P62381 (HIS1_THET2) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
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: ATP phosphoribosyltransferase Short name=ATP-PRT Short name=ATP-PRTase EC=2.4.2.17 | ||||
| Gene names |
| ||||
| Organism | Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 262724 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus |
Protein attributes
| Sequence length | 206 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity By similarity. HAMAP MF_01018 |
| Catalytic activity | 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_01018 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_01018 |
| Subunit structure | Heteromultimer composed of HisG and HisZ subunits By similarity. |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01018. |
| Domain | Lacks the C-terminal regulatory region which is replaced by HisZ. HAMAP MF_01018 |
| Sequence similarities | Belongs to the ATP phosphoribosyltransferase family. Short subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Glycosyltransferase Transferase |
| 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 ATP phosphoribosyltransferase 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 – 206 | 206 | ATP phosphoribosyltransferase HAMAP MF_01018 | PRO_0000151945 | ||||||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 4 – 11 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 16 – 25 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 46 – 52 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 54 – 56 | 3 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 57 – 62 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 65 – 72 | 8 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 73 – 78 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 88 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 94 – 100 | 7 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 110 – 114 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 116 – 125 | 10 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 131 – 134 | 4 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 140 – 144 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 147 – 158 | 12 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 159 – 163 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 167 – 175 | 9 | ||||||||||||||||||||||||||||||||||||||||||
| Beta strand | 177 – 181 | 5 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 183 – 188 | 6 | ||||||||||||||||||||||||||||||||||||||||||
| Helix | 190 – 202 | 13 | ||||||||||||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "The genome sequence of the extreme thermophile Thermus thermophilus." Henne A., Brueggemann H., Raasch C., Wiezer A., Hartsch T., Liesegang H., Johann A., Lienard T., Gohl O., Martinez-Arias R., Jacobi C., Starkuviene V., Schlenczeck S., Dencker S., Huber R., Klenk H.-P., Kramer W., Merkl R., Gottschalk G., Fritz H.-J. Nat. Biotechnol. 22:547-553(2004) [PubMed: 15064768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HB27 / ATCC BAA-163 / DSM 7039. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE017221 Genomic DNA. Translation: AAS82208.1. | ||||||||||||
| RefSeq | YP_005835.1. NC_005835.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | P62381. | ||||||||||||
| SMR | P62381. Positions 1-206. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | P62381. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 2775570. | ||||||||||||
| GenomeReviews | Gene locus TT_C1866 in contig AE017221_GR. | ||||||||||||
| PATRIC | 23954203. VBITheThe54392_1865. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | COG0040. | ||||||||||||
| HOGENOM | HBG391868. | ||||||||||||
| OMA | QVDIIKL. | ||||||||||||
| PhylomeDB | P62381. | ||||||||||||
| ProtClustDB | PRK01686. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | TTHE262724:TT_C1866-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01018. HisG_Short. [Tree] | ||||||||||||
| InterPro | IPR013820. ATP_PRibTrfase_cat. IPR018198. ATP_PRibTrfase_CS. IPR001348. ATP_PRibTrfase_HisG. IPR024893. ATP_PRibTrfase_HisG_short. [Graphical view] | ||||||||||||
| PANTHER | PTHR21403. ATP_phspho_trans. 1 hit. | ||||||||||||
| Pfam | PF01634. HisG. 1 hit. [Graphical view] | ||||||||||||
| TIGRFAMs | TIGR00070. HisG. 1 hit. | ||||||||||||
| PROSITE | PS01316. ATP_P_PHORIBOSYLTR. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | HIS1_THET2 | ||||||||
| Accession | Primary (citable) accession number: P62381 | ||||||||
| 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 |

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