Q7P0E6 (HIS2_CHRVO) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 60.
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: Phosphoribosyl-ATP pyrophosphatase Short name=PRA-PH EC=3.6.1.31 | ||||
| Gene names |
| ||||
| Organism | Chromobacterium violaceum [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 536 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium |
Protein attributes
| Sequence length | 108 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 | 3D-structure Complete proteome |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| 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: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||
Molecule processing | ||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 108 | 108 | Phosphoribosyl-ATP pyrophosphatase HAMAP MF_01020 | PRO_0000136356 | ||||||||||||||||||
Secondary structure | ||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||
| Helix | 6 – 15 | 10 | ||||||||||||||||||||
| Helix | 16 – 18 | 3 | ||||||||||||||||||||
| Turn | 21 – 23 | 3 | ||||||||||||||||||||
| Helix | 25 – 32 | 8 | ||||||||||||||||||||
| Helix | 34 – 53 | 20 | ||||||||||||||||||||
| Helix | 57 – 77 | 21 | ||||||||||||||||||||
| Helix | 82 – 92 | 11 | ||||||||||||||||||||
Sequences
References
| [1] | "The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability." Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. Simpson A.J.G.Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE016825 Genomic DNA. Translation: AAQ58297.1. | ||||||||||||
| RefSeq | NP_900291.1. NC_005085.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q7P0E6. | ||||||||||||
| SMR | Q7P0E6. Positions 4-94. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 2550491. | ||||||||||||
| GenomeReviews | Gene locus CV_0621 in contig AE016825_GR. | ||||||||||||
| KEGG | cvi:CV_0621. | ||||||||||||
| NMPDR | fig|243365.1.peg.621. | ||||||||||||
| PATRIC | 21436038. VBIChrVio67196_0620. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG646527. | ||||||||||||
| OMA | ETVMAAK. | ||||||||||||
| ProtClustDB | PRK00400. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | CVIO243365:CV_0621-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01020. HisE. [Tree] | ||||||||||||
| InterPro | IPR008179. PRib-ATP_PPHydrolase. IPR021130. PRib-ATP_PPHydrolase-like. [Graphical view] | ||||||||||||
| KO | K01523. | ||||||||||||
| Pfam | PF01503. PRA-PH. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR03188. Histidine_hisI. 1 hit. | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | HIS2_CHRVO | ||||||||
| Accession | Primary (citable) accession number: Q7P0E6 | ||||||||
| 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 |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with