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Reviewed, UniProtKB/Swiss-Prot Q57DY1 (RISB1_BRUAB)

Last modified November 25, 2008. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
Name: ribH1
Synonyms: ribH, ribH-1
Ordered Locus Names: BruAb1_0785
OrganismBrucella abortus [Complete proteome] [HAMAP]
Taxonomic identifier235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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

Cofactor biosynthesis; riboflavin biosynthesis; 6,7-dimethyl-8-(1-D-ribityl)lumazine and riboflavin from 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine: step 1/1.

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

Keywords

   Biological processRiboflavin biosynthesis
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome

Gene Ontology (GO)

   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1571576,7-dimethyl-8-ribityllumazine synthase 1
PRO_0000134724

Secondary structure

...................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q57DY1-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 657DE105F885A875

FASTA15716,791
        10         20         30         40         50         60 
MEFLMSKHEA DAPHLLIVEA RFYDDLADAL LDGAKAALDE AGATYDVVTV PGALEIPATI 

        70         80         90        100        110        120 
SFALDGADNG GTEYDGFVAL GTVIRGETYH FDIVSNESCR ALTDLSVEES IAIGNGILTV 

       130        140        150 
ENEEQAWVHA RREDKDKGGF AARAALTMIG LRKKFGA 

« Hide

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.
RefSeqYP_221514.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2F59X-ray2.30A/B/C/D/E1-157[»]
2I0FX-ray2.22A/B/C/D/E1-157[»]
ModBaseSearch...

Genome annotation databases

GeneID3339926.
GenomeReviewsGene locus BruAb1_0785 in contig AE017223_GR.
KEGGbmb:BruAb1_0785.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ57DY1.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_0785-MON.

Family and domain databases

HAMAPMF_00178.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
ProDomPD003664. DMRL_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00114. lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB1_BRUAB
AccessionPrimary (citable) accession number: Q57DY1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: May 10, 2005
Last modified: November 25, 2008
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents