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Q6HE53 (RISB_BACHK) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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:BT9727_3854
OrganismBacillus thuringiensis subsp. konkukian (strain 97-27) [Complete proteome] [HAMAP]
Taxonomic identifier281309 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length153 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 – 1531536,7-dimethyl-8-ribityllumazine synthase HAMAP MF_00178
PRO_1000040369

Sequences

Sequence LengthMass (Da)Tools
Q6HE53 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: AA5386484EA66839

FASTA15316,246
        10         20         30         40         50         60 
MVFEGHLVGT GLKVGVVVGR FNEFITSKLL GGALDGLKRH GVEENDIDVA WVPGAFEIPL 

        70         80         90        100        110        120 
IAKKMANSGK YDAVITLGTV IRGATTHYDY VCNEVAKGVA SLSLQTDIPV IFGVLTTETI 

       130        140        150 
EQAIERAGTK AGNKGYESAV AAIEMAHLSK QWA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017355 Genomic DNA. Translation: AAT63108.1.
RefSeqYP_038173.1. NC_005957.1.

3D structure databases

HSSPHSSP built from PDB template 1RVV based on UniProtKB P11998.
ProteinModelPortalQ6HE53.
SMRQ6HE53. Positions 2-152.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000076534; EBBACP00000074620; EBBACG00000076525.
GeneID2858227.
GenomeReviewsGene locus BT9727_3854 in contig AE017355_GR.
KEGGbtk:BT9727_3854.
PATRIC18988766. VBIBacThu119411_4109.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000002577.
HOGENOMHBG311126.
OMADYVCNEA.
ProtClustDBPRK00061.

Enzyme and pathway databases

BioCycBTHU281309:BT9727_3854-MONOMER.

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_BACHK
AccessionPrimary (citable) accession number: Q6HE53
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2004
Last modified: January 25, 2012
This is version 48 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