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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//
