Reviewed,
UniProtKB/Swiss-Prot P0A5H9 (GGPPS_MYCBO)
Last modified
February 9, 2010.
Version 33.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Probable geranylgeranyl pyrophosphate synthetase Short name=GGPP synthetase Short name=GGPPSase Alternative name(s): Geranylgeranyl diphosphate synthase Including the following 3 domains: 1- Recommended name: Dimethylallyltranstransferase EC=2.5.1.1 2- Recommended name: Geranyltranstransferase EC=2.5.1.10 3- Recommended name: Farnesyltranstransferase EC=2.5.1.29 | ||
| Gene names |
| ||
| Organism | Mycobacterium bovis [Complete proteome] [HAMAP] | ||
| Taxonomic identifier | 1765 [NCBI] | ||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Catalyzes the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate which is a precursor of the ether-linked lipids. |
| Catalytic activity | Dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + geranyl diphosphate. Geranyl diphosphate + isopentenyl diphosphate = diphosphate + trans,trans-farnesyl diphosphate. Trans,trans-farnesyl diphosphate + isopentenyl diphosphate = diphosphate + geranylgeranyl diphosphate. |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Pathway | |
| Sequence similarities | Belongs to the FPP/GGPP synthetase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Isoprene biosynthesis Lipid synthesis |
| Ligand | Magnesium Metal-binding |
| Molecular function | Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | isoprenoid biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | dimethylallyltranstransferase activity Inferred from electronic annotation. Source: EC farnesyltranstransferase activityInferred from electronic annotation. Source: EC geranyltranstransferase activityInferred from electronic annotation. Source: EC magnesium 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 – 359 | 359 | Probable geranylgeranyl pyrophosphate synthetase | PRO_0000123969 | |||||
Sites | |||||||||
| Metal binding | 112 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 242 | 1 | Magnesium 3 By similarity | ||||||
| Binding site | 73 | 1 | Isopentenyl diphosphate By similarity | ||||||
| Binding site | 76 | 1 | Isopentenyl diphosphate By similarity | ||||||
| Binding site | 105 | 1 | Isopentenyl diphosphate By similarity | ||||||
| Binding site | 121 | 1 | Dimethylallyl diphosphate By similarity | ||||||
| Binding site | 122 | 1 | Isopentenyl diphosphate By similarity | ||||||
| Binding site | 201 | 1 | Dimethylallyl diphosphate By similarity | ||||||
| Binding site | 202 | 1 | Dimethylallyl diphosphate By similarity | ||||||
| Binding site | 239 | 1 | Dimethylallyl diphosphate By similarity | ||||||
| Binding site | 256 | 1 | Dimethylallyl diphosphate By similarity | ||||||
| Binding site | 266 | 1 | Dimethylallyl diphosphate By similarity | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium bovis." Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J. Hewinson R.G.Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003) [PubMed: 12788972] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-935 / AF2122/97. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX248346 Genomic DNA. Translation: CAD95619.1. |
| RefSeq | NP_857072.1. |
3D structure databases | |
| SMR | P0A5H9. Positions 32-358. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1090991. |
| KEGG | mbo:Mb3431c. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG732667. |
| OMA | RMAPLES. |
Enzyme and pathway databases | |
| BioCyc | MBOV233413:MB3431C-MONOMER. |
| BRENDA | 2.5.1.1. 3091. 2.5.1.10. 3091. 2.5.1.29. 3091. |
Family and domain databases | |
| InterPro | IPR000092. Polyprenyl_synt. IPR017446. Polyprenyl_synth-rel. IPR008949. Terpenoid_synth. [Graphical view] |
| Gene3D | G3DSA:1.10.600.10. Terpenoid_synth. 1 hit. |
| PANTHER | PTHR12001. Polyprenyl_synt. 1 hit. |
| Pfam | PF00348. polyprenyl_synt. 1 hit. [Graphical view] |
| PROSITE | PS00723. POLYPRENYL_SYNTHET_1. 1 hit. PS00444. POLYPRENYL_SYNTHET_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GGPPS_MYCBO | ||||||||
| Accession | Primary (citable) accession number: P0A5H9 Secondary accession number(s): Q50727 | ||||||||
| Entry history |
| ||||||||
| 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


