ID   AATM_CATRO              Reviewed;          28 AA.
AC   P85310;
DT   04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 31.
DE   RecName: Full=Aspartate aminotransferase, mitochondrial;
DE            EC=2.6.1.1;
DE   AltName: Full=Glutamate oxaloacetate transaminase 2;
DE   AltName: Full=Transaminase A;
DE   Flags: Fragments;
OS   Catharanthus roseus (Madagascar periwinkle) (Vinca rosea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Gentianales; Apocynaceae; Rauvolfioideae; Vinceae;
OC   Catharanthinae; Catharanthus.
OX   NCBI_TaxID=4058;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE.
RA   Varman P.A.M., Ranjitha Kumari B.D.;
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: Plays a key role in amino acid metabolism. Important for
CC       metabolite exchange between mitochondria and cytosol (By similarity).
CC       {ECO:0000250}.
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:0000250|UniProtKB:P00508};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250|UniProtKB:P00508};
CC   -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P00508}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:P00508}.
CC   -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC       chloroplastic isozymes. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000255}.
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DR   AlphaFoldDB; P85310; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; ISS:UniProtKB.
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.
PE   1: Evidence at protein level;
KW   Aminotransferase; Direct protein sequencing; Mitochondrion;
KW   Pyridoxal phosphate; Transferase.
FT   CHAIN           <1..>28
FT                   /note="Aspartate aminotransferase, mitochondrial"
FT                   /id="PRO_0000312771"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000305"
FT   NON_TER         1
FT   NON_TER         28
SQ   SEQUENCE   28 AA;  3031 MW;  8D8BE476675B227A CRC64;
     DDNGKPYVLP SVRTCGFDFT GAVEDISK