Reviewed,
UniProtKB/Swiss-Prot P26512 (AK_CORGL)
Last modified
June 16, 2009.
Version 83.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Aspartokinase EC=2.7.2.4 Alternative name(s): Aspartate kinase | ||||
| Gene names |
| ||||
| Organism | Corynebacterium glutamicum (Brevibacterium flavum) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1718 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium |
Protein attributes
| Sequence length | 421 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 | Feedback inhibition by lysine and threonine. |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. |
| Subunit structure | Tetramer consisting of two isoforms Alpha (catalytic) and two isoforms Beta (function not known). |
| Sequence similarities | Belongs to the aspartokinase family. Contains 2 ACT domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Coding sequence diversity | Alternative initiation |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | diaminopimelate 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... | |
Alternative products
| This entry describes 2 isoforms produced by alternative initiation. [Align] [Select] | ||||||
| Isoform Alpha (identifier: P26512-1) Also known as: Aspartokinase subunit alpha; This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Beta (identifier: P26512-2) Also known as: Aspartokinase subunit beta; The sequence of this isoform differs from the canonical sequence as follows: 1-249: Missing. 250-250: V → M |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 421 | 421 | Aspartokinase | PRO_0000002379 | ||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||
| Domain | 266 – 339 | 74 | ACT 1 | |||||||||||||||||||||||||||||||||
| Domain | 348 – 413 | 66 | ACT 2 | |||||||||||||||||||||||||||||||||
Natural variations | ||||||||||||||||||||||||||||||||||||
| Alternative sequence | 1 – 249 | 249 | Missing in isoform Beta. | VSP_018659 | ||||||||||||||||||||||||||||||||
| Alternative sequence | 250 | 1 | V → M in isoform Beta. | VSP_018660 | ||||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||||
| Mutagenesis | 301 | 1 | S → Y: Feedback-resistant and enhanced expression of the asd gene. | |||||||||||||||||||||||||||||||||
| Sequence conflict | 40 | 1 | C → V Ref.1 | |||||||||||||||||||||||||||||||||
| Sequence conflict | 40 | 1 | C → V Ref.4 | |||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||
| Beta strand | 254 – 261 | 8 | ||||||||||||||||||||||||||||||||||
| Beta strand | 263 – 273 | 11 | ||||||||||||||||||||||||||||||||||
| Helix | 278 – 288 | 11 | ||||||||||||||||||||||||||||||||||
| Beta strand | 295 – 298 | 4 | ||||||||||||||||||||||||||||||||||
| Turn | 303 – 305 | 3 | ||||||||||||||||||||||||||||||||||
| Beta strand | 307 – 315 | 9 | ||||||||||||||||||||||||||||||||||
| Helix | 316 – 318 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 319 – 327 | 9 | ||||||||||||||||||||||||||||||||||
| Turn | 328 – 334 | 7 | ||||||||||||||||||||||||||||||||||
| Beta strand | 336 – 342 | 7 | ||||||||||||||||||||||||||||||||||
| Beta strand | 344 – 352 | 9 | ||||||||||||||||||||||||||||||||||
| Helix | 358 – 370 | 13 | ||||||||||||||||||||||||||||||||||
| Beta strand | 377 – 381 | 5 | ||||||||||||||||||||||||||||||||||
| Beta strand | 384 – 390 | 7 | ||||||||||||||||||||||||||||||||||
| Helix | 391 – 393 | 3 | ||||||||||||||||||||||||||||||||||
| Helix | 394 – 405 | 12 | ||||||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum." Kalinowski J., Cremer J., Bachmann B., Eggeling L., Sahm H., Puehler A. Mol. Microbiol. 5:1197-1204(1991) [PubMed: 1956296] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [2] | "Complete genomic sequence of Corynebacterium glutamicum ATCC 13032." Nakagawa S. Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [3] | "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins." Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A., Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A., Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F., Moeckel B. Tauch A.J. Biotechnol. 104:5-25(2003) [PubMed: 12948626] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [4] | "Leucine synthesis in Corynebacterium glutamicum: enzyme activities, structure of leuA, and effect of leuA inactivation on lysine synthesis." Patek M., Krumbach K., Eggeling L., Sahm H. Appl. Environ. Microbiol. 60:133-140(1994) [PubMed: 8117072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-51. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| [5] | "Aspartokinase genes lysC alpha and lysC beta overlap and are adjacent to the aspartate beta-semialdehyde dehydrogenase gene asd in Corynebacterium glutamicum." Kalinowski J., Bachmann B., Thierbach G., Puehler A. Mol. Gen. Genet. 224:317-324(1990) [PubMed: 1980002] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 158-421. Strain: ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| X57226 Genomic DNA. Translation: CAA40502.1. X57226 Genomic DNA. Translation: CAA40503.1. BA000036 Genomic DNA. Translation: BAB97644.1. BX927148 Genomic DNA. Translation: CAF18822.1. X70959 Genomic DNA. Translation: CAA50296.1. Sequence problems. | |||||||||||||
| PIR | I40723. S15276. | ||||||||||||
| RefSeq | NP_599504.1. YP_224551.1. | ||||||||||||
3D structure databases | |||||||||||||
| |||||||||||||
| ModBase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1021294. 3345161. | ||||||||||||
| GenomeReviews | Gene locus Cgl0251 in contig BA000036_GR. Gene locus cg0306 in contig BX927147_GR. | ||||||||||||
| KEGG | cgb:cg0306. cgl:NCgl0247. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | P26512. | ||||||||||||
| OMA | P26512. YEEMLEM. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | CGLU196627-1:CG0306-MON. MetaCyc:MON-6461. MetaCyc:MON-6462. | ||||||||||||
| BRENDA | 2.7.2.4. 812. | ||||||||||||
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. 2 hits. [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 | AK_CORGL | ||||||||
| Accession | Primary (citable) accession number: P26512 Secondary accession number(s): Q59286 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| 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


