ID A0A816I5D1_BRANA Unreviewed; 450 AA. AC A0A816I5D1; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 25-MAY-2022, entry version 3. DE RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480}; DE EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480}; GN ORFNames=DARMORV10_C03P05800.1 {ECO:0000313|EMBL:CAF1697056.1}; OS Brassica napus (Rape). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica. OX NCBI_TaxID=3708 {ECO:0000313|EMBL:CAF1697056.1}; RN [1] {ECO:0000313|EMBL:CAF1697056.1} RP NUCLEOTIDE SEQUENCE. RG Genoscope - CEA; RA William W.; RL Submitted (JAN-2021) to the EMBL/GenBank/DDBJ databases. 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|ARBA:ARBA00000984, CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; HG994367; CAF1697056.1; -; Genomic_DNA. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. 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 3: Inferred from homology; KW Aminotransferase {ECO:0000256|RuleBase:RU000480}; KW Transferase {ECO:0000256|RuleBase:RU000480}. FT DOMAIN 75..442 FT /note="Aminotran_1_2" FT /evidence="ECO:0000259|Pfam:PF00155" SQ SEQUENCE 450 AA; 49133 MW; F473F0FF662BC11A CRC64; MKTNDFSSST SPSDRRIGAL FRHLTAGTDA DRVSSVFASP TSGGAGGSVF AHLVQAPEDA ILGVTIAYNK DPSPIKLNLG VGAYRTEEGK PLVLNVVRKA EQQLINDRSR IKEYLPIVGL VEFNKLSAKL ILGADSPAIR ENRVTTVECL SGTGSLRVGG EFLARHYHQK TIYIPQPTWG NHPKIFTLAG LSVKTYRYYD PSTRGLNFQG LLEDLGAAPQ GSIVLLHACA HNPTGVDPTL EQWEQIRKLM RSKGLMPFFD SAYQGFASGS LDTDAKPIRM FVADGGELLV AQSYAKNMGL YGERVGALSI VCKAADVAGR VESQLKLVIR PMYSNPPIHG ASIVAVILRD RNLFNEWTLE LKAMADRIIS MRKQLFEALR ARGTPGDWTH IIKQIGMFTF TGLNPAQVSY MTKEYHIYMT SDGRISMAGL SSKTVPHLAD AIHAVVTKAL //