ID I3TVE6_TISMK Unreviewed; 400 AA.
AC I3TVE6;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Aminotransferase {ECO:0000256|RuleBase:RU000481};
DE EC=2.6.1.- {ECO:0000256|RuleBase:RU000481};
GN Name=aatA {ECO:0000313|EMBL:AFK56734.1};
GN OrderedLocusNames=TMO_c0124 {ECO:0000313|EMBL:AFK56734.1};
OS Tistrella mobilis (strain KA081020-065).
OG Plasmid pTM3 {ECO:0000313|EMBL:AFK56734.1,
OG ECO:0000313|Proteomes:UP000005258}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK56734.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK56734.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|Proteomes:UP000005258};
RC PLASMID=Plasmid pTM3 {ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003239; AFK56734.1; -; Genomic_DNA.
DR RefSeq; WP_014747723.1; NC_017958.1.
DR AlphaFoldDB; I3TVE6; -.
DR KEGG; tmo:TMO_c0124; -.
DR PATRIC; fig|1110502.3.peg.4987; -.
DR HOGENOM; CLU_017584_4_3_5; -.
DR Proteomes; UP000005258; Plasmid pTM3.
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:AFK56734.1}; Plasmid {ECO:0000313|EMBL:AFK56734.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Transferase {ECO:0000256|RuleBase:RU000481, ECO:0000313|EMBL:AFK56734.1}.
FT DOMAIN 32..392
FT /note="Aminotransferase class I/classII"
FT /evidence="ECO:0000259|Pfam:PF00155"
SQ SEQUENCE 400 AA; 42885 MW; E321BE184963DA16 CRC64;
MSVIADRLSR IKPSPTLAVT AKAAQLKEAG RDIIGLGAGE PDFDTPDNIK DAAIKAIRDG
QTKYTPVQGT RALVEAVRNK FKRENGLDYA ANQIVVGTGG KQVLYNAFMA TLNPGDEVII
PAPYWVSYPD MALLAEGVPV FVEAGRETGF KIQPAQLEAA ITPRTKWLIL NSPSNPSGAA
YSAAELRALA DVLVRHPHVL VLTDDMYEHI LFDGFEFATI AQVAPELYDR TLTVNGVSKA
YSMTGWRIGY AGGPANIIKA MTAIQSQSTS NPSSVSQAAA VEALNGPQDF IAERAARFQV
RRDLVVRLLN QAPGLVCPVP EGAFYVYPSC EGVLGKKTPS GQVIGSSEDF ATYLLEHVGI
AVVHGAAFGL DPYFRISYAT ADEVLEEACG RIARACNELV
//
