ID   A0A1I6LKA5_9RHOB        Unreviewed;       400 AA.
AC   A0A1I6LKA5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE            EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN   ORFNames=SAMN05444714_0621 {ECO:0000313|EMBL:SFS03967.1};
OS   Yoonia litorea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Yoonia.
OX   NCBI_TaxID=1123755 {ECO:0000313|EMBL:SFS03967.1, ECO:0000313|Proteomes:UP000198926};
RN   [1] {ECO:0000313|EMBL:SFS03967.1, ECO:0000313|Proteomes:UP000198926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29433 {ECO:0000313|EMBL:SFS03967.1,
RC   ECO:0000313|Proteomes:UP000198926};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|RuleBase:RU000481};
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|ARBA:ARBA00007441,
CC       ECO:0000256|RuleBase:RU000481}.
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DR   EMBL; FOZM01000001; SFS03967.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6LKA5; -.
DR   STRING; 1123755.SAMN05444714_0621; -.
DR   OrthoDB; 9763453at2; -.
DR   Proteomes; UP000198926; Unassembled WGS sequence.
DR   GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:RHEA.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; 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; 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; PTHR46383; ASPARTATE AMINOTRANSFERASE; 1.
DR   PANTHER; PTHR46383:SF1; ASPARTATE AMINOTRANSFERASE; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
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:RU000481,
KW   ECO:0000313|EMBL:SFS03967.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198926};
KW   Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:SFS03967.1}.
FT   DOMAIN          32..392
FT                   /note="Aminotransferase class I/classII"
FT                   /evidence="ECO:0000259|Pfam:PF00155"
SQ   SEQUENCE   400 AA;  43006 MW;  4B4B6C674F342576 CRC64;
     MTFLSATLDR VKPSPTIAVT TKAAELKAAG RDVIGLGAGE PDFDTPQNIK DAAIAAINAG
     KTKYTAVDGI PELKQAICAK FARDNGLTYS PAQVSVGTGG KQVLYNAFMA TLNASDEVII
     PAPYWVSYPD MVLLAGGTPV TVEATLEANF KITAEQLEAA ITPKTKWFLF NSPSNPTGAG
     YSWDELKALT DVLLRHPHVW VMTDDMYEHL AYDDFAFCTP AQVEPQLYDR TLTVNGVSKA
     YAMTGWRIGY AAGPEALIKA MRKVQSQSTS NPCSVSQWAA VEALNGTQDF LAPNNEIFTR
     RRDLVVEMLN QAPGIVCPKP EGAFYVYPSI AECIGKTSAG GALIENDEAF ATALLEEKGV
     AVVFGAAFGL SPNFRVSYAT SDEALKEACQ RIIDFCNALK
//