Q1CU78 (ISPDF_HELPH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 41.
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: Bifunctional enzyme IspD/IspF Including the following 2 domains: | ||||
| Gene names |
| ||||
| Organism | Helicobacter pylori (strain HPAG1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 357544 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Protein attributes
| Sequence length | 406 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (IspF) By similarity. HAMAP MF_01520 |
| Catalytic activity | CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_01520 2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_01520 |
| Cofactor | Divalent metal cations By similarity. HAMAP MF_01520 |
| Pathway | Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520 |
| Sequence similarities | In the N-terminal section; belongs to the IspD family. In the C-terminal section; belongs to the IspF family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Isoprene biosynthesis |
| Ligand | Metal-binding |
| Molecular function | Lyase Nucleotidyltransferase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | terpenoid biosynthetic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: EC 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 406 | 406 | Bifunctional enzyme IspD/IspF HAMAP MF_01520 | PRO_0000296747 | |||||
Regions | |||||||||
| Region | 1 – 247 | 247 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520 | ||||||
| Region | 248 – 406 | 159 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520 | ||||||
Sites | |||||||||
| Metal binding | 254 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 256 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 288 | 1 | Divalent metal cation By similarity | ||||||
| Site | 48 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 55 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 175 | 1 | Positions MEP for the nucleophilic attack By similarity | ||||||
| Site | 227 | 1 | Positions MEP for the nucleophilic attack By similarity | ||||||
| Site | 280 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 379 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of a chronic atrophic gastritis Helicobacter pylori strain: evolution during disease progression." Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A., Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G., Gordon J.I. Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006) [PubMed: 16788065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: HPAG1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000241 Genomic DNA. Translation: ABF84494.1. |
| RefSeq | YP_627168.1. NC_008086.1. |
3D structure databases | |
| ProteinModelPortal | Q1CU78. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q1CU78. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4098804. |
| GenomeReviews | Gene locus HPAG1_0427 in contig CP000241_GR. |
| KEGG | hpa:HPAG1_0427. |
| PATRIC | 20602195. VBIHelPyl56048_0446. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1211. |
| HOGENOM | HBG672839. |
| OMA | GGDIGEW. |
| ProtClustDB | PRK09382. |
Enzyme and pathway databases | |
| BioCyc | HPYL357544:HPAG1_0427-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01520. IspDF. [Tree] |
| InterPro | IPR023423. IpsF_dom. IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase. IPR020555. MECDP_synthase_CS. [Graphical view] |
| Gene3D | G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit. |
| KO | K12506. |
| Pfam | PF01128. IspD. 1 hit. PF02542. YgbB. 1 hit. [Graphical view] |
| SUPFAM | SSF69765. YgbB_synth. 1 hit. |
| TIGRFAMs | TIGR00453. IspD. 1 hit. TIGR00151. IspF. 1 hit. |
| PROSITE | PS01295. ISPD. 1 hit. PS01350. ISPF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ISPDF_HELPH | ||||||||
| Accession | Primary (citable) accession number: Q1CU78 | ||||||||
| 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