Q81MB5 (RISB_BACAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 62.
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: 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 | ||||
| Taxonomic identifier | 1392 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 153 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | riboflavin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | riboflavin synthase complex Inferred from electronic annotation. Source: InterPro |
| Molecular function | riboflavin synthase activity Inferred from electronic annotation. Source: EC |
| 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 | ||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 14 – 19 | 6 | ||||||||||||||||||||||||||||
| Helix | 23 – 39 | 17 | ||||||||||||||||||||||||||||
| Beta strand | 46 – 54 | 9 | ||||||||||||||||||||||||||||
| Helix | 55 – 57 | 3 | ||||||||||||||||||||||||||||
| Helix | 58 – 66 | 9 | ||||||||||||||||||||||||||||
| Turn | 67 – 69 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 72 – 81 | 10 | ||||||||||||||||||||||||||||
| Helix | 87 – 98 | 12 | ||||||||||||||||||||||||||||
| Turn | 99 – 101 | 3 | ||||||||||||||||||||||||||||
| Helix | 102 – 104 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 110 – 118 | 9 | ||||||||||||||||||||||||||||
| Helix | 120 – 126 | 7 | ||||||||||||||||||||||||||||
| Helix | 134 – 146 | 13 | ||||||||||||||||||||||||||||
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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE016879 Genomic DNA. Translation: AAP28053.1. AE017334 Genomic DNA. Translation: AAT33455.1. AE017225 Genomic DNA. Translation: AAT56322.1. | ||||||||||||||||||||||||
| RefSeq | NP_846567.1. NC_003997.3. YP_020980.1. NC_007530.2. YP_030271.1. NC_005945.1. | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||
| ProteinModelPortal | Q81MB5. | ||||||||||||||||||||||||
| SMR | Q81MB5. Positions 2-152. | ||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| EnsemblBacteria | EBBACT00000008556; EBBACP00000008312; EBBACG00000008548. EBBACT00000015171; EBBACP00000014792; EBBACG00000015163. EBBACT00000022183; EBBACP00000021668; EBBACG00000022174. | ||||||||||||||||||||||||
| 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:BA_4334. bar:GBAA_4334. bat:BAS4021. | ||||||||||||||||||||||||
| TIGR | BA_4334. GBAA_4334. | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| GeneTree | EBGT00050000002577. | ||||||||||||||||||||||||
| HOGENOM | HBG311126. | ||||||||||||||||||||||||
| OMA | DYVCNEA. | ||||||||||||||||||||||||
| ProtClustDB | PRK00061. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| BioCyc | BANT260799:BAS4021-MONOMER. BANT261594:GBAA4334-MONOMER. | ||||||||||||||||||||||||
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. | ||||||||||||||||||||||||
| KO | K00794. | ||||||||||||||||||||||||
| PANTHER | PTHR21058. DMRL_synthase. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00885. DMRL_synthase. 1 hit. [Graphical view] | ||||||||||||||||||||||||
| SUPFAM | SSF52121. DMRL_synthase. 1 hit. | ||||||||||||||||||||||||
| 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 program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

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