ID A0A0D9YZP3_9ORYZ Unreviewed; 458 AA.
AC A0A0D9YZP3;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM02G37210.1};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM02G37210.1}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM02G37210.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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 AlphaFoldDB; A0A0D9YZP3; -.
DR STRING; 40148.A0A0D9YZP3; -.
DR EnsemblPlants; OGLUM02G37210.1; OGLUM02G37210.1; OGLUM02G37210.
DR Gramene; OGLUM02G37210.1; OGLUM02G37210.1; OGLUM02G37210.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR Proteomes; UP000026961; Unassembled WGS sequence.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
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 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|RuleBase:RU000480};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898};
KW Reference proteome {ECO:0000313|Proteomes:UP000026961};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 84..450
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 458 AA; 50381 MW; 09CA7F41F1AE6961 CRC64;
MASAPFAVSS SPAASALAAR SKVLRGGRSE ARTGCRLGIT RKNFGRVMMA LAVDVSRFEG
VPMAPPDPIL GVSEAFKADQ NDLKLNLGVG AYRTEELQPY VLNVVKKAET LMLEKGENKE
YLPIEGLAAF NKATAELLFG ADNPVLKQGR VATLQSLSGT GSLRLAAAFI QRYFPEAKVL
ISSPTWGNHK NIFNDAKVPW SEYRYYDPKT VGLDFEGMIA DIQAAPDGSF VLLHGCAHNP
TGIDPTLEQW EKIADVIQEK KHMPFFDVAY QGFASGSLDE DASSVRLFVQ RGLEVFVAQS
YSKNLGLYAE RIGAINVVCS TPEVANRVKS QLKRLARPMY SNPPIHGARI VANVVGDPTM
FGEWKQEMEE MAGRIKNVRQ KLYDSLSAKD DSGKDWSFIL RQIGMFSYTG LNKTQSDNMT
DKWHIYMTKD GRISLAGLSL AKCEYLADAI IDSFHNVS
//
