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Q01T71 (RISB_SOLUE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 34. 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=Lumazine synthase
EC=2.5.1.9
Alternative name(s):
Riboflavin synthase beta chain
Gene names
Name:ribH
Ordered Locus Names:Acid_6223
OrganismSolibacter usitatus (strain Ellin6076) [Complete proteome] [HAMAP]
Taxonomic identifier234267 [NCBI]
Taxonomic lineageBacteriaAcidobacteriaSolibacteresSolibacteralesSolibacteraceaeCandidatus Solibacter

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.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular functionriboflavin synthase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1581586,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_1000040520

Sequences

Sequence LengthMass (Da)Tools
Q01T71 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 79D106501F965698

FASTA15816,711
        10         20         30         40         50         60 
MPKVFEGQLS AAGLRFAIVV SRFNSFITDR LLGGAMDALT RAGADPELID IVKVPGSWEV 

        70         80         90        100        110        120 
PLVTGELARQ HRYDALICLS AVIRGETPHF DYVAGEAAKG IAHVSSETGV PVAFGVLTTN 

       130        140        150 
TLEQAIDRAG AKGGNKGFDA AMTAIEMANL LRTLRQAT 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000473 Genomic DNA. Translation: ABJ87149.1.
RefSeqYP_827434.1. NC_008536.1.

3D structure databases

ProteinModelPortalQ01T71.
SMRQ01T71. Positions 3-155.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ01T71.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4425559.
GenomeReviewsGene locus Acid_6223 in contig CP000473_GR.
KEGGsus:Acid_6223.
NMPDRfig|234267.9.peg.5914.
PATRIC32015122. VBICanSol30224_6516.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0054.
HOGENOMHBG311126.
OMADYVCNEA.
PhylomeDBQ01T71.

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.
TIGRFAMsTIGR00114. Lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB_SOLUE
AccessionPrimary (citable) accession number: Q01T71
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 14, 2006
Last modified: January 25, 2012
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families