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Database: UniProt/TrEMBL
Entry: W1NVA1_AMBTC
LinkDB: W1NVA1_AMBTC
Original site: W1NVA1_AMBTC 
ID   W1NVA1_AMBTC            Unreviewed;       452 AA.
AC   W1NVA1;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   RecName: Full=Aspartate aminotransferase {ECO:0000256|RuleBase:RU000480};
DE            EC=2.6.1.1 {ECO:0000256|RuleBase:RU000480};
GN   ORFNames=AMTR_s00109p00068640 {ECO:0000313|EMBL:ERM98604.1};
OS   Amborella trichopoda.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Amborellales; Amborellaceae; Amborella.
OX   NCBI_TaxID=13333 {ECO:0000313|EMBL:ERM98604.1, ECO:0000313|Proteomes:UP000017836};
RN   [1] {ECO:0000313|Proteomes:UP000017836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=24357323;
RG   Amborella Genome Project;
RT   "The Amborella genome and the evolution of flowering plants.";
RL   Science 342:1241089-1241089(2013).
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; KI395307; ERM98604.1; -; Genomic_DNA.
DR   RefSeq; XP_006833326.1; XM_006833263.2.
DR   AlphaFoldDB; W1NVA1; -.
DR   STRING; 13333.W1NVA1; -.
DR   EnsemblPlants; ERM98604; ERM98604; AMTR_s00109p00068640.
DR   GeneID; 18426621; -.
DR   Gramene; ERM98604; ERM98604; AMTR_s00109p00068640.
DR   KEGG; atr:18426621; -.
DR   eggNOG; KOG1411; Eukaryota.
DR   HOGENOM; CLU_032440_1_2_1; -.
DR   OMA; FIFICEY; -.
DR   OrthoDB; 360at2759; -.
DR   Proteomes; UP000017836; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IBA:GO_Central.
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   GO; GO:0006979; P:response to oxidative stress; 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; IPR018028; Catalase.
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:SF22; ASPARTATE AMINOTRANSFERASE, MITOCHONDRIAL; 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.
DR   PROSITE; PS51402; CATALASE_3; 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:UP000017836};
KW   Transferase {ECO:0000256|RuleBase:RU000480}.
FT   DOMAIN          78..444
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   452 AA;  49155 MW;  B703C6EFFC2C6959 CRC64;
     MTGTSPAVSP LDSVAFRRIS AVSRHLGHRS EMDSQDQSLS LSKTAGHGFS VFESINQAPE
     DPILGVTVAY NKDPSPVKLN LGVGAYRTEE GKPLVLNVVK QAEQLLINDG SRVKEYLPIT
     GLADFNKLSA TLILGADSPA ILEKRVATVQ GLSGTGSLRV GAEFLTRHYY NRTIYIPLPT
     WGNHPKVFTI AGLSVKTYRY YDPATRGLDF QGLLEDLGLA PSGAVVLLHA CAHNPTGVDP
     TPEQWEQIRQ LIRSKGFLPF FDSAYQGFAS GSLDTDAQSV RMFVADGGEL FAAQSYAKNM
     GLYGERVGAL SVVCKSAAVA GRVESQLKLV IRPMYSNPPL HGASIVAKIL GDRNLFNEWT
     VELKAMADRI ISMRKQLYDA LCSRGTPGDW SHIIKQIGMF TFTGLNTEQV AFMTKEYHIY
     MTSDGRISMA GLSSRTVPHL ADAIHAAVTR FA
//
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