ID   AATC_DAUCA              Reviewed;         405 AA.
AC   P28734;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Aspartate aminotransferase, cytoplasmic;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
OS   Daucus carota (Wild carrot).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; campanulids; Apiales; Apiaceae; Apioideae; Scandiceae; Daucinae;
OC   Daucus; Daucus sect. Daucus.
OX   NCBI_TaxID=4039;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16652971; DOI=10.1104/pp.100.1.374;
RA   Turano F.J., Weisemann J.M., Matthews B.F.;
RT   "Identification and expression of a cDNA clone encoding aspartate
RT   aminotransferase in carrot.";
RL   Plant Physiol. 100:374-381(1992).
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. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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; M92660; AAA33134.1; -; mRNA.
DR   PIR; T14311; T14311.
DR   AlphaFoldDB; P28734; -.
DR   SMR; P28734; -.
DR   PRIDE; P28734; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
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   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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..405
FT                   /note="Aspartate aminotransferase, cytoplasmic"
FT                   /id="PRO_0000123871"
FT   BINDING         37
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         134
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         187
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         379
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         251
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   405 AA;  44175 MW;  71DFB64B977769AD CRC64;
     MSSVFANVVR APEDPILGVT VAYHKDQSPN KLNLGVGAYR TEEGKPLVLN VVKKAEQMLV
     NDQSRVKEYL PIVGLADFNK LSAKLIFGAD SPAIQENRVA TVQCLSGTGS LRVGGEFLAR
     HYHEHTVYIP QPTWGNHPKI FTLAGLSVKT YRYYNPETRG LDFEGMLEDL GSAPLGAIVL
     LHACAHNPTG VDPTIEQWEQ IRQLMRSKSL LPFFDSAYQG FASGSLDADA QSVRIFVADG
     GECLAAQSYA KNMGLYGERV GALSIVCKTA DVASKVESQL KLVIRPMYSS PPLHGASIVA
     AILKDGDLYN EWTLELKAMA DRIISMRQEL FNALQAKGTP GDWSHIVKQI GMFTFTGLNS
     EQVTFMTNEY HIYLTSDGRI SMAGLSSRTV PHLADAIHAA VTGKA