Reviewed,
UniProtKB/Swiss-Prot A0JVK2 (RISB_ARTS2)
Last modified
November 3, 2009.
Version 23.
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 | Arthrobacter sp. (strain FB24) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 290399 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Micrococcineae › Micrococcaceae › Arthrobacter |
Protein attributes
| Sequence length | 161 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| 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; 5-amino-6-(D-ribitylamino)uracil and riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine: step 1/1. HAMAP MF_00178 |
| Sequence similarities | Belongs to the DMRL synthase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Riboflavin biosynthesis |
| Molecular function | Transferase |
| Technical term | Complete proteome |
| 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 – 161 | 161 | 6,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178 | PRO_1000077225 | |||
Sequences
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References
| [1] | "Complete sequence of chromosome 1 of Arthrobacter sp. FB24." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Thompson S., Brettin T., Bruce D., Han C., Tapia R., Gilna P. Richardson P.Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000454 Genomic DNA. Translation: ABK03072.1. | |
| RefSeq | YP_831172.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A0JVK2. |
Genome annotation databases | |
| GeneID | 4445784. |
| GenomeReviews | Gene locus Arth_1678 in contig CP000454_GR. |
| KEGG | art:Arth_1678. |
| TIGR | Arth_1678. |
Phylogenomic databases | |
| OMA | TIHFEIV. |
Family and domain databases | |
| HAMAP | MF_00178. [Tree] |
| InterPro | IPR002180. DMRL_synthase. [Graphical view] |
| PANTHER | PTHR21058. DMRL_synthase. 1 hit. |
| Pfam | PF00885. DMRL_synthase. 1 hit. [Graphical view] |
| ProDom | PD003664. DMRL_synthase. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR00114. lumazine-synth. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | RISB_ARTS2 | ||||||||
| Accession | Primary (citable) accession number: A0JVK2 | ||||||||
| 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 |

Clusters with


