Q8KB10 (HIS1_CHLTE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 72.
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 | Chlorobium tepidum (strain ATCC 49652 / DSM 12025 / TLS) [Reference proteome] [HAMAP] | ||||
| Taxonomic identifier | 194439 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Chlorobi › Chlorobia › Chlorobiales › Chlorobiaceae › Chlorobaculum › ![]() |
Protein attributes
| Sequence length | 293 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
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-Rule MF_00079 |
| Catalytic activity | 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_00079 |
| Cofactor | Magnesium By similarity. HAMAP-Rule MF_00079 |
| Enzyme regulation | Feedback inhibited by histidine By similarity. HAMAP-Rule MF_00079 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP-Rule MF_00079 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00079. |
| Sequence similarities | Belongs to the ATP phosphoribosyltransferase family. Long subfamily. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | ATP-binding Magnesium Metal-binding Nucleotide-binding |
| Molecular function | Glycosyltransferase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | histidine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| 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 magnesium ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 293 | 293 | ATP phosphoribosyltransferase HAMAP-Rule MF_00079 | PRO_0000151843 | |||
Sequences
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References
| [1] | "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic, anaerobic, green-sulfur bacterium." Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J., DeBoy R.T., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D., Durkin A.S., Kolonay J.F., Yang F., Holt I.E., Umayam L.A., Mason T.M. Fraser C.M.Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49652 / DSM 12025 / TLS. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE006470 Genomic DNA. Translation: AAM73206.1. |
| RefSeq | NP_662864.1. NC_002932.3. |
3D structure databases | |
| ProteinModelPortal | Q8KB10. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 194439.CT1988. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAM73206; AAM73206; CT1988. |
| GeneID | 1007573. |
| KEGG | cte:CT1988. |
| PATRIC | 21401795. VBIChlTep116050_1801. |
Phylogenomic databases | |
| eggNOG | COG0040. |
| HOGENOM | HOG000223250. |
| KO | K00765. |
| OMA | EGKHIAT. |
| ProtClustDB | PRK00489. |
Enzyme and pathway databases | |
| BioCyc | CTEP194439:GHN0-2028-MONOMER. |
| UniPathway | UPA00031; UER00006. |
Family and domain databases | |
| Gene3D | 3.30.70.120. 1 hit. |
| HAMAP | MF_00079. HisG_Long. |
| InterPro | IPR013820. ATP_PRibTrfase_cat. IPR001348. ATP_PRibTrfase_HisG. IPR020621. ATP_PRibTrfase_HisG_long. IPR013115. HisG_C. IPR011322. N-reg_PII-like_a/b. IPR015867. N-reg_PII/ATP_PRibTrfase_C. [Graphical view] |
| PANTHER | PTHR21403. PTHR21403. 1 hit. |
| Pfam | PF01634. HisG. 1 hit. PF08029. HisG_C. 1 hit. [Graphical view] |
| SUPFAM | SSF54913. N-reg_PII-like_a/b. 1 hit. |
| TIGRFAMs | TIGR00070. hisG. 1 hit. TIGR03455. HisG_C-term. 1 hit. |
| PROSITE | PS01316. ATP_P_PHORIBOSYLTR. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS1_CHLTE | ||||||||
| Accession | Primary (citable) accession number: Q8KB10 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with
