Reviewed,
UniProtKB/Swiss-Prot Q898L3 (HIS2_CLOTE)
Last modified
June 16, 2009.
Version 37.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Phosphoribosyl-ATP pyrophosphatase Short name=PRA-PH EC=3.6.1.31 | ||||
| Gene names |
| ||||
| Organism | Clostridium tetani [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1513 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium |
Protein attributes
| Sequence length | 107 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01020 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01020 |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the PRA-PH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosyl-ATP diphosphatase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 107 | 107 | Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020 | PRO_0000136358 | |||
Sequences
References
| [1] | "The genome sequence of Clostridium tetani, the causative agent of tetanus disease." Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G. Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003) [PubMed: 12552129] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Massachusetts / E88. |
Cross-references
Sequence databases | |
|---|---|
| AE015927 Genomic DNA. Translation: AAO35066.1. | |
| RefSeq | NP_781129.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1060034. |
| GenomeReviews | Gene locus CTC_00432 in contig AE015927_GR. |
| KEGG | ctc:CTC00432. |
| NMPDR | fig|212717.1.peg.351. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q898L3. |
Enzyme and pathway databases | |
| BioCyc | CTET212717:CTC_00432-MON. |
| BRENDA | 3.6.1.31. 2082. |
Family and domain databases | |
| HAMAP | MF_01020. Divergent sequence. [Tree] |
| InterPro | IPR008179. PRib-ATP_pyrophosphohydrolase. [Graphical view] |
| Pfam | PF01503. PRA-PH. 1 hit. [Graphical view] |
| ProDom | PD002611. Pra_PH/CH. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR03188. histidine_hisI. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HIS2_CLOTE | ||||||||
| Accession | Primary (citable) accession number: Q898L3 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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