Q72B63 (RIBB_DESVH) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 49.
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: 3,4-dihydroxy-2-butanone 4-phosphate synthase Short name=DHBP synthase EC=4.1.99.12 | ||||
| Gene names |
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| Organism | Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / NCIMB 8303) | ||||
| Taxonomic identifier | 882 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Deltaproteobacteria › Desulfovibrionales › Desulfovibrionaceae › Desulfovibrio |
Protein attributes
| Sequence length | 214 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. HAMAP MF_00180 |
| Catalytic activity | D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_00180 |
| Cofactor | Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity. |
| Pathway | Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180 |
| Subunit structure | Homodimer By similarity. HAMAP MF_00180 |
| Sequence similarities | Belongs to the DHBP synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Riboflavin biosynthesis |
| Ligand | Magnesium Manganese Metal-binding |
| Molecular function | Lyase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | 3,4-dihydroxy-2-butanone-4-phosphate synthase activity Inferred 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 – 214 | 214 | 3,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180 | PRO_1000040603 | |||||
Regions | |||||||||
| Region | 37 – 38 | 2 | Substrate binding By similarity | ||||||
| Region | 150 – 154 | 5 | Substrate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 38 | 1 | Magnesium or manganese 1 By similarity | ||||||
| Metal binding | 38 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Metal binding | 153 | 1 | Magnesium or manganese 2 By similarity | ||||||
| Binding site | 42 | 1 | Substrate By similarity | ||||||
| Binding site | 174 | 1 | Substrate By similarity | ||||||
| Site | 136 | 1 | Essential for catalytic activity By similarity | ||||||
| Site | 174 | 1 | Essential for catalytic activity By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the anaerobic, sulfate-reducing bacterium Desulfovibrio vulgaris Hildenborough." Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T., Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Fouts D.E. Fraser C.M.Nat. Biotechnol. 22:554-559(2004) [PubMed: 15077118] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Hildenborough / ATCC 29579 / NCIMB 8303. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017285 Genomic DNA. Translation: AAS96252.1. |
| RefSeq | YP_010993.1. NC_002937.3. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1G58 based on UniProtKB P0A7J0. |
| ProteinModelPortal | Q72B63. |
| SMR | Q72B63. Positions 1-210. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q72B63. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2794282. |
| GenomeReviews | Gene locus DVU_1775 in contig AE017285_GR. |
| KEGG | dvu:DVU1775. |
| NMPDR | fig|882.1.peg.1768. |
| PATRIC | 32063314. VBIDesVul119526_1630. |
| TIGR | DVU_1775. |
Phylogenomic databases | |
| eggNOG | COG0108. |
| HOGENOM | HBG735778. |
| OMA | GDMIFAA. |
| PhylomeDB | Q72B63. |
| ProtClustDB | PRK03353. |
Enzyme and pathway databases | |
| BioCyc | DVUL882:DVU_1775-MONOMER. |
Family and domain databases | |
| HAMAP | MF_00180. RibB. [Tree] |
| InterPro | IPR017945. DHBP_synth_RibB-like_a/b_dom. IPR000422. DHBP_synthase_RibB. [Graphical view] |
| Gene3D | G3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit. |
| KO | K02858. |
| Pfam | PF00926. DHBP_synthase. 1 hit. [Graphical view] |
| SUPFAM | SSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit. |
| TIGRFAMs | TIGR00506. RibB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RIBB_DESVH | ||||||||
| Accession | Primary (citable) accession number: Q72B63 | ||||||||
| 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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