Q8YGH2 (RISB1_BRUME) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 58.
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 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 melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 224914 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Brucella |
Protein attributes
| Sequence length | 157 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 |
| 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 – 157 | 157 | 6,7-dimethyl-8-ribityllumazine synthase 1 HAMAP MF_00178 | PRO_0000134726 | |||||||||||||||||||||||||
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 | |||||||||||||||||||||||||||
| Helix | 90 – 108 | 19 | |||||||||||||||||||||||||||
| Beta strand | 112 – 122 | 11 | |||||||||||||||||||||||||||
| Helix | 123 – 130 | 8 | |||||||||||||||||||||||||||
| Turn | 132 – 135 | 4 | |||||||||||||||||||||||||||
| Helix | 137 – 154 | 18 | |||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "The genome sequence of the facultative intracellular pathogen Brucella melitensis." DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T., Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G., Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E., Selkov E. Overbeek R.Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002) [PubMed: 11756688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 16M / ATCC 23456 / NCTC 10094. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | AE008917 Genomic DNA. Translation: AAL52368.1. | ||||||||||||
| PIR | AE3400. | ||||||||||||
| RefSeq | NP_540104.1. NC_003317.1. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q8YGH2. | ||||||||||||
| SMR | Q8YGH2. Positions 11-157. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| GeneID | 1196898. | ||||||||||||
| GenomeReviews | Gene locus BMEI1187 in contig AE008917_GR. | ||||||||||||
| KEGG | bme:BMEI1187. | ||||||||||||
| NMPDR | fig|224914.1.peg.1186. | ||||||||||||
| PATRIC | 17797634. VBIBruMel146950_0635. | ||||||||||||
Organism-specific databases | |||||||||||||
| CMR | Search... | ||||||||||||
Phylogenomic databases | |||||||||||||
| HOGENOM | HBG311126. | ||||||||||||
| OMA | SSRALMD. | ||||||||||||
| PhylomeDB | Q8YGH2. | ||||||||||||
| ProtClustDB | PRK00061. | ||||||||||||
Enzyme and pathway databases | |||||||||||||
| BioCyc | BMEL224914:BMEI1187-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 | RISB1_BRUME | ||||||||
| Accession | Primary (citable) accession number: Q8YGH2 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Brucella melitensis Brucella melitensis (strain 16M): 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