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Database: UniProt
Entry: A0A0E0NM66_ORYRU
LinkDB: A0A0E0NM66_ORYRU
Original site: A0A0E0NM66_ORYRU 
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
//
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