Reviewed,
UniProtKB/Swiss-Prot Q57DY1 (RISB1_BRUAB)
Last modified
November 25, 2008.
Version 31.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: 6,7-dimethyl-8-ribityllumazine synthase 1 Short name=DMRL synthase 1 Short name=Lumazine synthase 1 EC=2.5.1.9 Alternative name(s): Riboflavin synthase 1 beta chain | ||||||
| Gene names |
| ||||||
| Organism | Brucella abortus [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 235 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 157 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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. |
| Catalytic activity | 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. |
| Pathway | |
| Sequence similarities | Belongs to the DMRL synthase family. |
Ontologies
Keywords | |
|---|---|
| Biological process | Riboflavin biosynthesis |
| Molecular function | Transferase |
| Technical term | 3D-structure 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 – 157 | 157 | 6,7-dimethyl-8-ribityllumazine synthase 1 | PRO_0000134724 | ||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||
| Beta strand | 14 – 20 | 7 | ||||||||||||||||||||||||||||
| Helix | 24 – 41 | 18 | ||||||||||||||||||||||||||||
| Beta strand | 44 – 52 | 9 | ||||||||||||||||||||||||||||
| Helix | 53 – 55 | 3 | ||||||||||||||||||||||||||||
| Helix | 56 – 67 | 12 | ||||||||||||||||||||||||||||
| Turn | 68 – 70 | 3 | ||||||||||||||||||||||||||||
| Beta strand | 75 – 84 | 10 | ||||||||||||||||||||||||||||
| Beta strand | 87 – 91 | 5 | ||||||||||||||||||||||||||||
| Helix | 92 – 108 | 17 | ||||||||||||||||||||||||||||
| Beta strand | 113 – 122 | 10 | ||||||||||||||||||||||||||||
| Helix | 123 – 130 | 8 | ||||||||||||||||||||||||||||
| Turn | 132 – 135 | 4 | ||||||||||||||||||||||||||||
| Helix | 137 – 155 | 19 | ||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis." Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C. J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 9-941 / Biovar 1. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AE017223 Genomic DNA. Translation: AAX74153.1. | |||||||||||||||||||
| RefSeq | YP_221514.1. | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| |||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| GeneID | 3339926. | ||||||||||||||||||
| GenomeReviews | Gene locus BruAb1_0785 in contig AE017223_GR. | ||||||||||||||||||
| KEGG | bmb:BruAb1_0785. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CMR | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| HOGENOM | Q57DY1. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| BioCyc | BABO262698:BRUAB1_0785-MON. | ||||||||||||||||||
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 | RISB1_BRUAB | ||||||||
| Accession | Primary (citable) accession number: Q57DY1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Brucella abortus strain 9-941 Brucella abortus (strain 9-941): entries and gene names |
| 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 |

Clusters with


