AAT_ECOLI
ID AAT_ECOLI Reviewed; 396 AA.
AC P00509;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Aspartate aminotransferase;
DE Short=AspAT;
DE EC=2.6.1.1 {ECO:0000269|PubMed:10556573};
DE AltName: Full=Transaminase A;
GN Name=aspC; OrderedLocusNames=b0928, JW0911;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=6378205; DOI=10.1016/0006-291x(84)90439-x;
RA Kondo K., Wakabayashi S., Yagi T., Kagamiyama H.;
RT "The complete amino acid sequence of aspartate aminotransferase from
RT Escherichia coli: sequence comparison with pig isoenzymes.";
RL Biochem. Biophys. Res. Commun. 122:62-67(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3897210; DOI=10.1093/oxfordjournals.jbchem.a135173;
RA Kuramitsu S., Okuno S., Ogawa T., Ogawa H., Kagamiyama H.;
RT "Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the
RT aspC gene.";
RL J. Biochem. 97:1259-1262(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3521591; DOI=10.1042/bj2340593;
RA Fotheringham I.G., Dacey S.A., Taylor P.P., Smith T.J., Hunter M.G.,
RA Finlay M.E., Primrose S.B., Parker D.M., Edwards R.M.;
RT "The cloning and sequence analysis of the aspC and tyrB genes from
RT Escherichia coli K12. Comparison of the primary structures of the aspartate
RT aminotransferase and aromatic aminotransferase of E. coli with those of the
RT pig aspartate aminotransferase isoenzymes.";
RL Biochem. J. 234:593-604(1986).
RN [4]
RP PROTEIN SEQUENCE.
RX PubMed=3298240; DOI=10.1016/s0021-9258(18)47463-7;
RA Kondo K., Wakabayashi S., Kagamiyama H.;
RT "Structural studies on aspartate aminotransferase from Escherichia coli.
RT Covalent structure.";
RL J. Biol. Chem. 262:8648-8657(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [8]
RP PROTEIN SEQUENCE OF 1-12.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [9]
RP MUTAGENESIS OF TYR-65.
RX PubMed=1868057; DOI=10.1021/bi00245a019;
RA Inoue K., Kuramitsu S., Okamoto A., Hirotsu K., Higuchi T., Kagamiyama H.;
RT "Site-directed mutagenesis of Escherichia coli aspartate aminotransferase:
RT role of Tyr70 in the catalytic processes.";
RL Biochemistry 30:7796-7801(1991).
RN [10]
RP MUTAGENESIS OF HIS-133.
RX PubMed=2007566; DOI=10.1016/s0021-9258(18)38086-4;
RA Yano T., Kuramitsu S., Tanase S., Morino Y., Hiromi K., Kagamiyama H.;
RT "The role of His143 in the catalytic mechanism of Escherichia coli
RT aspartate aminotransferase.";
RL J. Biol. Chem. 266:6079-6085(1991).
RN [11]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [12]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF ARG-280 AND ARG-374.
RX PubMed=10556573; DOI=10.1016/s0167-4838(99)00181-8;
RA Mahon M.M., Graber R., Christen P., Malthouse J.P.;
RT "The aspartate aminotransferase-catalysed exchange of the alpha-protons of
RT aspartate and glutamate: the effects of the R386A and R292V mutations on
RT this exchange reaction.";
RL Biochim. Biophys. Acta 1434:191-201(1999).
RN [13]
RP INDUCTION BY 2,4,6-TRINITROTOLUENE, AND BIOTECHNOLOGY.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=25561288; DOI=10.1007/s12013-014-0481-8;
RA Tan J., Kan N., Wang W., Ling J., Qu G., Jin J., Shao Y., Liu G., Chen H.;
RT "Construction of 2,4,6-trinitrotoluene biosensors with novel sensing
RT elements from Escherichia coli K-12 MG1655.";
RL Cell Biochem. Biophys. 72:417-428(2015).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
RX PubMed=2513875; DOI=10.1021/bi00446a030;
RA Smith D.L., Almo S.C., Toney M.D., Ringe D.;
RT "2.8-A-resolution crystal structure of an active-site mutant of aspartate
RT aminotransferase from Escherichia coli.";
RL Biochemistry 28:8161-8167(1989).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND MUTAGENESIS OF ARG-374.
RX PubMed=1993208; DOI=10.1021/bi00221a035;
RA Danishefsky A.T., Onnufer J.J., Petsko G.A., Ringe D.;
RT "Activity and structure of the active-site mutants R386Y and R386F of
RT Escherichia coli aspartate aminotransferase.";
RL Biochemistry 30:1980-1985(1991).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
RX PubMed=9891001; DOI=10.1074/jbc.274.4.2344;
RA Oue S., Okamoto A., Yano T., Kagamiyama H.;
RT "Redesigning the substrate specificity of an enzyme by cumulative effects
RT of the mutations of non-active site residues.";
RL J. Biol. Chem. 274:2344-2349(1999).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-183/PHE-214;
RP ALA-183/LEU-280; ALA-183/LEU-374 AND ALA-183/LEU-280/LEU-374 IN COMPLEXES
RP WITH PYRIDOXAL PHOSPHATE, COFACTOR, AND PYRIDOXAL PHOSPHATE AT LYS-246.
RX PubMed=11148029; DOI=10.1021/bi001403e;
RA Mizuguchi H., Hayashi H., Okada K., Miyahara I., Hirotsu K., Kagamiyama H.;
RT "Strain is more important than electrostatic interaction in controlling the
RT pKa of the catalytic group in aspartate aminotransferase.";
RL Biochemistry 40:353-360(2001).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE
RP AND SADTA, AND PYRIDOXAL PHOSPHATE AT LYS-246.
RX PubMed=17713924; DOI=10.1021/bi700663n;
RA Liu D., Pozharski E., Lepore B.W., Fu M., Silverman R.B., Petsko G.A.,
RA Ringe D.;
RT "Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-
RT amino-4,5-dihydro-2-thiophenecarboxylic acid reveals 'a tale of two
RT mechanisms'.";
RL Biochemistry 46:10517-10527(2007).
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:0000269|PubMed:10556573};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:11148029};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17713924}.
CC -!- INTERACTION:
CC P00509; P00509: aspC; NbExp=4; IntAct=EBI-907474, EBI-907474;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Transcription is increased specifically in response to
CC 2,4,6-trinitrotoluene (TNT) and its indicator compounds 1,3-DNB, 2,4-
CC DNT, and 2,6-DNT. {ECO:0000269|PubMed:25561288}.
CC -!- BIOTECHNOLOGY: Has been used to construct a 2,4,6-trinitrotoluene (TNT)
CC biosensor strain. {ECO:0000269|PubMed:25561288}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X03629; CAA27279.1; -; Genomic_DNA.
DR EMBL; X05904; CAA29333.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74014.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35674.1; -; Genomic_DNA.
DR PIR; A00598; XNECD.
DR RefSeq; NP_415448.1; NC_000913.3.
DR RefSeq; WP_000462687.1; NZ_STEB01000006.1.
DR PDB; 1AAM; X-ray; 2.80 A; A=1-396.
DR PDB; 1AAW; X-ray; 2.40 A; A=1-396.
DR PDB; 1AHE; X-ray; 2.30 A; A/B=1-396.
DR PDB; 1AHF; X-ray; 2.30 A; A/B=1-396.
DR PDB; 1AHG; X-ray; 2.50 A; A/B=1-396.
DR PDB; 1AHX; X-ray; 2.00 A; A/B=1-396.
DR PDB; 1AHY; X-ray; 2.30 A; A/B=1-396.
DR PDB; 1AIA; X-ray; 2.20 A; A/B=1-396.
DR PDB; 1AIB; X-ray; 2.80 A; A/B=1-396.
DR PDB; 1AIC; X-ray; 2.40 A; A/B=1-396.
DR PDB; 1AMQ; X-ray; 2.20 A; A=1-396.
DR PDB; 1AMR; X-ray; 2.10 A; A=1-396.
DR PDB; 1AMS; X-ray; 2.70 A; A=1-396.
DR PDB; 1ARG; X-ray; 2.20 A; A/B=1-396.
DR PDB; 1ARH; X-ray; 2.30 A; A/B=1-396.
DR PDB; 1ARI; X-ray; 2.30 A; A/B=1-396.
DR PDB; 1ARS; X-ray; 1.80 A; A=1-396.
DR PDB; 1ART; X-ray; 1.80 A; A=1-396.
DR PDB; 1ASA; X-ray; 2.40 A; A=1-396.
DR PDB; 1ASB; X-ray; 2.60 A; A=1-396.
DR PDB; 1ASC; X-ray; 2.40 A; A=1-396.
DR PDB; 1ASD; X-ray; 2.20 A; A=1-396.
DR PDB; 1ASE; X-ray; 2.50 A; A=1-396.
DR PDB; 1ASF; X-ray; 2.80 A; A=1-396.
DR PDB; 1ASG; X-ray; 2.80 A; A=1-396.
DR PDB; 1ASL; X-ray; 2.60 A; A/B=1-396.
DR PDB; 1ASM; X-ray; 2.35 A; A/B=1-396.
DR PDB; 1ASN; X-ray; 2.50 A; A/B=1-396.
DR PDB; 1B4X; X-ray; 2.45 A; A=1-396.
DR PDB; 1BQA; X-ray; 2.10 A; A/B=1-396.
DR PDB; 1BQD; X-ray; 2.10 A; A/B=1-396.
DR PDB; 1C9C; X-ray; 2.40 A; A=1-396.
DR PDB; 1CQ6; X-ray; 2.70 A; A=1-396.
DR PDB; 1CQ7; X-ray; 2.40 A; A=1-396.
DR PDB; 1CQ8; X-ray; 2.40 A; A=1-396.
DR PDB; 1CZC; X-ray; 2.50 A; A=1-396.
DR PDB; 1CZE; X-ray; 2.40 A; A=1-396.
DR PDB; 1G4V; X-ray; 2.00 A; A=1-396.
DR PDB; 1G4X; X-ray; 2.20 A; A=1-396.
DR PDB; 1G7W; X-ray; 2.20 A; A=1-396.
DR PDB; 1G7X; X-ray; 2.20 A; A=1-396.
DR PDB; 1IX6; X-ray; 2.20 A; A=1-396.
DR PDB; 1IX7; X-ray; 2.20 A; A=1-396.
DR PDB; 1IX8; X-ray; 2.20 A; A=1-396.
DR PDB; 1QIR; X-ray; 2.20 A; A=1-396.
DR PDB; 1QIS; X-ray; 1.90 A; A=1-396.
DR PDB; 1QIT; X-ray; 1.90 A; A=1-396.
DR PDB; 1SPA; X-ray; 2.00 A; A=1-396.
DR PDB; 1TOE; X-ray; 2.00 A; A=1-396.
DR PDB; 1TOG; X-ray; 2.31 A; A/B=1-396.
DR PDB; 1TOI; X-ray; 1.90 A; A=1-396.
DR PDB; 1TOJ; X-ray; 1.90 A; A=1-396.
DR PDB; 1TOK; X-ray; 1.85 A; A/B=1-396.
DR PDB; 1X28; X-ray; 2.40 A; A/B=1-396.
DR PDB; 1X29; X-ray; 2.20 A; A/B=1-396.
DR PDB; 1X2A; X-ray; 2.20 A; A/B=1-396.
DR PDB; 1YOO; X-ray; 2.40 A; A=1-396.
DR PDB; 2AAT; X-ray; 2.80 A; A=1-396.
DR PDB; 2D5Y; X-ray; 1.98 A; A=1-396.
DR PDB; 2D61; X-ray; 2.01 A; A=1-396.
DR PDB; 2D63; X-ray; 2.05 A; A=1-396.
DR PDB; 2D64; X-ray; 2.05 A; A=1-396.
DR PDB; 2D65; X-ray; 2.30 A; A=1-396.
DR PDB; 2D66; X-ray; 2.18 A; A=1-396.
DR PDB; 2D7Y; X-ray; 2.66 A; A=1-396.
DR PDB; 2D7Z; X-ray; 2.65 A; A=1-396.
DR PDB; 2Q7W; X-ray; 1.40 A; A=1-396.
DR PDB; 2QA3; X-ray; 1.75 A; A=1-396.
DR PDB; 2QB2; X-ray; 1.70 A; A=1-396.
DR PDB; 2QB3; X-ray; 1.45 A; A=1-396.
DR PDB; 2QBT; X-ray; 1.75 A; A=1-396.
DR PDB; 3AAT; X-ray; 2.80 A; A=1-396.
DR PDB; 3QN6; X-ray; 1.79 A; A=1-396.
DR PDB; 3QPG; X-ray; 1.79 A; A=1-396.
DR PDB; 3ZZJ; X-ray; 2.50 A; A=1-396.
DR PDB; 3ZZK; X-ray; 1.78 A; A=1-396.
DR PDB; 4A00; X-ray; 2.34 A; A=1-396.
DR PDB; 4DBC; X-ray; 1.50 A; A=1-396.
DR PDB; 4F5F; X-ray; 2.25 A; A/B=2-396.
DR PDB; 4F5G; X-ray; 1.67 A; A/B=2-396.
DR PDB; 4F5H; X-ray; 1.60 A; A/B=2-396.
DR PDB; 4F5I; X-ray; 2.20 A; A/B=2-396.
DR PDB; 4F5J; X-ray; 1.95 A; A/B=2-396.
DR PDB; 4F5K; X-ray; 2.20 A; A/B=2-396.
DR PDB; 4F5L; X-ray; 1.40 A; A/B=2-396.
DR PDB; 4F5M; X-ray; 1.65 A; A/B=2-396.
DR PDB; 5EAA; X-ray; 2.40 A; A=1-396.
DR PDB; 5T4L; X-ray; 1.53 A; A=1-396.
DR PDB; 5VWQ; X-ray; 1.80 A; A/D/G/J=1-396.
DR PDB; 5VWR; X-ray; 1.72 A; A=1-396.
DR PDBsum; 1AAM; -.
DR PDBsum; 1AAW; -.
DR PDBsum; 1AHE; -.
DR PDBsum; 1AHF; -.
DR PDBsum; 1AHG; -.
DR PDBsum; 1AHX; -.
DR PDBsum; 1AHY; -.
DR PDBsum; 1AIA; -.
DR PDBsum; 1AIB; -.
DR PDBsum; 1AIC; -.
DR PDBsum; 1AMQ; -.
DR PDBsum; 1AMR; -.
DR PDBsum; 1AMS; -.
DR PDBsum; 1ARG; -.
DR PDBsum; 1ARH; -.
DR PDBsum; 1ARI; -.
DR PDBsum; 1ARS; -.
DR PDBsum; 1ART; -.
DR PDBsum; 1ASA; -.
DR PDBsum; 1ASB; -.
DR PDBsum; 1ASC; -.
DR PDBsum; 1ASD; -.
DR PDBsum; 1ASE; -.
DR PDBsum; 1ASF; -.
DR PDBsum; 1ASG; -.
DR PDBsum; 1ASL; -.
DR PDBsum; 1ASM; -.
DR PDBsum; 1ASN; -.
DR PDBsum; 1B4X; -.
DR PDBsum; 1BQA; -.
DR PDBsum; 1BQD; -.
DR PDBsum; 1C9C; -.
DR PDBsum; 1CQ6; -.
DR PDBsum; 1CQ7; -.
DR PDBsum; 1CQ8; -.
DR PDBsum; 1CZC; -.
DR PDBsum; 1CZE; -.
DR PDBsum; 1G4V; -.
DR PDBsum; 1G4X; -.
DR PDBsum; 1G7W; -.
DR PDBsum; 1G7X; -.
DR PDBsum; 1IX6; -.
DR PDBsum; 1IX7; -.
DR PDBsum; 1IX8; -.
DR PDBsum; 1QIR; -.
DR PDBsum; 1QIS; -.
DR PDBsum; 1QIT; -.
DR PDBsum; 1SPA; -.
DR PDBsum; 1TOE; -.
DR PDBsum; 1TOG; -.
DR PDBsum; 1TOI; -.
DR PDBsum; 1TOJ; -.
DR PDBsum; 1TOK; -.
DR PDBsum; 1X28; -.
DR PDBsum; 1X29; -.
DR PDBsum; 1X2A; -.
DR PDBsum; 1YOO; -.
DR PDBsum; 2AAT; -.
DR PDBsum; 2D5Y; -.
DR PDBsum; 2D61; -.
DR PDBsum; 2D63; -.
DR PDBsum; 2D64; -.
DR PDBsum; 2D65; -.
DR PDBsum; 2D66; -.
DR PDBsum; 2D7Y; -.
DR PDBsum; 2D7Z; -.
DR PDBsum; 2Q7W; -.
DR PDBsum; 2QA3; -.
DR PDBsum; 2QB2; -.
DR PDBsum; 2QB3; -.
DR PDBsum; 2QBT; -.
DR PDBsum; 3AAT; -.
DR PDBsum; 3QN6; -.
DR PDBsum; 3QPG; -.
DR PDBsum; 3ZZJ; -.
DR PDBsum; 3ZZK; -.
DR PDBsum; 4A00; -.
DR PDBsum; 4DBC; -.
DR PDBsum; 4F5F; -.
DR PDBsum; 4F5G; -.
DR PDBsum; 4F5H; -.
DR PDBsum; 4F5I; -.
DR PDBsum; 4F5J; -.
DR PDBsum; 4F5K; -.
DR PDBsum; 4F5L; -.
DR PDBsum; 4F5M; -.
DR PDBsum; 5EAA; -.
DR PDBsum; 5T4L; -.
DR PDBsum; 5VWQ; -.
DR PDBsum; 5VWR; -.
DR AlphaFoldDB; P00509; -.
DR SMR; P00509; -.
DR BioGRID; 4260021; 28.
DR BioGRID; 849927; 1.
DR DIP; DIP-9181N; -.
DR IntAct; P00509; 4.
DR STRING; 511145.b0928; -.
DR DrugBank; DB02024; 3-phenylpropionic acid.
DR DrugBank; DB03553; Glutaric Acid.
DR DrugBank; DB02758; Indolepropionic acid.
DR DrugBank; DB03750; Isovaleric Acid.
DR DrugBank; DB04299; Maleic acid.
DR DrugBank; DB04083; N(6)-(pyridoxal phosphate)-L-lysine.
DR DrugBank; DB04467; N-(5'-phosphopyridoxyl)-L-alanine.
DR DrugBank; DB01639; N-Methyl-Pyridoxal-5'-Phosphate.
DR DrugBank; DB04765; N-PYRIDOXYL-2-METHYL-L-GLUTAMIC ACID-5'-MONOPHOSPHATE.
DR DrugBank; DB04762; N-PYRIDOXYL-D-GLUTAMIC ACID-5'-MONOPHOSPHATE.
DR DrugBank; DB08845; Oxogluric acid.
DR DrugBank; DB03629; Pyridoxal-5'-Phosphate-N-Oxide.
DR DrugBank; DB02981; Vitamin B6 Complexed with 2-Amino-Hexanoic Acid.
DR DrugBank; DB03662; Vitamin B6 Complexed with 2-Amino-Pentanoic Acid.
DR SWISS-2DPAGE; P00509; -.
DR jPOST; P00509; -.
DR PaxDb; P00509; -.
DR PRIDE; P00509; -.
DR EnsemblBacteria; AAC74014; AAC74014; b0928.
DR EnsemblBacteria; BAA35674; BAA35674; BAA35674.
DR GeneID; 66670796; -.
DR GeneID; 945553; -.
DR KEGG; ecj:JW0911; -.
DR KEGG; eco:b0928; -.
DR PATRIC; fig|1411691.4.peg.1348; -.
DR EchoBASE; EB0094; -.
DR eggNOG; COG1448; Bacteria.
DR HOGENOM; CLU_032440_1_2_6; -.
DR InParanoid; P00509; -.
DR OMA; VGACTIV; -.
DR PhylomeDB; P00509; -.
DR BioCyc; EcoCyc:ASPAMINOTRANS-MON; -.
DR BioCyc; MetaCyc:ASPAMINOTRANS-MON; -.
DR BRENDA; 2.6.1.1; 2026.
DR SABIO-RK; P00509; -.
DR EvolutionaryTrace; P00509; -.
DR PRO; PR:P00509; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IMP:EcoliWiki.
DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate aminotransferase activity; IMP:EcoliWiki.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IGI:EcoliWiki.
DR GO; GO:0033585; P:L-phenylalanine biosynthetic process from chorismate via phenylpyruvate; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Aminotransferase; Cytoplasm; Direct protein sequencing;
KW Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..396
FT /note="Aspartate aminotransferase"
FT /id="PRO_0000123838"
FT BINDING 34
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0007744|PDB:1ART, ECO:0007744|PDB:1CZE,
FT ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC"
FT BINDING 130
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART,
FT ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1SPA,
FT ECO:0007744|PDB:3QPG, ECO:0007744|PDB:4DBC"
FT BINDING 183
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0007744|PDB:1AIB, ECO:0007744|PDB:1ART,
FT ECO:0007744|PDB:1ASC, ECO:0007744|PDB:1CZE,
FT ECO:0007744|PDB:1SPA, ECO:0007744|PDB:3QPG,
FT ECO:0007744|PDB:4DBC"
FT BINDING 374
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0007744|PDB:1AHG, ECO:0007744|PDB:1AIB,
FT ECO:0007744|PDB:1ARG, ECO:0007744|PDB:1ART,
FT ECO:0007744|PDB:1CZE, ECO:0007744|PDB:3QPG,
FT ECO:0007744|PDB:4DBC"
FT MOD_RES 246
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000269|PubMed:11148029,
FT ECO:0000269|PubMed:1993208, ECO:0000269|PubMed:3298240,
FT ECO:0000269|PubMed:9891001, ECO:0007744|PDB:1AAW,
FT ECO:0007744|PDB:1AHE, ECO:0007744|PDB:1AHF,
FT ECO:0007744|PDB:1AHX, ECO:0007744|PDB:1AHY,
FT ECO:0007744|PDB:1ARI, ECO:0007744|PDB:1ARS,
FT ECO:0007744|PDB:1ASA, ECO:0007744|PDB:1ASB,
FT ECO:0007744|PDB:1ASD, ECO:0007744|PDB:1ASE,
FT ECO:0007744|PDB:1ASF, ECO:0007744|PDB:1ASG,
FT ECO:0007744|PDB:1ASM, ECO:0007744|PDB:1ASN,
FT ECO:0007744|PDB:1B4X, ECO:0007744|PDB:1CZC,
FT ECO:0007744|PDB:1CZE, ECO:0007744|PDB:1G4V,
FT ECO:0007744|PDB:1G4X, ECO:0007744|PDB:1G7W,
FT ECO:0007744|PDB:1G7X, ECO:0007744|PDB:1IX6,
FT ECO:0007744|PDB:1IX7, ECO:0007744|PDB:1IX8,
FT ECO:0007744|PDB:1QIR, ECO:0007744|PDB:1QIS,
FT ECO:0007744|PDB:1QIT, ECO:0007744|PDB:1YOO,
FT ECO:0007744|PDB:2D5Y, ECO:0007744|PDB:2D61,
FT ECO:0007744|PDB:2D63, ECO:0007744|PDB:2D7Y,
FT ECO:0007744|PDB:3AAT, ECO:0007744|PDB:3ZZJ,
FT ECO:0007744|PDB:5EAA"
FT MUTAGEN 65
FT /note="Y->F,S: Slight changes in activity."
FT /evidence="ECO:0000269|PubMed:1868057"
FT MUTAGEN 133
FT /note="H->A: Slight increase in maximum velocity of the
FT overall transamination reaction between aspartate and 2-
FT oxoglutarate."
FT /evidence="ECO:0000269|PubMed:2007566"
FT MUTAGEN 133
FT /note="H->N: Decreases to 60% in maximum rate of the
FT overall reactions in both directions."
FT /evidence="ECO:0000269|PubMed:2007566"
FT MUTAGEN 280
FT /note="R->V: Reduces first-order rate constant over 25000-
FT fold."
FT /evidence="ECO:0000269|PubMed:10556573"
FT MUTAGEN 374
FT /note="R->A: Reduces first-order rate constant about 10000-
FT fold."
FT /evidence="ECO:0000269|PubMed:10556573,
FT ECO:0000269|PubMed:1993208"
FT MUTAGEN 374
FT /note="R->F,Y: Second-order rate constants are reduced by
FT >5 orders of magnitude."
FT /evidence="ECO:0000269|PubMed:10556573,
FT ECO:0000269|PubMed:1993208"
FT TURN 2..4
FT /evidence="ECO:0007829|PDB:4F5H"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:4F5L"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:4A00"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1ASE"
FT HELIX 47..59
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 72..83
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 88..91
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 95..101
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 122..128
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 132..139
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:2Q7W"
FT TURN 152..155
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2AAT"
FT TURN 183..185
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 207..213
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 217..219
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 226..234
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:2Q7W"
FT TURN 245..249
FT /evidence="ECO:0007829|PDB:4DBC"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 256..261
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 265..280
FT /evidence="ECO:0007829|PDB:2Q7W"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 288..298
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 301..331
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 340..343
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 346..350
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 355..365
FT /evidence="ECO:0007829|PDB:2Q7W"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1TOG"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:1ART"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 377..379
FT /evidence="ECO:0007829|PDB:2Q7W"
FT TURN 382..384
FT /evidence="ECO:0007829|PDB:2Q7W"
FT HELIX 385..395
FT /evidence="ECO:0007829|PDB:2Q7W"
SQ SEQUENCE 396 AA; 43573 MW; 9F0437E76DD4FC0F CRC64;
MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE
TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT PGGTGALRVA ADFLAKNTSV
KRVWVSNPSW PNHKSVFNSA GLEVREYAYY DAENHTLDFD ALINSLNEAQ AGDVVLFHGC
CHNPTGIDPT LEQWQTLAQL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV
ASSYSKNFGL YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN
DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKEQVLR
LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL
