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}.
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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
//