Reviewed,
UniProtKB/Swiss-Prot P08660 (AK3_ECOLI)
Last modified
June 16, 2009.
Version 86.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysine-sensitive aspartokinase 3 EC=2.7.2.4 Alternative name(s): Lysine-sensitive aspartokinase III Aspartate kinase III | ||||||
| Gene names |
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| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 449 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | ATP + L-aspartate = ADP + 4-phospho-L-aspartate. |
| Enzyme regulation | Synthesis and activity are sensitive to lysine, which is one of the end metabolites of the aspartic acid family branched pathway. |
| Pathway | |
| Subunit structure | Homodimer. |
| Miscellaneous | Aspartokinases I and II also catalyze the same reaction(s). |
| Sequence similarities | Belongs to the aspartokinase family. Contains 1 ACT domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Lysine biosynthesis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | lysine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid bindingInferred from electronic annotation. Source: InterPro aspartate kinase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||||||||||||||||||||||||||||||||||
Molecule processing | |||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 449 | 449 | Lysine-sensitive aspartokinase 3 | PRO_0000066676 | |||||||||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||||||||
| Domain | 309 – 386 | 78 | ACT | ||||||||||||||||||||||||||||||||||||||||
| Region | 1 – 245 | 245 | Aspartokinase | ||||||||||||||||||||||||||||||||||||||||
| Region | 246 – 449 | 204 | Interface | ||||||||||||||||||||||||||||||||||||||||
Experimental info | |||||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 58 | 1 | G → C in AAA24095. Ref.1 | ||||||||||||||||||||||||||||||||||||||||
| Sequence conflict | 401 | 1 | G → A in AAA24095. Ref.1 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||||||||
| Helix | 68 – 82 | 15 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 87 – 90 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 93 – 103 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 119 | 11 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 122 – 133 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Turn | 150 – 152 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 161 – 168 | 8 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 176 – 179 | 4 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 181 – 186 | 6 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 190 – 192 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 196 – 198 | 3 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 201 – 212 | 12 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 216 – 220 | 5 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 222 – 231 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 236 – 245 | 10 | |||||||||||||||||||||||||||||||||||||||||
| Helix | 250 – 264 | 15 | |||||||||||||||||||||||||||||||||||||||||
| Beta strand | 269 – 277 | 9 | |||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of lysC gene encoding the lysine-sensitive aspartokinase III of Escherichia coli K12. Evolutionary pathway leading to three isofunctional enzymes." Cassan M., Parsot C., Cohen G.N., Patte J.-C. J. Biol. Chem. 261:1052-1057(1986) [PubMed: 3003049] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "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 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [5] | "Nucleotide sequence of the promoter region of the E. coli lysC gene." Cassan M., Ronceray J., Patte J.-C. Nucleic Acids Res. 11:6157-6166(1983) [PubMed: 6312411] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-20. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| M11812 Genomic DNA. Translation: AAA24095.1. U00006 Genomic DNA. Translation: AAC43118.1. U00096 Genomic DNA. Translation: AAC76994.1. AP009048 Genomic DNA. Translation: BAE78026.1. X00008 Genomic DNA. Translation: CAA24910.1. Sequence problems. | |||||||||||||||||||
| PIR | KIECD3. G65209. | ||||||||||||||||||
| RefSeq | AP_004525.1. NP_418448.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 948531. | ||||||||||||||||||
| GenomeReviews | Gene locus JW3984 in contig AP009048_GR. Gene locus b4024 in contig U00096_GR. | ||||||||||||||||||
| KEGG | ecj:JW3984. eco:b4024. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| EchoBASE | EB0545. | ||||||||||||||||||
| EcoGene | EG10550. lysC. | ||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | P08660. | ||||||||||||||||||
| OMA | P08660. GFIGADE. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | EcoCyc:ASPKINIII-MON. MetaCyc:ASPKINIII-MON. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR005260. Asp_kin_monofn. IPR001341. Asp_kin_reg. IPR018042. Aspartate_kinase_CS. [Graphical view] | ||||||||||||||||||
| Gene3D | G3DSA:3.40.1160.10. Aa_kinase. 1 hit. | ||||||||||||||||||
| Pfam | PF00696. AA_kinase. 1 hit. PF01842. ACT. 1 hit. [Graphical view] | ||||||||||||||||||
| TIGRFAMs | TIGR00656. asp_kin_monofn. 1 hit. TIGR00657. asp_kinases. 1 hit. | ||||||||||||||||||
| PROSITE | PS00324. ASPARTOKINASE. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Entry information
| Entry name | AK3_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P08660 Secondary accession number(s): Q2M6T0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


