
     NVGVGAYRDD NGKPVVLECV REAEKRLAGS TFMEYLPMGG SAKMVDLTLK LAYGDNSEFI
     KDKRIAAVQT LSGTGACRLF ADFQKRFSPG SQIYIPVPTW SNHHNIWKDA QVPQKTYHYY
     HPETKGLDFS ALMDDVKNAP EGSFFLLHAC AHNPTGVDPT EEQWREISQL FKAKKHFAFF
     DMAYQGFASG DPARDAKSIR IFLEDGHHIG ISQSYAKNMG LYGQRVGCLS VLCEDPKQAV
     AVKSQLQQLA RPMYSNPPLH GAQLVSTILE DPELKSLWLK EVKVMADRII GMRTTLRESL
     EKLGSPLSWE HVTKQIGMFC YSGLTPEQVD RLTSEYHIYM TRNGRISMAG VTTGNVGYLA
     NAIHEVTKSS
//