Reviewed,
UniProtKB/Swiss-Prot Q8GLK5 (RISB_AQUPY)
Last modified
February 9, 2010.
Version 29.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 6,7-dimethyl-8-ribityllumazine synthase Short name=DMRL synthase Short name=Lumazine synthase EC=2.5.1.9 Alternative name(s): Riboflavin synthase beta chain | ||
| Gene names |
| ||
| Organism | Aquifex pyrophilus | ||
| Taxonomic identifier | 2714 [NCBI] | ||
| Taxonomic lineage | Bacteria › Aquificae › Aquificales › Aquificaceae › Aquifex |
Protein attributes
| Sequence length | 154 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine By similarity. HAMAP MF_00178 |
| Catalytic activity | 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. HAMAP MF_00178 |
| Pathway | Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2. HAMAP MF_00178 |
| Sequence similarities | Belongs to the DMRL synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Riboflavin biosynthesis |
| Molecular function | Transferase |
| Gene Ontology (GO) | |
| Biological process | riboflavin biosynthetic process Inferred from electronic annotation. Source: HAMAP |
| Cellular component | riboflavin synthase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | riboflavin synthase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 154 | 154 | 6,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178 | PRO_0000134709 | |||
Sequences
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References
| [1] | "Cloning, expression, and biochemical characterization of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthase from the hyperthermophilic bacterium Aquifex pyrophilus." Shulami S., Yaniv O., Rabkin E., Shoham Y., Baasov T. Extremophiles 7:471-481(2003) [PubMed: 12955602] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AY135660 Genomic DNA. Translation: AAN12292.1. |
3D structure databases | |
| SMR | Q8GLK5. Positions 1-154. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 2.5.1.9. 271525. |
Family and domain databases | |
| HAMAP | MF_00178. Lumazine_synth. [Tree] |
| InterPro | IPR002180. DMRL_synthase. [Graphical view] |
| Gene3D | G3DSA:3.40.50.960. DMRL_synthase. 1 hit. |
| PANTHER | PTHR21058. DMRL_synthase. 1 hit. |
| Pfam | PF00885. DMRL_synthase. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00114. lumazine-synth. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RISB_AQUPY | ||||||||
| Accession | Primary (citable) accession number: Q8GLK5 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

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