Reviewed,
UniProtKB/Swiss-Prot P62346 (HIS2_BACC1)
Last modified
February 9, 2010.
Version 40.
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 | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 107 AA. |
| Sequence status | Complete. |
| 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 HAMAP MF_01020. |
| 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_0000136344 | |||
Sequences
References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS40461.1. |
| RefSeq | NP_977853.1. |
3D structure databases | |
| SMR | P62346. Positions 4-95. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P62346. |
Genome annotation databases | |
| GeneID | 2751481. |
| GenomeReviews | Gene locus BCE_1532 in contig AE017194_GR. |
| KEGG | bca:BCE_1532. |
| NMPDR | fig|222523.1.peg.1525. |
| TIGR | BCE_1532. |
Phylogenomic databases | |
| eggNOG | COG0140. |
| HOGENOM | HBG646527. |
| OMA | THEKGEN. |
Family and domain databases | |
| HAMAP | MF_01020. HisE. [Tree] |
| InterPro | IPR008179. PRib-ATP_pyrophosphohydrolase. IPR021130. PRib-ATP_pyroPHydrolase-like. [Graphical view] |
| Pfam | PF01503. PRA-PH. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR03188. histidine_hisI. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HIS2_BACC1 | ||||||||
| Accession | Primary (citable) accession number: P62346 | ||||||||
| 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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