Reviewed,
UniProtKB/Swiss-Prot Q81MB5 (RISB_BACAN)
Last modified
November 3, 2009.
Version 43.
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 | Bacillus anthracis [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 153 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 – 153 | 153 | 6,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178 | PRO_0000134710 | |||
Sequences
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References
| [1] | "The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria." Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. Fraser C.M.Nature 423:81-86(2003) [PubMed: 12721629] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames / isolate Porton. |
| [2] | "Bacillus anthracis comparative genomics." Ravel J., Rasko D.A., Shumway M.F., Jiang L., Cer R.Z., Federova N.B., Wilson M., Stanley S., Decker S., Read T.D., Salzberg S.L., Fraser C.M. Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Ames ancestor. |
| [3] | "Complete genome sequence of Bacillus anthracis Sterne." Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H. Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Sterne. |
Cross-references
Sequence databases | |
|---|---|
| AE016879 Genomic DNA. Translation: AAP28053.1. AE017334 Genomic DNA. Translation: AAT33455.1. AE017225 Genomic DNA. Translation: AAT56322.1. | |
| RefSeq | NP_846567.1. YP_020980.1. YP_030271.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1RVV based on UniProtKB P11998. |
| SMR | Q81MB5. Positions 2-152. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1087551. 2815209. 2850962. |
| GenomeReviews | Gene locus BA_4334 in contig AE016879_GR. Gene locus BAS4021 in contig AE017225_GR. Gene locus GBAA_4334 in contig AE017334_GR. |
| KEGG | ban:BA4334. bar:GBAA4334. bat:BAS4021. |
| TIGR | BA_4334. GBAA_4334. |
Phylogenomic databases | |
| HOGENOM | Q81MB5. |
| OMA | LTTDTMQ. |
Enzyme and pathway databases | |
| BioCyc | BANT260799:BAS4021-MON. BANT261594:GBAA4334-MON. |
| BRENDA | 2.5.1.9. 267517. |
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] |
| 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_BACAN | ||||||||
| Accession | Primary (citable) accession number: Q81MB5 Secondary accession number(s): Q6HTR7, Q6KN05 | ||||||||
| 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


