Q8PWS3 (HIS1_METMA) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 65.
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 |
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| Organism | Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 192952 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanomicrobia › Methanosarcinales › Methanosarcinaceae › Methanosarcina |
Protein attributes
| Sequence length | 289 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 MF_00079 |
| Catalytic activity | 1-(5-phospho-D-ribosyl)-ATP + diphosphate = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP MF_00079 |
| Cofactor | Magnesium By similarity. HAMAP MF_00079 |
| Enzyme regulation | Feedback inhibited by histidine By similarity. HAMAP MF_00079 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. HAMAP MF_00079 |
| Subcellular location | Cytoplasm By similarity HAMAP 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 |
| 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 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 – 289 | 289 | ATP phosphoribosyltransferase HAMAP MF_00079 | PRO_0000151884 | |||
Sequences
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References
| [1] | "The genome of Methanosarcina mazei: evidence for lateral gene transfer between Bacteria and Archaea." Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A., Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C., Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S., Bhattacharyya A., Lykidis A., Overbeek R. Gottschalk G.J. Mol. Microbiol. Biotechnol. 4:453-461(2002) [PubMed: 12125824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE008384 Genomic DNA. Translation: AAM31199.1. |
| RefSeq | NP_633527.1. NC_003901.1. |
3D structure databases | |
| ProteinModelPortal | Q8PWS3. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1479845. |
| GenomeReviews | Gene locus MM_1503 in contig AE008384_GR. |
| KEGG | mma:MM_1503. |
| NMPDR | fig|192952.1.peg.1503. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG391868. |
| OMA | IMLHAPS. |
| PhylomeDB | Q8PWS3. |
| ProtClustDB | PRK00489. |
Enzyme and pathway databases | |
| BioCyc | MMAZ192952:MM1503-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00079. HisG_Long. [Tree] |
| InterPro | IPR013820. ATP_PRibTrfase_cat. IPR018198. ATP_PRibTrfase_CS. 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] |
| Gene3D | G3DSA:3.30.70.120. PII_glnB. 1 hit. |
| KO | K00765. |
| PANTHER | PTHR21403. ATP_phspho_trans. 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. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | HIS1_METMA | ||||||||
| Accession | Primary (citable) accession number: Q8PWS3 | ||||||||
| 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