P96771 (PURA_AGGAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 69.
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 |
| ||
| Organism | Aggregatibacter actinomycetemcomitans (Actinobacillus actinomycetemcomitans) (Haemophilus actinomycetemcomitans) | ||
| Taxonomic identifier | 714 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Aggregatibacter |
Protein attributes
| Sequence length | 259 AA. |
| Sequence status | Fragment. |
| 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 |
| 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 – 259 | ›259 | Adenylosuccinate synthetase HAMAP MF_00011 | PRO_0000095139 | |||||
Regions | |||||||||
| Nucleotide binding | 3 – 9 | 7 | GTP By similarity | ||||||
| Nucleotide binding | 31 – 33 | 3 | GTP By similarity | ||||||
| Region | 4 – 7 | 4 | IMP binding By similarity | ||||||
Sites | |||||||||
| Active site | 4 | 1 | Proton acceptor By similarity | ||||||
| Active site | 32 | 1 | Proton donor By similarity | ||||||
| Metal binding | 4 | 1 | Magnesium By similarity | ||||||
| Metal binding | 31 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 120 | 1 | IMP By similarity | ||||||
| Binding site | 134 | 1 | IMP; shared with dimeric partner By similarity | ||||||
| Binding site | 215 | 1 | IMP By similarity | ||||||
| Binding site | 230 | 1 | IMP By similarity | ||||||
Experimental info | |||||||||
| Non-terminal residue | 1 | 1 | |||||||
Sequences
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References
| [1] | "Codon usage in Actinobacillus actinomycetemcomitans." Kaplan J.B., Fine D.H. FEMS Microbiol. Lett. 163:31-36(1998) [PubMed: 9631542] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: CU1000. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U89525 Genomic DNA. Translation: AAC46412.1. |
3D structure databases | |
| ProteinModelPortal | P96771. |
| SMR | P96771. Positions 1-259. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
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] |
| PROSITE | PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. PS00513. ADENYLOSUCCIN_SYN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PURA_AGGAC | ||||||||
| Accession | Primary (citable) accession number: P96771 | ||||||||
| 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 |

Clusters with