Q7N8D4 (PURA1_PHOLL) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 59.
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: Adenylosuccinate synthetase 1 Short name=AMPSase 1 Short name=AdSS 1 EC=6.3.4.4 Alternative name(s): IMP--aspartate ligase 1 | ||||
| Gene names |
| ||||
| Organism | Photorhabdus luminescens subsp. laumondii (strain TT01) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243265 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Photorhabdus |
Protein attributes
| Sequence length | 419 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first commited step in the biosynthesis of AMP from IMP By similarity. HAMAP MF_00011 |
| Catalytic activity | GTP + IMP + L-aspartate = GDP + phosphate + N(6)-(1,2-dicarboxyethyl)-AMP. HAMAP MF_00011 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. HAMAP MF_00011 |
| Pathway | Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2. HAMAP MF_00011 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00011 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00011. |
| Sequence similarities | Belongs to the adenylosuccinate synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | GTP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Ligase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylosuccinate synthase activityInferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 419 | 419 | Adenylosuccinate synthetase 1 HAMAP MF_00011 | PRO_0000095207 | |||||
Regions | |||||||||
| Nucleotide binding | 11 – 17 | 7 | GTP By similarity | ||||||
| Nucleotide binding | 326 – 328 | 3 | GTP By similarity | ||||||
| Nucleotide binding | 407 – 409 | 3 | GTP By similarity | ||||||
| Region | 12 – 15 | 4 | IMP binding By similarity | ||||||
| Region | 37 – 40 | 4 | IMP binding By similarity | ||||||
| Region | 294 – 300 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 12 | 1 | Proton acceptor By similarity | ||||||
| Active site | 40 | 1 | Proton donor By similarity | ||||||
| Metal binding | 12 | 1 | Magnesium By similarity | ||||||
| Metal binding | 39 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 138 | 1 | IMP; shared with dimeric partner By similarity | ||||||
| Binding site | 220 | 1 | IMP By similarity | ||||||
| Binding site | 298 | 1 | IMP By similarity | ||||||
| Binding site | 300 | 1 | GTP By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the entomopathogenic bacterium Photorhabdus luminescens." Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A., Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F., Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C., Lanois A., Powell K. Kunst F.Nat. Biotechnol. 21:1307-1313(2003) [PubMed: 14528314] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: TT01. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX571861 Genomic DNA. Translation: CAE13089.1. |
| RefSeq | NP_928139.1. NC_005126.1. |
3D structure databases | |
| ProteinModelPortal | Q7N8D4. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2800757. |
| GenomeReviews | Gene locus plu0794 in contig BX470251_GR. |
| KEGG | plu:plu0794. |
| NMPDR | fig|243265.1.peg.763. |
| PATRIC | 20505199. VBIPhoLum48522_0873. |
Organism-specific databases | |
| GenoList | plu0794. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG658237. |
| OMA | RERGNEY. |
| PhylomeDB | Q7N8D4. |
| ProtClustDB | CLSK2521706. |
Enzyme and pathway databases | |
| BioCyc | PLUM243265:PLU0794-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00011. Adenylosucc_synth. [Tree] |
| InterPro | IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view] |
| KO | K01939. |
| PANTHER | PTHR11846. Asucc_synthtase. 1 hit. |
| Pfam | PF00709. Adenylsucc_synt. 1 hit. [Graphical view] |
| SMART | SM00788. Adenylsucc_synt. 1 hit. [Graphical view] |
| PROSITE | PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PURA1_PHOLL | ||||||||
| Accession | Primary (citable) accession number: Q7N8D4 | ||||||||
| 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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