P27725 (AK1H_SERMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 87.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Bifunctional aspartokinase/homoserine dehydrogenase 1 Alternative name(s): Aspartokinase I/homoserine dehydrogenase I Short name=AKI-HDI | ||||
| Gene names |
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| Organism | Serratia marcescens | ||||
| Taxonomic identifier | 615 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Serratia |
Protein attributes
| Sequence length | 819 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | L-homoserine + NAD(P)+ = L-aspartate 4-semialdehyde + NAD(P)H. ATP + L-aspartate = ADP + 4-phospho-L-aspartate. |
| Enzyme regulation | The enzyme activities are regulated allosterically by L-threonine. |
| Pathway | Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5. |
| Subunit structure | Homotetramer. |
| Sequence similarities | In the N-terminal section; belongs to the aspartokinase family. In the C-terminal section; belongs to the homoserine dehydrogenase family. Contains 2 ACT domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Threonine biosynthesis |
| Domain | Repeat |
| Ligand | ATP-binding NADP Nucleotide-binding |
| Molecular function | Kinase Oxidoreductase Transferase |
| Technical term | Allosteric enzyme Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | threonine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW NADP bindingInferred from electronic annotation. Source: InterPro amino acid bindingInferred from electronic annotation. Source: InterPro aspartate kinase activityInferred from electronic annotation. Source: EC homoserine dehydrogenase 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 – 819 | 819 | Bifunctional aspartokinase/homoserine dehydrogenase 1 | PRO_0000066682 | |||||
Regions | |||||||||
| Domain | 316 – 385 | 70 | ACT 1 | ||||||
| Domain | 397 – 468 | 72 | ACT 2 | ||||||
| Nucleotide binding | 471 – 478 | 8 | NADP Potential | ||||||
| Region | 1 – 249 | 249 | Aspartokinase By similarity | ||||||
| Region | 250 – 470 | 221 | Interface By similarity | ||||||
| Region | 471 – 819 | 349 | Homoserine dehydrogenase By similarity | ||||||
Natural variations | |||||||||
| Natural variant | 330 | 1 | G → D in strain: Sr41 / 8000, Sr41 / HNr21; loss of feedback inhibition. | ||||||
| Natural variant | 352 | 1 | S → F in strain: Sr41 / TLr156; loss of feedback inhibition. | ||||||
| Natural variant | 479 | 1 | A → T in strain: Sr41 / HNr59; Thr-resistant HDI. | ||||||
Sequences
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References
| [1] | "Nucleotide sequence of the Serratia marcescens threonine operon and analysis of the threonine operon mutations which alter feedback inhibition of both aspartokinase I and homoserine dehydrogenase I." Omori K., Suzuki S., Komatsubara S. J. Bacteriol. 175:785-794(1993) [PubMed: 8423151] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Sr41 / 8000, Sr41 / HNr21, Sr41 / HNr59 and Sr41 / TLr156. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D10385 Genomic DNA. Translation: BAA38474.1. D10386 Genomic DNA. Translation: BAA38477.1. D10387 Genomic DNA. Translation: BAA38480.1. X60821 Genomic DNA. Translation: CAA43212.1. |
| PIR | B47057. |
3D structure databases | |
| ProteinModelPortal | P27725. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR002912. ACT-bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR005106. Asp/hSer_DH_NAD-bd. IPR001341. Asp_kinase_dom. IPR018042. Aspartate_kinase_CS. IPR011147. Bifunc_aspartokin/hSer_DH. IPR001342. HDH_cat. IPR019811. HDH_CS. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.1160.10. Aa_kinase. 2 hits. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00696. AA_kinase. 1 hit. PF01842. ACT. 2 hits. PF00742. Homoserine_dh. 1 hit. PF03447. NAD_binding_3. 1 hit. [Graphical view] |
| PIRSF | PIRSF000727. ThrA. 1 hit. |
| SUPFAM | SSF53633. Aa_kinase. 1 hit. |
| TIGRFAMs | TIGR00657. Asp_kinases. 1 hit. |
| PROSITE | PS00324. ASPARTOKINASE. 1 hit. PS01042. HOMOSER_DHGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AK1H_SERMA | ||||||||
| Accession | Primary (citable) accession number: P27725 Secondary accession number(s): Q59936 Q60157 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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