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B2SAX4 (B2SAX4_BRUA1) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
6,7-dimethyl-8-ribityllumazine synthase 1 HAMAP MF_00178

Short name=DMRL synthase 1 HAMAP MF_00178
Short name=Lumazine synthase 1 HAMAP MF_00178
EC=2.5.1.9 HAMAP MF_00178
Alternative name(s):
Riboflavin synthase beta chain 1 HAMAP MF_00178
Gene names
Name:ribH1 HAMAP MF_00178
Ordered Locus Names:BAbS19_II05140
OrganismBrucella abortus (strain S19) [Complete proteome] [HAMAP]
Taxonomic identifier430066 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Protein existenceInferred 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. 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. HAMAP MF_00178

Ontologies

Keywords
   Biological processRiboflavin biosynthesis HAMAP MF_00178
   Molecular functionTransferase HAMAP MF_00178
   Technical termComplete 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...

Sequences

Sequence LengthMass (Da)Tools
B2SAX4 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: EE59C2C815E53A2B

FASTA15817,356
        10         20         30         40         50         60 
MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD VPGAYEIPLH 

        70         80         90        100        110        120 
AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ VQLETEVPVL SVVLTPHHFH 

       130        140        150 
ESKEHHDFFH AHFKVKGVEA AHAALQIVSE RSRIAALV 

« Hide

References

[1]"Genome sequence of Brucella abortus vaccine strain S19 compared to virulent strains yields candidate virulence genes."
Crasta O.R., Folkerts O., Fei Z., Mane S.P., Evans C., Martino-Catt S., Bricker B., Yu G., Du L., Sobral B.W.
PLoS ONE 3:E2193-E2193(2008) [PubMed: 18478107] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000888 Genomic DNA. Translation: ACD74011.1.
RefSeqYP_001932457.1. NC_010740.1.

3D structure databases

ProteinModelPortalB2SAX4.
SMRB2SAX4. Positions 8-157.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2SAX4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6326353.
GenomeReviewsGene locus BAbS19_II05140 in contig CP000888_GR.
KEGGbmc:BAbS19_II05140.
PATRIC17815526. VBIBruAbo38055_0567.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG311126.
OMARRYTAIV.
ProtClustDBPRK12419.

Family and domain databases

HAMAPMF_00178. Lumazine_synth.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
KOK00794.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
ProtoNetSearch...

Entry information

Entry nameB2SAX4_BRUA1
AccessionPrimary (citable) accession number: B2SAX4
Entry history
Integrated into UniProtKB/TrEMBL: July 1, 2008
Last sequence update: July 1, 2008
Last modified: December 14, 2011
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)