AAT1_ARATH
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 03-AUG-2022, entry version 162.
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 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 [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 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 [8]
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=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:18318836, ECO:0000269|PubMed:9535706};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.0 mM for L-aspartate {ECO:0000269|PubMed:18318836};
CC KM=3.0 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 sec(-
CC 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; 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; 1.
DR STRING; 3702.AT2G30970.1; -.
DR MetOSite; P46643; -.
DR PaxDb; P46643; -.
DR PRIDE; P46643; -.
DR ProteomicsDB; 244373; -.
DR EnsemblPlants; AT2G30970.1; AT2G30970.1; AT2G30970.
DR EnsemblPlants; AT2G30970.2; AT2G30970.2; AT2G30970.
DR GeneID; 817648; -.
DR Gramene; AT2G30970.1; AT2G30970.1; AT2G30970.
DR Gramene; AT2G30970.2; AT2G30970.2; AT2G30970.
DR KEGG; ath:AT2G30970; -.
DR Araport; AT2G30970; -.
DR TAIR; locus:2052851; AT2G30970.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P46643; -.
DR OMA; QLKKQWY; -.
DR OrthoDB; 1104596at2759; -.
DR PhylomeDB; P46643; -.
DR SABIO-RK; P46643; -.
DR PRO; PR:P46643; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; P46643; baseline and differential.
DR Genevisible; P46643; AT.
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 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: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 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
