A0RN28 (ISPDF_CAMFF) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 37.
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 | Campylobacter fetus subsp. fetus (strain 82-40) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 360106 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 372 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 – 372 | 372 | Bifunctional enzyme IspD/IspF HAMAP MF_01520 | PRO_0000296741 | |||||
Regions | |||||||||
| Region | 1 – 210 | 210 | 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520 | ||||||
| Region | 211 – 372 | 162 | 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520 | ||||||
Sites | |||||||||
| Metal binding | 217 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 219 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 251 | 1 | Divalent metal cation By similarity | ||||||
| Site | 16 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 23 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 139 | 1 | Positions MEP for the nucleophilic attack By similarity | ||||||
| Site | 191 | 1 | Positions MEP for the nucleophilic attack By similarity | ||||||
| Site | 243 | 1 | Transition state stabilizer By similarity | ||||||
| Site | 342 | 1 | Transition state stabilizer By similarity | ||||||
Sequences
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References
| [1] | "Sequence of Campylobacter fetus subsp. fetus 82-40." Fouts D.E., Nelson K.E. Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 82-40. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000487 Genomic DNA. Translation: ABK81838.1. |
| RefSeq | YP_891611.1. NC_008599.1. |
3D structure databases | |
| ProteinModelPortal | A0RN28. |
| SMR | A0RN28. Positions 3-370. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A0RN28. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 4537765. |
| GenomeReviews | Gene locus CFF8240_0409 in contig CP000487_GR. |
| KEGG | cff:CFF8240_0409. |
| NMPDR | fig|360106.5.peg.396. |
| PATRIC | 20035344. VBICamFet25865_0404. |
| TIGR | CFF8240_0409. |
Phylogenomic databases | |
| eggNOG | COG1211. |
| HOGENOM | HBG672839. |
| OMA | IVLIHDA. |
| ProtClustDB | PRK09382. |
Enzyme and pathway databases | |
| BioCyc | CFET360106:CFF8240_0409-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01520. IspDF. [Tree] |
| InterPro | IPR023423. IpsF_dom. IPR001228. ISPD_synthase. 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. False negative. PS01350. ISPF. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ISPDF_CAMFF | ||||||||
| Accession | Primary (citable) accession number: A0RN28 | ||||||||
| 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 |

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