Reviewed,
UniProtKB/Swiss-Prot Q8A7Z7 (HIS2_BACTN)
Last modified
February 9, 2010.
Version 49.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Histidine biosynthesis bifunctional protein hisIE Including the following 2 domains: 1- Recommended name: Phosphoribosyl-AMP cyclohydrolase Short name=PRA-CH EC=3.5.4.19 2- Recommended name: Phosphoribosyl-ATP pyrophosphatase Short name=PRA-PH EC=3.6.1.31 | ||||||
| Gene names |
| ||||||
| Organism | Bacteroides thetaiotaomicron [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 818 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Bacteroidetes › Bacteroidia › Bacteroidales › Bacteroidaceae › Bacteroides |
Protein attributes
| Sequence length | 203 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Catalytic activity | 1-(5-phosphoribosyl)-ATP + H2O = 1-(5-phosphoribosyl)-AMP + diphosphate. HAMAP MF_01019 1-(5-phosphoribosyl)-AMP + H2O = 1-(5-phosphoribosyl)-5-((5-phosphoribosylamino)methylideneamino)imidazole-4-carboxamide. HAMAP MF_01019 |
| Pathway | Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. HAMAP MF_01019 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_01019. |
| Sequence similarities | In the N-terminal section; belongs to the PRA-CH family. In the C-terminal section; 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 | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | histidine biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosyl-AMP cyclohydrolase activityInferred from electronic annotation. Source: HAMAP phosphoribosyl-ATP diphosphatase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||
Molecule processing | ||||||||
|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 203 | 203 | Histidine biosynthesis bifunctional protein hisIE HAMAP MF_01019 | PRO_0000136404 | ||||
Regions | ||||||||
| Region | 1 – 108 | 108 | Phosphoribosyl-AMP cyclohydrolase HAMAP MF_01019 | |||||
| Region | 109 – 203 | 95 | Phosphoribosyl-ATP pyrophosphohydrolase HAMAP MF_01019 | |||||
Sequences
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References
| [1] | "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis." Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I. Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE015928 Genomic DNA. Translation: AAO76484.1. |
| RefSeq | NP_810290.1. |
3D structure databases | |
| SMR | Q8A7Z7. Positions 1-101, 108-197. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1072959. |
| GenomeReviews | Gene locus BT_1377 in contig AE015928_GR. |
| KEGG | bth:BT_1377. |
| NMPDR | fig|226186.1.peg.1377. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG294308. |
| OMA | VHYWSRS. |
| PhylomeDB | Q8A7Z7. |
Enzyme and pathway databases | |
| BioCyc | BTHE226186:BT_1377-MONOMER. |
| BRENDA | 3.5.4.19. 21018. 3.6.1.31. 21018. |
Family and domain databases | |
| HAMAP | MF_01019. HisIE. [Tree] |
| InterPro | IPR002496. PRA_CycHdrlase. IPR008179. PRib-ATP_pyrophosphohydrolase. IPR021130. PRib-ATP_pyroPHydrolase-like. [Graphical view] |
| Pfam | PF01502. PRA-CH. 1 hit. PF01503. PRA-PH. 1 hit. [Graphical view] |
| ProDom | PD002610. PRA_CycHdrlase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR03188. histidine_hisI. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | HIS2_BACTN | ||||||||
| Accession | Primary (citable) accession number: Q8A7Z7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


