ID   AAT1_MEDSA              Reviewed;         418 AA.
AC   P28011; Q40324;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Aspartate aminotransferase 1;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
GN   Name=AAT-1;
OS   Medicago sativa (Alfalfa).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Trifolieae; Medicago.
OX   NCBI_TaxID=3879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Saranac; TISSUE=Seedling;
RX   PubMed=8049365; DOI=10.1007/bf00043868;
RA   Gregerson R.G., Miller S.S., Petrowski M., Gantt J.S., Vance C.P.;
RT   "Genomic structure, expression and evolution of the alfalfa aspartate
RT   aminotransferase genes.";
RL   Plant Mol. Biol. 25:387-399(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 2-418.
RC   STRAIN=cv. Ladak; TISSUE=Leaf;
RX   PubMed=1753949; DOI=10.1007/bf00293827;
RA   Udvardi M.K., Kahn M.L.;
RT   "Isolation and analysis of a cDNA clone that encodes an alfalfa (Medicago
RT   sativa) aspartate aminotransferase.";
RL   Mol. Gen. Genet. 231:97-105(1991).
CC   -!- FUNCTION: Important for the metabolism of amino acids and Krebs-cycle
CC       related organic acids. In plants, it is involved in nitrogen metabolism
CC       and in aspects of carbon and energy 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: Nodules, roots, stems and leaves, in decreasing
CC       order of aspartate aminotransferase 1 concentration. Is the predominant
CC       aspartate aminotransferase isoenzyme in roots.
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; L25334; AAB46610.1; -; Genomic_DNA.
DR   EMBL; X61577; CAA43779.1; -; mRNA.
DR   PIR; S46315; S46315.
DR   AlphaFoldDB; P28011; -.
DR   SMR; P28011; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro.
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   2: Evidence at transcript level;
KW   Aminotransferase; Cytoplasm; Pyridoxal phosphate; Transferase.
FT   CHAIN           1..418
FT                   /note="Aspartate aminotransferase 1"
FT                   /id="PRO_0000123870"
FT   MOD_RES         264
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        3..4
FT                   /note="SQ -> RE (in Ref. 2; CAA43779)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        408
FT                   /note="H -> D (in Ref. 2; CAA43779)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   418 AA;  45691 MW;  389B9EA93CF5BCE6 CRC64;
     MASQNITPSP TASSDSVFAH LVRAPEDPIL GVTVAYNKDP SPIKLNLGVG AYRTEEGKPL
     VLDVVRRVER QLLNDMSRNK EYIPIVGLAD FNKLSAKLIF GADSPAIQEN RVTTVQGLSG
     TGSLRVGGEF LAKHYHQRII YLPTPTWGNH TKVFNLAGLT VKTYRYYAPA TRGLDFQGLL
     EDLGSAPSGS VVLLHACAHN PTGVDPTLEQ WEQIRQLIRS KSLLPFFDSA YQGFASGSLD
     ADAQPVRLFV ADGGELLVAQ SYAKNMGLYG ERVGALSIVS KSADVSSRVE SQLKLVIRPM
     YSSPPIHGAS IVAAILKDRD LYNDWTIELK AMADRIINMR QQLFDALRAR GTPGDWSHII
     KQIGMFTFTG LNPEQVSILT KEYHIYLTSD GRISMAGLSS KTVPHLAHAI HAVVTRVA