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P00509 (AAT_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 154. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aspartate aminotransferase

Short name=AspAT
EC=2.6.1.1
Alternative name(s):
Transaminase A
Gene names
Name:aspC
Ordered Locus Names:b0928, JW0911
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length396 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Ref.12

Cofactor

Pyridoxal phosphate. Ref.16

Subunit structure

Homodimer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself4EBI-907474,EBI-907474

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 396396Aspartate aminotransferase
PRO_0000123838

Sites

Binding site341Aspartate; via amide nitrogen
Binding site1301Aspartate
Binding site1831Aspartate
Binding site3741Aspartate

Amino acid modifications

Modified residue2461N6-(pyridoxal phosphate)lysine Ref.4

Experimental info

Mutagenesis651Y → F or S: Slight changes in activity. Ref.9
Mutagenesis1331H → A: Slight increase in maximum velocity of the overall transamination reaction between aspartate and 2-oxoglutarate. Ref.10
Mutagenesis1331H → N: Decreases to 60% in maximum rate of the overall reactions in both directions. Ref.10
Mutagenesis2801R → V: Reduces first-order rate constant over 25000-fold. Ref.12
Mutagenesis3741R → A: Reduces first-order rate constant about 10000-fold. Ref.12 Ref.14
Mutagenesis3741R → F or Y: Second-order rate constants are reduced by >5 orders of magnitude. Ref.12 Ref.14

Secondary structure

.......................................................................... 396
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00509 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 9F0437E76DD4FC0F

FASTA39643,573
        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 

« Hide

References

« Hide 'large scale' references
[1]"The complete amino acid sequence of aspartate aminotransferase from Escherichia coli: sequence comparison with pig isoenzymes."
Kondo K., Wakabayashi S., Yagi T., Kagamiyama H.
Biochem. Biophys. Res. Commun. 122:62-67(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[2]"Aspartate aminotransferase of Escherichia coli: nucleotide sequence of the aspC gene."
Kuramitsu S., Okuno S., Ogawa T., Ogawa H., Kagamiyama H.
J. Biochem. 97:1259-1262(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"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."
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.
Biochem. J. 234:593-604(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Structural studies on aspartate aminotransferase from Escherichia coli. Covalent structure."
Kondo K., Wakabayashi S., Kagamiyama H.
J. Biol. Chem. 262:8648-8657(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
[5]"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."
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. expand/collapse author list , 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.
DNA Res. 3:137-155(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Link A.J., Robison K., Church G.M.
Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12.
Strain: K12 / EMG2.
[9]"Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes."
Inoue K., Kuramitsu S., Okamoto A., Hirotsu K., Higuchi T., Kagamiyama H.
Biochemistry 30:7796-7801(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-65.
[10]"The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase."
Yano T., Kuramitsu S., Tanase S., Morino Y., Hiromi K., Kagamiyama H.
J. Biol. Chem. 266:6079-6085(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF HIS-133.
[11]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[12]"The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction."
Mahon M.M., Graber R., Christen P., Malthouse J.P.
Biochim. Biophys. Acta 1434:191-201(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY, MUTAGENESIS OF ARG-280 AND ARG-374.
[13]"2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli."
Smith D.L., Almo S.C., Toney M.D., Ringe D.
Biochemistry 28:8161-8167(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246.
[14]"Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase."
Danishefsky A.T., Onnufer J.J., Petsko G.A., Ringe D.
Biochemistry 30:1980-1985(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), MUTAGENESIS OF ARG-374.
[15]"Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues."
Oue S., Okamoto A., Yano T., Kagamiyama H.
J. Biol. Chem. 274:2344-2349(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT.
[16]"Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase."
Mizuguchi H., Hayashi H., Okada K., Miyahara I., Hirotsu K., Kagamiyama H.
Biochemistry 40:353-360(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF MUTANTS ALA-183/PHE-214; ALA-183/LEU-280; ALA-183/LEU-374 AND ALA-183/LEU-280/LEU-374 IN COMPLEXES WITH PYRIDOXAL PHOSPHATE, COFACTOR, PYRIDOXAL PHOSPHATE AT LYS-246.
[17]"Inactivation of Escherichia coli L-aspartate aminotransferase by (S)-4-amino-4,5-dihydro-2-thiophenecarboxylic acid reveals 'a tale of two mechanisms'."
Liu D., Pozharski E., Lepore B.W., Fu M., Silverman R.B., Petsko G.A., Ringe D.
Biochemistry 46:10517-10527(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL PHOSPHATE AND SADTA, PYRIDOXAL PHOSPHATE AT LYS-246.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03629 Genomic DNA. Translation: CAA27279.1.
X05904 Genomic DNA. Translation: CAA29333.1.
U00096 Genomic DNA. Translation: AAC74014.1.
AP009048 Genomic DNA. Translation: BAA35674.1.
PIRXNECD. A00598.
RefSeqNP_415448.1. NC_000913.3.
YP_489200.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AAMX-ray2.80A1-396[»]
1AAWX-ray2.40A1-396[»]
1AHEX-ray2.30A/B1-396[»]
1AHFX-ray2.30A/B1-396[»]
1AHGX-ray2.50A/B1-396[»]
1AHXX-ray2.00A/B1-396[»]
1AHYX-ray2.30A/B1-396[»]
1AIAX-ray2.20A/B1-396[»]
1AIBX-ray2.80A/B1-396[»]
1AICX-ray2.40A/B1-396[»]
1AMQX-ray2.20A1-396[»]
1AMRX-ray2.10A1-396[»]
1AMSX-ray2.70A1-396[»]
1ARGX-ray2.20A/B1-396[»]
1ARHX-ray2.30A/B1-396[»]
1ARIX-ray2.30A/B1-396[»]
1ARSX-ray1.80A1-396[»]
1ARTX-ray1.80A1-396[»]
1ASAX-ray2.40A1-396[»]
1ASBX-ray2.60A1-396[»]
1ASCX-ray2.40A1-396[»]
1ASDX-ray2.20A1-396[»]
1ASEX-ray2.50A1-396[»]
1ASFX-ray2.80A1-396[»]
1ASGX-ray2.80A1-396[»]
1ASLX-ray2.60A/B1-396[»]
1ASMX-ray2.35A/B1-396[»]
1ASNX-ray2.50A/B1-396[»]
1B4XX-ray2.45A1-396[»]
1BQAX-ray2.10A/B1-396[»]
1BQDX-ray2.10A/B1-396[»]
1C9CX-ray2.40A1-396[»]
1CQ6X-ray2.70A1-396[»]
1CQ7X-ray2.40A1-396[»]
1CQ8X-ray2.40A1-396[»]
1CZCX-ray2.50A1-396[»]
1CZEX-ray2.40A1-396[»]
1G4VX-ray2.00A1-396[»]
1G4XX-ray2.20A1-396[»]
1G7WX-ray2.20A1-396[»]
1G7XX-ray2.20A1-396[»]
1IX6X-ray2.20A1-396[»]
1IX7X-ray2.20A1-396[»]
1IX8X-ray2.20A1-396[»]
1QIRX-ray2.20A1-396[»]
1QISX-ray1.90A1-396[»]
1QITX-ray1.90A1-396[»]
1SPAX-ray2.00A1-396[»]
1TOEX-ray2.00A1-388[»]
1TOGX-ray2.31A/B1-388[»]
1TOIX-ray1.90A1-388[»]
1TOJX-ray1.90A1-388[»]
1TOKX-ray1.85A/B1-388[»]
1X28X-ray2.40A/B1-396[»]
1X29X-ray2.20A/B1-396[»]
1X2AX-ray2.20A/B1-396[»]
1YOOX-ray2.40A1-396[»]
2AATX-ray2.80A1-396[»]
2D5YX-ray1.98A1-396[»]
2D61X-ray2.01A1-396[»]
2D63X-ray2.05A1-396[»]
2D64X-ray2.05A1-396[»]
2D65X-ray2.30A1-396[»]
2D66X-ray2.18A1-396[»]
2D7YX-ray2.66A1-396[»]
2D7ZX-ray2.65A1-396[»]
2Q7WX-ray1.40A1-396[»]
2QA3X-ray1.75A1-396[»]
2QB2X-ray1.70A1-396[»]
2QB3X-ray1.45A1-396[»]
2QBTX-ray1.75A1-396[»]
3AATX-ray2.80A1-396[»]
3QN6X-ray1.79A1-396[»]
3QPGX-ray1.79A1-396[»]
3ZZJX-ray2.50A1-396[»]
3ZZKX-ray1.78A1-396[»]
4A00X-ray2.34A1-396[»]
4DBCX-ray1.50A1-396[»]
4F5FX-ray2.25A/B2-396[»]
4F5GX-ray1.67A/B2-396[»]
4F5HX-ray1.60A/B2-396[»]
4F5IX-ray2.20A/B2-396[»]
4F5JX-ray1.95A/B2-396[»]
4F5KX-ray2.20A/B2-396[»]
4F5LX-ray1.40A/B2-396[»]
4F5MX-ray1.65A/B2-396[»]
5EAAX-ray2.40A1-396[»]
ProteinModelPortalP00509.
SMRP00509. Positions 1-396.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-9181N.
IntActP00509. 4 interactions.
STRING511145.b0928.

2D gel databases

SWISS-2DPAGEP00509.

Proteomic databases

PaxDbP00509.
PRIDEP00509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74014; AAC74014; b0928.
BAA35674; BAA35674; BAA35674.
GeneID12931027.
945553.
KEGGecj:Y75_p0900.
eco:b0928.
PATRIC32117069. VBIEscCol129921_0959.

Organism-specific databases

EchoBASEEB0094.
EcoGeneEG10096. aspC.

Phylogenomic databases

eggNOGCOG1448.
HOGENOMHOG000185899.
KOK00813.
OMARVGACTI.
OrthoDBEOG6C2WBK.
PhylomeDBP00509.

Enzyme and pathway databases

BioCycEcoCyc:ASPAMINOTRANS-MONOMER.
ECOL316407:JW0911-MONOMER.
MetaCyc:ASPAMINOTRANS-MONOMER.
BRENDA2.6.1.1. 2026.
SABIO-RKP00509.

Gene expression databases

GenevestigatorP00509.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
InterProIPR004839. Aminotransferase_I/II.
IPR000796. Asp_trans.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
[Graphical view]
PANTHERPTHR11879. PTHR11879. 1 hit.
PfamPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
PRINTSPR00799. TRANSAMINASE.
SUPFAMSSF53383. SSF53383. 1 hit.
PROSITEPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP00509.
PROP00509.

Entry information

Entry nameAAT_ECOLI
AccessionPrimary (citable) accession number: P00509
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 154 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene