Reviewed,
UniProtKB/Swiss-Prot O84367 (AK_CHLTR)
Last modified
June 16, 2009.
Version 49.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Aspartokinase EC=2.7.2.4 Alternative name(s): Aspartate kinase | ||||
| Gene names |
| ||||
| Organism | Chlamydia trachomatis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 813 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlamydiae › Chlamydiales › Chlamydiaceae › Chlamydia |
Protein attributes
| Sequence length | 431 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | ATP + L-aspartate = ADP + 4-phospho-L-aspartate. |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. |
| Sequence similarities | Belongs to the aspartokinase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Kinase Transferase |
| Technical term | 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 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 – 431 | 431 | Aspartokinase | PRO_0000066675 | |||
Sequences
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References
| [1] | "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia trachomatis." Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L., Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W. Science 282:754-759(1998) [PubMed: 9784136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: D/UW-3/Cx. |
Cross-references
Sequence databases | |
|---|---|
| AE001273 Genomic DNA. Translation: AAC67958.1. | |
| PIR | G71524. |
| RefSeq | NP_219871.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 884754. |
| GenomeReviews | Gene locus CT_362 in contig AE001273_GR. |
| KEGG | ctr:CT362. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O84367. |
| OMA | O84367. RERHESI. |
Enzyme and pathway databases | |
| BioCyc | CTRA315277:CT362-MON. |
| BRENDA | 2.7.2.4. 108. |
Family and domain databases | |
| InterPro | IPR001048. Asp/Glu/Uridylate_kinase. 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. [Graphical view] |
| TIGRFAMs | TIGR00657. asp_kinases. 1 hit. |
| PROSITE | PS00324. ASPARTOKINASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AK_CHLTR | ||||||||
| Accession | Primary (citable) accession number: O84367 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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