ID M1BTN1_SOLTU Unreviewed; 425 AA.
AC M1BTN1;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN Name=102605189 {ECO:0000313|EnsemblPlants:PGSC0003DMT400052597};
OS Solanum tuberosum (Potato).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400052597, ECO:0000313|Proteomes:UP000011115};
RN [1] {ECO:0000313|Proteomes:UP000011115}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX PubMed=21743474; DOI=10.1038/nature10158;
RG The Potato Genome Sequencing Consortium;
RT "Genome sequence and analysis of the tuber crop potato.";
RL Nature 475:189-195(2011).
RN [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400052597}
RP IDENTIFICATION.
RC STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400052597};
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
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:0000256|RuleBase:RU000480};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU000480}.
CC -!- MISCELLANEOUS: In eukaryotes there are cytoplasmic, mitochondrial and
CC chloroplastic isozymes. {ECO:0000256|RuleBase:RU000480}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00007441}.
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DR RefSeq; XP_006348885.1; XM_006348823.2.
DR AlphaFoldDB; M1BTN1; -.
DR STRING; 4113.M1BTN1; -.
DR PaxDb; 4113-PGSC0003DMT400052597; -.
DR EnsemblPlants; PGSC0003DMT400052597; PGSC0003DMT400052597; PGSC0003DMG400020416.
DR GeneID; 102605189; -.
DR Gramene; PGSC0003DMT400052597; PGSC0003DMT400052597; PGSC0003DMG400020416.
DR KEGG; sot:102605189; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; M1BTN1; -.
DR OMA; MGFEMFC; -.
DR OrthoDB; 360at2759; -.
DR Proteomes; UP000011115; Unassembled WGS sequence.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
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:SF54; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 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 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000011115};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 53..418
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 425 AA; 47037 MW; EFC890E130E6C7CB CRC64;
MAIRAAISGS HLKLSSSSLG ARSLSSWWRN VEPAPKDPIL GVTEAFLADP SPDKVNVGVG
AYRDDNGKPV VLECVREAER RIAGGFNMEY LPMGGSVNMI QESLKLAYGE NSDLIKDKRI
AAIQALSGTG ACRIFADFQK RFCPDSQIYI PVPTWSNHHN IWRDAHVPER TYHYYHAESK
GLDFAAMMDD IKNAPKGSFF LLHACAHNPT GVDPTEEQWR EISHQFKVKG HFALFDMAYQ
GFASGYPEKD AKAIRIFLED GHPIACAQSY AKNMGLYGQR VGCLSVVCED EKQAVAVKSQ
LQQLARPMYS NPPVHGALVV STILGDPNLK NLWLGEVKGM ADRIIGMRTA LRENLEKLGS
PLSWEHITNQ IGMFCYSGMT PEQVDRLTKE YHIYMTRNGR ISMAGVTTGN VGYLANAIHE
VTKSA
//
