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Q39V66 (RISB_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

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

Short name=DMRL synthase
Short name=LS
Short name=Lumazine synthase
EC=2.5.1.78
Gene names
Name:ribH
Ordered Locus Names:Gmet_1627
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesGeobacteraceaeGeobacter

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin By similarity. HAMAP-Rule MF_00178

Catalytic activity

1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate. HAMAP-Rule MF_00178

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. HAMAP-Rule MF_00178

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6,7-dimethyl-8-ribityllumazine synthase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1551556,7-dimethyl-8-ribityllumazine synthase HAMAP-Rule MF_00178
PRO_1000040424

Regions

Region57 – 5935-amino-6-(D-ribitylamino)uracil binding By similarity
Region81 – 8335-amino-6-(D-ribitylamino)uracil binding By similarity
Region86 – 8721-deoxy-L-glycero-tetrulose 4-phosphate binding By similarity

Sites

Active site891Proton donor Potential
Binding site2315-amino-6-(D-ribitylamino)uracil By similarity
Binding site11415-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygen By similarity
Binding site12811-deoxy-L-glycero-tetrulose 4-phosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q39V66 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 53573BDD63670235

FASTA15516,462
        10         20         30         40         50         60 
MPRFIEGKLD ATGLKFGIIV GRFNSFIGER LLEGALDALV RNGADEATID VARVPGAFEI 

        70         80         90        100        110        120 
PLTAKKMAQT GSYDAIICLG AVIRGSTPHF DYVAAEVSKG VAHVSLETGV PVSFGVLTTD 

       130        140        150 
TIEQAVERAG TKAGNKGFDA AMTAIETVRV FREFR 

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000148 Genomic DNA. Translation: ABB31858.1.
RefSeqYP_006720594.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39V66.
SMRQ39V66. Positions 5-154.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING269799.Gmet_1627.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB31858; ABB31858; Gmet_1627.
GeneID3739366.
KEGGgme:Gmet_1627.
PATRIC22002478. VBIGeoMet55070_1665.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0054.
HOGENOMHOG000229249.
KOK00794.
OMAIEMANLS.
OrthoDBEOG6RC3WC.

Enzyme and pathway databases

BioCycGMET269799:GHNY-1652-MONOMER.
UniPathwayUPA00275; UER00404.

Family and domain databases

Gene3D3.40.50.960. 1 hit.
HAMAPMF_00178. Lumazine_synth.
InterProIPR002180. DMRL_synthase.
[Graphical view]
PANTHERPTHR21058. PTHR21058. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. SSF52121. 1 hit.
TIGRFAMsTIGR00114. lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB_GEOMG
AccessionPrimary (citable) accession number: Q39V66
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: May 14, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways