Reviewed,
UniProtKB/Swiss-Prot B7J444 (RISB_ACIF2)
Last modified
September 22, 2009.
Version 9.
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 |
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| Organism | Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / NCIB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243159 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Acidithiobacillales › Acidithiobacillaceae › Acidithiobacillus |
Protein attributes
| Sequence length | 154 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 – 154 | 154 | 6,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178 | PRO_1000195448 | |||
Sequences
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References
| [1] | "Acidithiobacillus ferrooxidans metabolism: from genome sequence to industrial applications." Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R. II, Eisen J.A., Holmes D.S. BMC Genomics 9:597-597(2008) [PubMed: 19077236] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP001219 Genomic DNA. Translation: ACK78084.1. | |
| RefSeq | YP_002424807.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 7136207. |
| GenomeReviews | Gene locus AFE_0300 in contig CP001219_GR. |
| KEGG | afr:AFE_0300. |
Organism-specific databases | |
| CMR | Search... |
Family and domain databases | |
| HAMAP | MF_00178. [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_ACIF2 | ||||||||
| Accession | Primary (citable) accession number: B7J444 | ||||||||
| 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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