Q0W3T3 (Q0W3T3_UNCMA) Unreviewed, UniProtKB/TrEMBL
Last modified
November 16, 2011.
Version 46.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Adenylosuccinate synthetase HAMAP MF_00011 Short name=AMPSase HAMAP MF_00011 Short name=AdSS HAMAP MF_00011 EC=6.3.4.4 HAMAP MF_00011 Alternative name(s): IMP--aspartate ligase HAMAP MF_00011 | ||||||
| Gene names |
| ||||||
| Organism | Uncultured methanogenic archaeon RC-I [Complete proteome] [HAMAP] EMBL CAJ36960.1 | ||||||
| Taxonomic identifier | 351160 [NCBI] | ||||||
| Taxonomic lineage | Archaea › Euryarchaeota › environmental samples |
Protein attributes
| Sequence length | 335 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 By similarity. RuleBase RU000520 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. RuleBase RU000520 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. RuleBase RU000520 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. HAMAP MF_00011 RuleBase RU004163 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis RuleBase RU000520 HAMAP MF_00011 |
| Cellular component | Cytoplasm HAMAP MF_00011 |
| Ligand | GTP-binding RuleBase RU000520 HAMAP MF_00011 Magnesium RuleBase RU000520 HAMAP MF_00011 Metal-binding RuleBase RU000520 HAMAP MF_00011 Nucleotide-binding |
| Molecular function | Ligase RuleBase RU000520 HAMAP MF_00011 EMBL CAJ36960.1 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | purine nucleotide biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | GTP binding Inferred from electronic annotation. Source: HAMAP adenylosuccinate synthase activityInferred from electronic annotation. Source: HAMAP magnesium ion bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 12 – 18 | 7 | GTP By similarity HAMAP MF_00011 | ||||||
| Nucleotide binding | 42 – 44 | 3 | GTP By similarity HAMAP MF_00011 | ||||||
| Nucleotide binding | 281 – 283 | 3 | GTP By similarity HAMAP MF_00011 | ||||||
| Nucleotide binding | 321 – 323 | 3 | GTP By similarity HAMAP MF_00011 | ||||||
| Region | 13 – 16 | 4 | IMP binding By similarity HAMAP MF_00011 | ||||||
| Region | 40 – 43 | 4 | IMP binding By similarity HAMAP MF_00011 | ||||||
| Region | 249 – 255 | 7 | Substrate binding By similarity HAMAP MF_00011 | ||||||
Sites | |||||||||
| Active site | 13 | 1 | Proton acceptor By similarity HAMAP MF_00011 | ||||||
| Active site | 43 | 1 | Proton donor By similarity HAMAP MF_00011 | ||||||
| Metal binding | 13 | 1 | Magnesium By similarity HAMAP MF_00011 | ||||||
| Metal binding | 42 | 1 | Magnesium; via carbonyl oxygen By similarity HAMAP MF_00011 | ||||||
| Binding site | 124 | 1 | IMP By similarity HAMAP MF_00011 | ||||||
| Binding site | 138 | 1 | IMP; shared with dimeric partner By similarity HAMAP MF_00011 | ||||||
| Binding site | 176 | 1 | IMP By similarity HAMAP MF_00011 | ||||||
| Binding site | 191 | 1 | IMP By similarity HAMAP MF_00011 | ||||||
| Binding site | 253 | 1 | IMP By similarity HAMAP MF_00011 | ||||||
| Binding site | 255 | 1 | GTP By similarity HAMAP MF_00011 | ||||||
Sequences
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References
| [1] | "Genome of rice cluster I archaea -- the key methane producers in the rice rhizosphere." Erkel C., Kube M., Reinhardt R., Liesack W. Science 313:370-372(2006) [PubMed: 16857943] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AM114193 Genomic DNA. Translation: CAJ36960.1. |
| RefSeq | YP_686286.1. NC_009464.1. |
3D structure databases | |
| ProteinModelPortal | Q0W3T3. |
| SMR | Q0W3T3. Positions 1-333. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q0W3T3. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5143947. |
| GenomeReviews | Gene locus UNCMA_12780 in contig AM114193_GR. |
| KEGG | rci:RCIX1751. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | arNOG04146. |
| HOGENOM | HBG658237. |
| OMA | IDPHVGI. |
| ProtClustDB | PRK04293. |
Enzyme and pathway databases | |
| BioCyc | UMET351160:RCIX1751-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. 2 hits. [Graphical view] |
| SMART | SM00788. Adenylsucc_synt. 1 hit. [Graphical view] |
| PROSITE | PS01266. ADENYLOSUCCIN_SYN_1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | Q0W3T3_UNCMA | ||||||||
| Accession | Primary (citable) accession number: Q0W3T3 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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