P56468 (PUR8_HELPY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 94.
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 lyase Short name=ASL EC=4.3.2.2 Alternative name(s): Adenylosuccinase Short name=ASase | ||||
| Gene names |
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| Organism | Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 85962 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter › ![]() |
Protein attributes
| Sequence length | 440 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Catalytic activity | N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. |
| Pathway | Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2. |
| Subunit structure | Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site By similarity. |
| Sequence similarities | Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Purine biosynthesis |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | 'de novo' AMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway 'de novo' IMP biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity Inferred from electronic annotation. Source: EC N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) 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 – 440 | 440 | Adenylosuccinate lyase | PRO_0000137881 | |||||
Regions | |||||||||
| Region | 4 – 5 | 2 | Substrate binding By similarity | ||||||
| Region | 67 – 69 | 3 | Substrate binding By similarity | ||||||
| Region | 93 – 94 | 2 | Substrate binding By similarity | ||||||
| Region | 268 – 270 | 3 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Active site | 141 | 1 | Proton donor/acceptor By similarity | ||||||
| Active site | 262 | 1 | Proton donor/acceptor By similarity | ||||||
| Binding site | 212 | 1 | Substrate By similarity | ||||||
| Binding site | 276 | 1 | Substrate By similarity | ||||||
| Binding site | 301 | 1 | Substrate By similarity | ||||||
| Binding site | 306 | 1 | Substrate By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C.Nature 388:539-547(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE000511 Genomic DNA. Translation: AAD08156.1. |
| PIR | H64658. |
| RefSeq | NP_207903.1. NC_000915.1. YP_006935027.1. NC_018939.1. |
3D structure databases | |
| ProteinModelPortal | P56468. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 85962.HP1112. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAD08156; AAD08156; HP_1112. |
| GeneID | 13870305. 899648. |
| KEGG | heo:C694_05735. hpy:HP1112. |
| PATRIC | 20593565. VBIHelPyl33062_1162. |
Phylogenomic databases | |
| eggNOG | COG0015. |
| KO | K01756. |
| OMA | KIAVNIR. |
| ProtClustDB | PRK08470. |
Enzyme and pathway databases | |
| UniPathway | UPA00074; UER00132. UPA00075; UER00336. |
Family and domain databases | |
| Gene3D | 1.10.275.10. 1 hit. |
| InterPro | IPR019468. AdenyloSucc_lyase_C. IPR024083. Fumarase/histidase_N. IPR000362. Fumarate_lyase. IPR020557. Fumarate_lyase_CS. IPR022761. Fumarate_lyase_N. IPR008948. L-Aspartase-like. IPR004769. Pur_lyase. [Graphical view] |
| PANTHER | PTHR11444:SF2. PTHR11444:SF2. 1 hit. |
| Pfam | PF10397. ADSL_C. 1 hit. PF00206. Lyase_1. 1 hit. [Graphical view] |
| PRINTS | PR00149. FUMRATELYASE. |
| SMART | SM00998. ADSL_C. 1 hit. [Graphical view] |
| SUPFAM | SSF48557. L-Aspartase-like. 1 hit. |
| TIGRFAMs | TIGR00928. purB. 1 hit. |
| PROSITE | PS00163. FUMARATE_LYASES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PUR8_HELPY | ||||||||
| Accession | Primary (citable) accession number: P56468 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Helicobacter pylori Helicobacter pylori (strain 26695): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
