ID   AATM_LUPAN              Reviewed;         454 AA.
AC   P26563;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   22-FEB-2023, entry version 112.
DE   RecName: Full=Aspartate aminotransferase P2, mitochondrial;
DE            EC=2.6.1.1;
DE   AltName: Full=Transaminase A;
DE   Flags: Precursor; Fragment;
OS   Lupinus angustifolius (Narrow-leaved blue lupine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   genistoids sensu lato; core genistoids; Genisteae; Lupinus.
OX   NCBI_TaxID=3871;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Uniharvest; TISSUE=Root nodule;
RX   PubMed=1623192; DOI=10.1007/bf00023394;
RA   Reynolds P.H.S., Smith L.A., Jones W.T., Dickson J.M.J., Jones S.J.,
RA   Rodber K., Liddane C.P.;
RT   "Molecular cloning of a cDNA encoding aspartate aminotransferase-P2 from
RT   lupin root nodules.";
RL   Plant Mol. Biol. 19:465-472(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: Mitochondrion matrix.
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; X59761; CAA42430.1; -; mRNA.
DR   PIR; S22465; XNYLB.
DR   AlphaFoldDB; P26563; -.
DR   SMR; P26563; -.
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: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   CDD; cd00609; AAT_like; 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.
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; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR11879:SF46; ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC; 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   2: Evidence at transcript level;
KW   Aminotransferase; Mitochondrion; Pyridoxal phosphate; Transferase;
KW   Transit peptide.
FT   TRANSIT         <1..49
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           50..454
FT                   /note="Aspartate aminotransferase P2, mitochondrial"
FT                   /id="PRO_0000001212"
FT   BINDING         86
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         182
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         235
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   BINDING         428
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         299
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
SQ   SEQUENCE   454 AA;  49916 MW;  744CC12F1D81E739 CRC64;
     SSLLSIPSLS LQYNDKLKVG GNSLRFSKEQ SNTFSNAKSS CRISMVAAVN VSRFEGIPMA
     PPDPILGVSE AFRADTSDAK LNLGVGAYRT EELQPYVLKV VNKAENLMLE RGQNKEYLAI
     EGLAAFNKAT AELLLGADNP AIKQQRVATV QGLSGTGSLR LGAALIERYF PGAKVLISAP
     TWGNHKNIFN DARVPWSEYR YYDPKTVGLD FEGMIEDIKA APEGTFVLLH GCAHNPTGID
     PTPEQWEKIA DVIQEKNHIP FFDVAYQGFA SGSLDEDAAS VRLFVARGLE VLVAQSYSKN
     LGLYAERIGA INVISSSPES AARVKSQLKR IARPMYSNPP VHGARIVADI VGNPALFDEW
     KVEMEMMAGR IKNVRQQLYD SISSKDKSGK DWSFILKQIG MFSYTGLNKN QSDNMTNKWH
     VYMTKDGRIS LAGLSLAKCE YLADAIIDSF HYVS
//