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 04-NOV-2026, entry version 223. 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; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; 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 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, 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 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 OF MUTANTS ALA-183/PHE-214; ALA-183/LEU-280; RP ALA-183/LEU-374 AND ALA-183/LEU-280/LEU-374 IN COMPLEXES WITH PYRIDOXAL RP 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 IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND SADTA, AND RP 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=L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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_CP009789.1. 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 PDB; 8E9C; X-ray; 2.18 A; A/B=2-396. DR PDB; 8E9D; X-ray; 1.37 A; A/B=2-396. DR PDB; 8E9J; X-ray; 2.09 A; A/B=2-396. DR PDB; 8E9K; X-ray; 1.83 A; A/B=2-396. DR PDB; 8E9L; X-ray; 2.31 A; A/B=2-396. DR PDB; 8E9M; X-ray; 1.76 A; A/B=2-396. DR PDB; 8E9N; X-ray; 1.88 A; A/B=2-396. DR PDB; 8E9O; X-ray; 1.96 A; A/B=2-396. DR PDB; 8E9P; X-ray; 2.08 A; A/B=2-396. DR PDB; 8E9Q; X-ray; 1.80 A; A/B=2-396. DR PDB; 8E9R; X-ray; 1.90 A; A/B=2-396. DR PDB; 8E9S; X-ray; 2.00 A; A/B=2-396. DR PDB; 8E9T; X-ray; 2.13 A; A/B=2-396. DR PDB; 8E9U; X-ray; 1.94 A; A/B=2-396. DR PDB; 8E9V; X-ray; 2.01 A; A/B=2-396. DR AlphaFoldDB; P00509; -. DR MDposit; P00509; -. DR MDRepo; P00509; -. DR SMR; P00509; -. DR BioGRID; 4260021; 32. DR BioGRID; 849927; 1. DR DIP; DIP-9181N; -. DR FunCoup; P00509; 652. 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 jPOST; P00509; -. DR PaxDb; 511145-b0928; -. DR EnsemblBacteria; AAC74014; AAC74014; b0928. DR GeneID; 93776486; -. DR GeneID; 945553; -. DR KEGG; ecj:JW0911; -. DR KEGG; eco:b0928; -. DR KEGG; ecoc:C3026_05700; -. 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; AACVSTW; -. DR OrthoDB; 9766445at2; -. DR PhylomeDB; P00509; -. DR BioCyc; EcoCyc:ASPAMINOTRANS-MONOMER; -. DR BioCyc; MetaCyc:ASPAMINOTRANS-MONOMER; -. DR BRENDA; 2.6.1.1; 2026. DR SABIO-RK; P00509; -. DR EvolutionaryTrace; P00509; -. DR PRO; PR:P00509; -. DR Proteomes; UP000000625; Chromosome. DR AbasyAtlas; P00509; -. 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 transaminase activity; IMP:EcoliWiki. DR GO; GO:0004838; F:L-tyrosine:2-oxoglutarate transaminase activity; IMP:EcoliWiki. DR GO; GO:0042803; F:protein homodimerization activity; IDA:EcoCyc. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IGI:EcoliWiki. DR CDD; cd00609; AAT_like; 1. DR FunFam; 3.40.640.10:FF:000015; Aspartate aminotransferase; 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_large. DR InterPro; IPR000796; Asp_trans. DR InterPro; IPR004838; NHTrfase_class1_PLP_cs. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small. DR NCBIfam; NF006719; PRK09257.1; 1. 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. 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 FT 2-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 FT 25000-fold." FT /evidence="ECO:0000269|PubMed:10556573" FT MUTAGEN 374 FT /note="R->A: Reduces first-order rate constant about FT 10000-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:8E9D" FT HELIX 5..11 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 12..15 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 16..22 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 29..31 FT /evidence="ECO:0007829|PDB:1TOG" FT TURN 39..41 FT /evidence="ECO:0007829|PDB:1ASE" FT HELIX 47..59 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 64..67 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 72..83 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 88..91 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 95..101 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 102..117 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 122..128 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 132..139 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 143..148 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 152..155 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 159..165 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 166..168 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 174..181 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 183..185 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 187..190 FT /evidence="ECO:0007829|PDB:1AAW" FT HELIX 191..204 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 207..213 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 217..219 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 221..224 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 226..234 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 238..243 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 245..247 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 251..253 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 256..261 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 265..280 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 281..283 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 288..298 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 301..331 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 339..343 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 346..350 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 355..365 FT /evidence="ECO:0007829|PDB:8E9D" FT STRAND 367..369 FT /evidence="ECO:0007829|PDB:1TOG" FT STRAND 373..376 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 377..379 FT /evidence="ECO:0007829|PDB:8E9D" FT TURN 382..384 FT /evidence="ECO:0007829|PDB:8E9D" FT HELIX 385..395 FT /evidence="ECO:0007829|PDB:8E9D" 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 //