B4S195 (PURA_ALTMD) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 25.
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 Short name=AMPSase Short name=AdSS EC=6.3.4.4 Alternative name(s): IMP--aspartate ligase | ||||
| Gene names |
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| Organism | Alteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 314275 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Alteromonadaceae › Alteromonas |
Protein attributes
| Sequence length | 432 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 – 432 | 432 | Adenylosuccinate synthetase HAMAP MF_00011 | PRO_1000089266 | |||||
Regions | |||||||||
| Nucleotide binding | 13 – 19 | 7 | GTP By similarity | ||||||
| Nucleotide binding | 41 – 43 | 3 | GTP By similarity | ||||||
| Nucleotide binding | 332 – 334 | 3 | GTP By similarity | ||||||
| Nucleotide binding | 415 – 417 | 3 | GTP By similarity | ||||||
| Region | 14 – 17 | 4 | IMP binding By similarity | ||||||
| Region | 39 – 42 | 4 | IMP binding By similarity | ||||||
| Region | 300 – 306 | 7 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 14 | 1 | Proton acceptor By similarity | ||||||
| Active site | 42 | 1 | Proton donor By similarity | ||||||
| Metal binding | 14 | 1 | Magnesium By similarity | ||||||
| Metal binding | 41 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 130 | 1 | IMP By similarity | ||||||
| Binding site | 144 | 1 | IMP; shared with dimeric partner By similarity | ||||||
| Binding site | 225 | 1 | IMP By similarity | ||||||
| Binding site | 240 | 1 | IMP By similarity | ||||||
| Binding site | 304 | 1 | IMP By similarity | ||||||
| Binding site | 306 | 1 | GTP By similarity | ||||||
Sequences
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References
| [1] | "Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter." Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F. ISME J. 2:1194-1212(2008) [PubMed: 18670397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: DSM 17117 / Deep ecotype. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001103 Genomic DNA. Translation: AEA96735.1. |
| RefSeq | YP_004425733.1. NC_011138.2. |
3D structure databases | |
| ProteinModelPortal | B4S195. |
| SMR | B4S195. Positions 4-432. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B4S195. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 10555932. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG658237. |
| OMA | YVLGIIK. |
| ProtClustDB | PRK01117. |
Family and domain databases | |
| HAMAP | MF_00011. Adenylosucc_synth. [Tree] |
| InterPro | IPR018220. Adenylosuccinate_synthase_AS. IPR001114. Adenylosuccinate_synthetase. [Graphical view] |
| PANTHER | PTHR11846. Asucc_synthtase. 1 hit. |
| Pfam | PF00709. Adenylsucc_synt. 1 hit. [Graphical view] |
| SMART | SM00788. Adenylsucc_synt. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00184. PurA. 1 hit. |
| PROSITE | PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PURA_ALTMD | ||||||||
| Accession | Primary (citable) accession number: B4S195 Secondary accession number(s): F2G7F5 | ||||||||
| 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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