O26347 (HIS3_METTH) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 80.
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-AMP cyclohydrolase Short name=PRA-CH EC=3.5.4.19 | ||||
| Gene names |
| ||||
| Organism | Methanobacterium thermoautotrophicum (strain Delta H) | ||||
| Taxonomic identifier | 187420 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanobacteria › Methanobacteriales › Methanobacteriaceae › Methanothermobacter |
Protein attributes
| Sequence length | 138 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01021 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. HAMAP MF_01021 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01021. |
| Sequence similarities | Belongs to the PRA-CH family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Amino-acid biosynthesis Histidine biosynthesis |
| Cellular component | Cytoplasm |
| Molecular function | Hydrolase |
| Technical term | 3D-structure Complete proteome Reference 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 | phosphoribosyl-AMP cyclohydrolase activity Inferred 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 – 138 | 138 | Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01021 | PRO_0000136511 | |||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||
| Helix | 9 – 11 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 18 – 20 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 24 – 30 | 7 | |||||||||||||||||||||||||||||||||
| Turn | 31 – 33 | 3 | |||||||||||||||||||||||||||||||||
| Beta strand | 36 – 42 | 7 | |||||||||||||||||||||||||||||||||
| Helix | 44 – 53 | 10 | |||||||||||||||||||||||||||||||||
| Beta strand | 57 – 60 | 4 | |||||||||||||||||||||||||||||||||
| Turn | 61 – 64 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 65 – 68 | 4 | |||||||||||||||||||||||||||||||||
| Turn | 69 – 73 | 5 | |||||||||||||||||||||||||||||||||
| Beta strand | 77 – 84 | 8 | |||||||||||||||||||||||||||||||||
| Beta strand | 88 – 99 | 12 | |||||||||||||||||||||||||||||||||
| Beta strand | 105 – 109 | 5 | |||||||||||||||||||||||||||||||||
| Beta strand | 112 – 115 | 4 | |||||||||||||||||||||||||||||||||
| Beta strand | 118 – 121 | 4 | |||||||||||||||||||||||||||||||||
Sequences
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References
| [1] | "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH: functional analysis and comparative genomics." Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J., Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D., Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R. Reeve J.N.J. Bacteriol. 179:7135-7155(1997) [PubMed: 9371463] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Delta H. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE000666 Genomic DNA. Translation: AAB84751.1. | ||||||||||||
| PIR | F69130. | ||||||||||||
| RefSeq | NP_275388.1. NC_000916.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | O26347. | ||||||||||||
| SMR | O26347. Positions 4-131. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein-protein interaction databases | |||||||||||||
| STRING | O26347. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1470206. | ||||||||||||
| GenomeReviews | Gene locus MTH_245 in contig AE000666_GR. | ||||||||||||
| KEGG | mth:MTH245. | ||||||||||||
| NMPDR | fig|187420.1.peg.243. | ||||||||||||
Phylogenomic databases | |||||||||||||
| eggNOG | arNOG12274. | ||||||||||||
| HOGENOM | HBG294308. | ||||||||||||
| OMA | TQYVHEV. | ||||||||||||
| PhylomeDB | O26347. | ||||||||||||
| ProtClustDB | PRK00051. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | MTHE187420:MTH245-MONOMER. | ||||||||||||
Family and domain databases | |||||||||||||
| HAMAP | MF_01021. HisI. [Tree] | ||||||||||||
| InterPro | IPR002496. PRib_AMP_CycHydrolase. [Graphical view] | ||||||||||||
| KO | K01496. | ||||||||||||
| Pfam | PF01502. PRA-CH. 1 hit. [Graphical view] | ||||||||||||
| ProDom | PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | HIS3_METTH | ||||||||
| Accession | Primary (citable) accession number: O26347 | ||||||||
| Entry history |
| ||||||||
| 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