AATC_ORYSJ
ID AATC_ORYSJ Reviewed; 407 AA.
AC P37833; Q5JMF4; Q7F594;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aspartate aminotransferase, cytoplasmic;
DE EC=2.6.1.1;
DE AltName: Full=Transaminase A;
GN OrderedLocusNames=Os01g0760600, LOC_Os01g55540;
GN ORFNames=P0460E08.21, P0512C01.10;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX NCBI_TaxID=39947;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Nipponbare; TISSUE=Callus;
RX PubMed=9039500; DOI=10.1093/dnares/3.5.303;
RA Song J., Sasaki T., Minobe Y.;
RT "Characterization and mapping of cDNA encoding aspartate aminotransferase
RT in rice, Oryza sativa L.";
RL DNA Res. 3:303-310(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Callus;
RX PubMed=15659629; DOI=10.1105/tpc.104.028456;
RA Moriguchi K., Suzuki T., Ito Y., Yamazaki Y., Niwa Y., Kurata N.;
RT "Functional isolation of novel nuclear proteins showing a variety of
RT subnuclear localizations.";
RL Plant Cell 17:389-403(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=12447438; DOI=10.1038/nature01184;
RA Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT "The genome sequence and structure of rice chromosome 1.";
RL Nature 420:312-316(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [5]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
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: Cytoplasm {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=BAD87343.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; D14673; BAA03504.1; -; mRNA.
DR EMBL; AB110193; BAC78585.1; -; mRNA.
DR EMBL; AP003256; BAB61211.1; -; Genomic_DNA.
DR EMBL; AP003274; BAD87343.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AP014957; BAS74451.1; -; Genomic_DNA.
DR PIR; JC5124; JC5124.
DR RefSeq; XP_015621160.1; XM_015765674.1.
DR AlphaFoldDB; P37833; -.
DR SMR; P37833; -.
DR STRING; 4530.OS01T0760600-01; -.
DR PaxDb; P37833; -.
DR PRIDE; P37833; -.
DR EnsemblPlants; Os01t0760600-04; Os01t0760600-04; Os01g0760600.
DR GeneID; 4325621; -.
DR Gramene; Os01t0760600-04; Os01t0760600-04; Os01g0760600.
DR KEGG; osa:4325621; -.
DR eggNOG; KOG1411; Eukaryota.
DR HOGENOM; CLU_032440_1_2_1; -.
DR InParanoid; P37833; -.
DR OrthoDB; 1104596at2759; -.
DR PlantReactome; R-OSA-1119281; Aspartate biosynthesis I.
DR PlantReactome; R-OSA-1119393; Asparagine degradation I.
DR PlantReactome; R-OSA-1119553; Asparagine biosynthesis.
DR Proteomes; UP000000763; Chromosome 1.
DR Proteomes; UP000059680; Chromosome 1.
DR ExpressionAtlas; P37833; baseline and differential.
DR Genevisible; P37833; OS.
DR GO; GO:0005737; C:cytoplasm; ISS:Gramene.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
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:0006522; P:alanine metabolic process; ISS:Gramene.
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 GO; GO:0006807; P:nitrogen compound metabolic process; ISS:Gramene.
DR GO; GO:0006099; P:tricarboxylic acid cycle; ISS:Gramene.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 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; PTHR11879; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00799; TRANSAMINASE.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 2: Evidence at transcript level;
KW Aminotransferase; Cytoplasm; Pyridoxal phosphate; Reference proteome;
KW Transferase.
FT CHAIN 1..407
FT /note="Aspartate aminotransferase, cytoplasmic"
FT /id="PRO_0000123874"
FT BINDING 39
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 136
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 189
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT BINDING 381
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000250"
FT MOD_RES 253
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 44507 MW; E1D0AAD663AAE887 CRC64;
MASSSVFAGL AQAPEDPILG VTVAYNKDPS PVKVNLGVGA YRTEEGKPLV LNVVRRAEQM
LINNPSRVKE YLPITGLADF NKLSAKLIFG ADSPAIQENR VATVQCLSGT GSLRVGGEFL
ARHYHERTIY IPQPTWGNHP KVFTLAGLTV RSYRYYDPAT RGLDFQGLLE DLGSAPSGAI
VLLHACAHNP TGVDPTLDQW EQIRQLMRSK ALLPFFDSAY QGFASGSLDQ DAQSVRMFVA
DGGELLMAQS YAKNMGLYGE RVGALSIVCG SADVAVRVES QLKLVIRPMY SNPPIHGASI
VATILKDSAM FNEWTVELKG MADRIISMRQ QLFDALKTRE TPGDWSHIIK QIGMFTFTGL
NSDQVAFMRQ EYHIYMTSDG RISMAGLSGR TIPHLADAIH AAVTKLK
