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UniProtKB/Swiss-Prot entry P00509


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AAT_ECOLI
Primary accession number P00509
Secondary accession numbers None
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 99)
Name and origin of the protein
Protein name Aspartate aminotransferase
Synonyms ASPAT
EC 2.6.1.1
Transaminase A
Gene name
Name: aspC
OrderedLocusNames: b0928, JW0911
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
PROTEIN SEQUENCE.
DOI=10.1016/0006-291X(84)90439-X; PubMed=6378205 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo K., Wakabayashi S., Yagi T., Kagamiyama H.;
"The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes.";
Biochem. Biophys. Res. Commun. 122:62-67(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3897210 [NCBI, ExPASy, EBI, Israel, Japan]
Kuramitsu S., Okuno S., Ogawa T., Ogawa H., Kagamiyama H.;
"Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene.";
J. Biochem. 97:1259-1262(1985).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3521591 [NCBI, ExPASy, EBI, Israel, Japan]
Fotheringham I.G., Dacey S.A., Taylor P.P., Smith T.J., Hunter M.G., Finlay M.E., Primrose S.B., Parker D.M., Edwards R.M.;
"The cloning and sequence analysis of the aspC and tyrB genes from Escherichia coli K12. Comparison of the primary structures of the aspartate aminotransferase and aromatic aminotransferase of E. coli with those of the pig aspartate aminotransferase isoenzymes.";
Biochem. J. 234:593-604(1986).
[4]
PROTEIN SEQUENCE.
PubMed=3298240 [NCBI, ExPASy, EBI, Israel, Japan]
Kondo K., Wakabayashi S., Kagamiyama H.;
"Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure.";
J. Biol. Chem. 262:8648-8657(1987).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1093/dnares/3.3.137; PubMed=8905232 [NCBI, ExPASy, EBI, Israel, Japan]
Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T.;
"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map.";
DNA Res. 3:137-155(1996).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[8]
PROTEIN SEQUENCE OF 1-12.
STRAIN=K12 / EMG2;
PubMed=9298646 [NCBI, ExPASy, EBI, Israel, Japan]
Link A.J., Robison K., Church G.M.;
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12.";
Electrophoresis 18:1259-1313(1997).
[9]
MUTAGENESIS OF TYR-65.
DOI=10.1021/bi00245a019; PubMed=1868057 [NCBI, ExPASy, EBI, Israel, Japan]
Inoue K., Kuramitsu S., Okamoto A., Hirotsu K., Higuchi T., Kagamiyama H.;
"Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.";
Biochemistry 30:7796-7801(1991).
[10]
MUTAGENESIS OF HIS-133.
PubMed=2007566 [NCBI, ExPASy, EBI, Israel, Japan]
Yano T., Kuramitsu S., Tanase S., Morino Y., Hiromi K., Kagamiyama H.;
"The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.";
J. Biol. Chem. 266:6079-6085(1991).
[11]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
DOI=10.1021/bi00446a030; PubMed=2513875 [NCBI, ExPASy, EBI, Israel, Japan]
Smith D.L., Almo S.C., Toney M.D., Ringe D.;
"2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.";
Biochemistry 28:8161-8167(1989).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND MUTAGENESIS OF ARG-374.
DOI=10.1021/bi00221a035; PubMed=1993208 [NCBI, ExPASy, EBI, Israel, Japan]
Danishefsky A.T., Onnufer J.J., Petsko G.A., Ringe D.;
"Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.";
Biochemistry 30:1980-1985(1991).
[13]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
DOI=10.1074/jbc.274.4.2344; PubMed=9891001 [NCBI, ExPASy, EBI, Israel, Japan]
Oue S., Okamoto A., Yano T., Kagamiyama H.;
"Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.";
J. Biol. Chem. 274:2344-2349(1999).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X03629; CAA27279.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X05904; CAA29333.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC74014.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAA35674.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A00598; XNECD.
RefSeq AP_001558.1; -.
NP_415448.1; -.
3D structure databases
PDB
1AAM; X-ray; 2.80 A; A=1-396.[ExPASy / RCSB / EBI]
1AAW; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1AHE; X-ray; 2.30 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AHF; X-ray; 2.30 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AHG; X-ray; 2.50 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AHX; X-ray; 2.00 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AHY; X-ray; 2.30 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AIA; X-ray; 2.20 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AIB; X-ray; 2.80 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AIC; X-ray; 2.40 A; A/B=1-396.[ExPASy / RCSB / EBI]
1AMQ; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1AMR; X-ray; 2.10 A; A=1-396.[ExPASy / RCSB / EBI]
1AMS; X-ray; 2.70 A; A=1-396.[ExPASy / RCSB / EBI]
1ARG; X-ray; 2.20 A; A/B=1-396.[ExPASy / RCSB / EBI]
1ARH; X-ray; 2.30 A; A/B=1-396.[ExPASy / RCSB / EBI]
1ARI; X-ray; 2.30 A; A/B=1-396.[ExPASy / RCSB / EBI]
1ARS; X-ray; 1.80 A; A=1-396.[ExPASy / RCSB / EBI]
1ART; X-ray; 1.80 A; A=1-396.[ExPASy / RCSB / EBI]
1ASA; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1ASB; X-ray; 2.60 A; A=1-396.[ExPASy / RCSB / EBI]
1ASC; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1ASD; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1ASE; X-ray; 2.50 A; A=1-396.[ExPASy / RCSB / EBI]
1ASF; X-ray; 2.80 A; A=1-396.[ExPASy / RCSB / EBI]
1ASG; X-ray; 2.80 A; A=1-396.[ExPASy / RCSB / EBI]
1ASL; X-ray; 2.60 A; A/B=1-396.[ExPASy / RCSB / EBI]
1ASM; X-ray; 2.35 A; A/B=1-396.[ExPASy / RCSB / EBI]
1ASN; X-ray; 2.50 A; A/B=1-396.[ExPASy / RCSB / EBI]
1B4X; X-ray; 2.45 A; A=1-396.[ExPASy / RCSB / EBI]
1BQA; X-ray; 2.10 A; A/B=1-396.[ExPASy / RCSB / EBI]
1BQD; X-ray; 2.10 A; A/B=1-396.[ExPASy / RCSB / EBI]
1C9C; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1CQ6; X-ray; 2.70 A; A=1-396.[ExPASy / RCSB / EBI]
1CQ7; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1CQ8; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1CZC; X-ray; 2.50 A; A=1-396.[ExPASy / RCSB / EBI]
1CZE; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
1G4V; X-ray; 2.00 A; A=1-396.[ExPASy / RCSB / EBI]
1G4X; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1G7W; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1G7X; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1IX6; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1IX7; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1IX8; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1QIR; X-ray; 2.20 A; A=1-396.[ExPASy / RCSB / EBI]
1QIS; X-ray; 1.90 A; A=1-396.[ExPASy / RCSB / EBI]
1QIT; X-ray; 1.90 A; A=1-396.[ExPASy / RCSB / EBI]
1SPA; X-ray; 2.00 A; A=1-396.[ExPASy / RCSB / EBI]
1TOE; X-ray; 2.00 A; A=1-396.[ExPASy / RCSB / EBI]
1TOG; X-ray; 2.31 A; A/B=1-396.[ExPASy / RCSB / EBI]
1TOI; X-ray; 1.90 A; A=1-396.[ExPASy / RCSB / EBI]
1TOJ; X-ray; 1.90 A; A=1-396.[ExPASy / RCSB / EBI]
1TOK; X-ray; 1.85 A; A/B=1-396.[ExPASy / RCSB / EBI]
1X28; X-ray; 2.40 A; A/B=1-396.[ExPASy / RCSB / EBI]
1X29; X-ray; 2.20 A; A/B=1-396.[ExPASy / RCSB / EBI]
1X2A; X-ray; 2.20 A; A/B=1-396.[ExPASy / RCSB / EBI]
1YOO; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
2AAT; X-ray; 2.80 A; A=1-396.[ExPASy / RCSB / EBI]
2D5Y; X-ray; 1.98 A; A=1-396.[ExPASy / RCSB / EBI]
2D61; X-ray; 2.01 A; A=1-396.[ExPASy / RCSB / EBI]
2D63; X-ray; 2.05 A; A=1-396.[ExPASy / RCSB / EBI]
2D64; X-ray; 2.05 A; A=-.[ExPASy / RCSB / EBI]
2D65; X-ray; 2.30 A; A=-.[ExPASy / RCSB / EBI]
2D66; X-ray; 2.18 A; A=-.[ExPASy / RCSB / EBI]
2D7Y; X-ray; 2.66 A; A=1-396.[ExPASy / RCSB / EBI]
2D7Z; X-ray; 2.65 A; A=-.[ExPASy / RCSB / EBI]
2Q7W; X-ray; 1.40 A; A=1-396.[ExPASy / RCSB / EBI]
2QA3; X-ray; 1.75 A; A=1-396.[ExPASy / RCSB / EBI]
2QB2; X-ray; 1.70 A; A=1-396.[ExPASy / RCSB / EBI]
2QB3; X-ray; 1.45 A; A=1-396.[ExPASy / RCSB / EBI]
2QBT; X-ray; 1.75 A; A=1-396.[ExPASy / RCSB / EBI]
3AAT; X-ray; 2.80 A; A=1-396.[ExPASy / RCSB / EBI]
5EAA; X-ray; 2.40 A; A=1-396.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1AAM; -.
1AAW; -.
1AHE; -.
1AHF; -.
1AHG; -.
1AHX; -.
1AHY; -.
1AIA; -.
1AIB; -.
1AIC; -.
1AMQ; -.
1AMR; -.
1AMS; -.
1ARG; -.
1ARH; -.
1ARI; -.
1ARS; -.
1ART; -.
1ASA; -.
1ASB; -.
1ASC; -.
1ASD; -.
1ASE; -.
1ASF; -.
1ASG; -.
1ASL; -.
1ASM; -.
1ASN; -.
1B4X; -.
1BQA; -.
1BQD; -.
1C9C; -.
1CQ6; -.
1CQ7; -.
1CQ8; -.
1CZC; -.
1CZE; -.
1G4V; -.
1G4X; -.
1G7W; -.
1G7X; -.
1IX6; -.
1IX7; -.
1IX8; -.
1QIR; -.
1QIS; -.
1QIT; -.
1SPA; -.
1TOE; -.
1TOG; -.
1TOI; -.
1TOJ; -.
1TOK; -.
1X28; -.
1X29; -.
1X2A; -.
1YOO; -.
2AAT; -.
2D5Y; -.
2D61; -.
2D63; -.
2D64; -.
2D65; -.
2D66; -.
2D7Y; -.
2D7Z; -.
2Q7W; -.
2QA3; -.
2QB2; -.
2QB3; -.
2QBT; -.
3AAT; -.
5EAA; -.
ModBase P00509.
Protein-protein interaction databases
IntAct P00509; -.
Enzyme and pathway databases
BioCyc EcoCyc:ASPAMINOTRANS-MON; -.
2D gel databases
SWISS-2DPAGE P00509; -.
ECO2DBASE F039.6; 6TH EDITION.
F039.7; 6TH EDITION.
Organism-specific databases
EchoBASE EB0094; -.
EcoGene EG10096; aspC.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
InterPro IPR004839; Aminotrans_I/II.
IPR000796; Asp_trans.
IPR004838; NHTrfase_class1_PyrdxlP-BS.
IPR015421; PyrdxlP-dep_Trfase_major_sub1.
Graphical view of domain structure.
Gene3D G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
PANTHER PTHR11879; Asp_trans; 1.
Pfam PF00155; Aminotran_1_2; 1.
Pfam graphical view of domain structure.
PRINTS PR00799; TRANSAMINASE.
PROSITE PS00105; AA_TRANSFER_CLASS_1; 1.
BLOCKS P00509.
Other
SWISS-3DIMAGE P00509.
Genome annotation databases
GeneID 945553; -.
GenomeReviews U00096_GR; b0928.
AP009048_GR; JW0911.
KEGG ecj:JW0911; -.
eco:b0928; -.
Phylogenomic databases
HOGENOM P00509; -.
Other
LinkHub P00509; -.
Genome annotation databases
CMR P00509; b0928.
Other
ProtoNet P00509.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Aminotransferase; Complete proteome; Cytoplasm; Direct protein sequencing; Pyridoxal phosphate; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   396  396     Aspartate aminotransferase. PRO_0000123838
BINDING   246   246        Pyridoxal phosphate (covalent). 
BINDING   374   374        Substrate. 
MUTAGEN   65    65        Y->F,S: Slight changes in activity. 
MUTAGEN   133   133        H->A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. 
MUTAGEN   133   133        H->N: Decreases to 60% in maximum rate of the overall reactions in both directions. 
MUTAGEN   374   374        R->F,Y: Second-order rate constants are reduced by >5 orders of magnitude. 
TURN   12    15  4      
HELIX   16    19  4      
TURN   20    22  3      
STRAND   29    32  4      
HELIX   47    59  13      
HELIX   72    83  12      
HELIX   88    91  4      
STRAND   95   101  7      
HELIX   102   117  16      
STRAND   122   128  7      
HELIX   132   139  8      
STRAND   143   148  6      
TURN   152   155  4      
HELIX   159   166  8      
STRAND   174   178  5      
TURN   183   185  3      
HELIX   191   204  14      
STRAND   207   213  7      
STRAND   217   219  3      
HELIX   221   224  4      
HELIX   226   234  9      
STRAND   238   243  6      
HELIX   251   253  3      
STRAND   256   261  6      
HELIX   265   280  16      
TURN   281   283  3      
HELIX   288   298  11      
HELIX   301   331  31      
HELIX   340   343  4      
STRAND   346   350  5      
HELIX   355   365  11      
STRAND   374   376  3      
HELIX   377   379  3      
TURN   382   384  3      
HELIX   385   395  11      
Sequence information
Length: 396 AA [This is the length of the unprocessed precursor] Molecular weight: 43573 Da [This is the MW of the unprocessed precursor] CRC64: 9F0437E76DD4FC0F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MFENITAAPA DPILGLADLF RADERPGKIN LGIGVYKDET GKTPVLTSVK KAEQYLLENE 

        70         80         90        100        110        120 
TTKNYLGIDG IPEFGRCTQE LLFGKGSALI NDKRARTAQT PGGTGALRVA ADFLAKNTSV 

       130        140        150        160        170        180 
KRVWVSNPSW PNHKSVFNSA GLEVREYAYY DAENHTLDFD ALINSLNEAQ AGDVVLFHGC 

       190        200        210        220        230        240 
CHNPTGIDPT LEQWQTLAQL SVEKGWLPLF DFAYQGFARG LEEDAEGLRA FAAMHKELIV 

       250        260        270        280        290        300 
ASSYSKNFGL YNERVGACTL VAADSETVDR AFSQMKAAIR ANYSNPPAHG ASVVATILSN 

       310        320        330        340        350        360 
DALRAIWEQE LTDMRQRIQR MRQLFVNTLQ EKGANRDFSF IIKQNGMFSF SGLTKEQVLR 

       370        380        390 
LREEFGVYAV ASGRVNVAGM TPDNMAPLCE AIVAVL 

P00509 in FASTA format

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