ID A0A0E0NM66_ORYRU Unreviewed; 428 AA.
AC A0A0E0NM66;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI02G37510.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI02G37510.1}
RP IDENTIFICATION.
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 AlphaFoldDB; A0A0E0NM66; -.
DR STRING; 4529.A0A0E0NM66; -.
DR EnsemblPlants; ORUFI02G37510.1; ORUFI02G37510.1; ORUFI02G37510.
DR Gramene; ORUFI02G37510.1; ORUFI02G37510.1; ORUFI02G37510.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR OMA; VGACTIV; -.
DR Proteomes; UP000008022; 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:UP000008022};
KW Transferase {ECO:0000256|RuleBase:RU000480}.
FT DOMAIN 54..420
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 428 AA; 47503 MW; CE3C513C50CAB223 CRC64;
MAFIGKAWCF DPNFGRVMMA LAVDVSRFEG VPMAPPDPIL GVSEAFKADQ NDLKLNLGVG
AYRTEELQPY VLNVVKKAET LMLEKGENKE YLPIEGLAAF NKATAELLFG ADNPVLKQGR
VATLQSLSGT GSLRLAAAFI QRYFPEAKVL ISSPTWGNHK NIFNDAKVPW SEYRYYDPKT
VGLDFEGMIA DIQAAPDGSF VLLHGCAHNP TGIDPTPEQW EKIADVIQEK KHMPFFDVAY
QGFASGSLDE DASSVRLFVQ RGLEVFVAQS YSKNLGLYAE RIGAINVVCS TPEVANRVKS
QLKRLARPMY SNPPIHGARI VANVVGDPTM FGEWKQEMEE MAGRIKNVRQ KLYDSLSAKD
DSGKDWSFIL RQIGMFSYTG LNKTQSDNMT DKWHIYMTKD GRISLAGLSL AKCEYLADAI
IDSFHNVS
//