Reviewed,
UniProtKB/Swiss-Prot O25664 (ISPDF_HELPY)
Last modified
November 3, 2009.
Version 61.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Bifunctional enzyme ispD/ispF Including the following 2 domains: 1- Recommended name: 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase EC=2.7.7.60 Alternative name(s): 4-diphosphocytidyl-2C-methyl-D-erythritol synthase MEP cytidylyltransferase Short name=MCT 2- Recommended name: 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase Short name=MECPS Short name=MECDP-synthase EC=4.6.1.12 | ||||
| Gene names |
| ||||
| Organism | Helicobacter pylori (Campylobacter pylori) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 210 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter |
Protein attributes
| Sequence length | 406 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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. |
| 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: HAMAP |
| Molecular function | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity Inferred from electronic annotation. Source: HAMAP 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activityInferred from electronic annotation. Source: HAMAP 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_0000075669 | |||||
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 the gastric pathogen Helicobacter pylori." Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J. Venter J.C.Nature 388:539-547(1997) [PubMed: 9252185] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700392 / 26695. |
Cross-references
Sequence databases | |
|---|---|
| AE000511 Genomic DNA. Translation: AAD08064.1. | |
| PIR | D64647. |
| RefSeq | NP_207810.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GX1 based on UniProtKB P36663. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 899555. |
| GenomeReviews | Gene locus HP_1020 in contig AE000511_GR. |
| KEGG | hpy:HP1020. |
| NMPDR | fig|85962.1.peg.1007. |
| TIGR | HP_1020. |
Phylogenomic databases | |
| HOGENOM | O25664. |
| OMA | GGDIGEW. |
Enzyme and pathway databases | |
| BRENDA | 2.7.7.60. 1131. 4.6.1.12. 1131. |
Family and domain databases | |
| HAMAP | MF_01520. [Tree] |
| InterPro | IPR001228. ISPD_synthase. IPR018294. ISPD_synthase_CS. IPR003526. MECDP_synthase_core. IPR020555. MECDP_synthase_CS. [Graphical view] |
| Gene3D | G3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit. |
| Pfam | PF01128. IspD. 1 hit. PF02542. YgbB. 1 hit. [Graphical view] |
| 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_HELPY | ||||||||
| Accession | Primary (citable) accession number: O25664 | ||||||||
| 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
| Helicobacter pylori Helicobacter pylori (strain 26695): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


