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C3F6E2 (C3F6E2_BACTU) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 15. 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 HAMAP MF_00178

Short name=DMRL synthase HAMAP MF_00178
Short name=Lumazine synthase HAMAP MF_00178
EC=2.5.1.9 HAMAP MF_00178
Alternative name(s):
Riboflavin synthase beta chain HAMAP MF_00178
Gene names
Name:ribH HAMAP MF_00178
ORF Names:bthur0007_39600 EMBL EEM58154.1
OrganismBacillus thuringiensis serovar monterrey BGSC 4AJ1 EMBL EEM58154.1
Taxonomic identifier527022 [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 RuleBase RU003795

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 RuleBase RU003795

Sequence similarities

Belongs to the DMRL synthase family. HAMAP MF_00178 RuleBase RU003795

Ontologies

Sequences

Sequence LengthMass (Da)Tools
C3F6E2 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: AA5391784EA66839

FASTA15316,255
        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 HWA 

« Hide

References

[1]"Annotation of the Bacillus thuringiensis BGSC 4AJ1 genome."
Read T.D., Akmal A., Bishop-Lilly K., Chen P.E., Cook C., Kiley M.P., Lentz S., Mateczun A., Nagarajan N., Nolan N., Osborne B.I., Pop M., Sozhamannan S., Stewart A.C., Sulakvelidze A., Thomason B., Willner K., Zwick M.E.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: BGSC 4AJ1 EMBL EEM58154.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
ACNE01000102 Genomic DNA. Translation: EEM58154.1.

3D structure databases

ProteinModelPortalC3F6E2.
SMRC3F6E2. Positions 2-152.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000398714; EBBACP00000391395; EBBACG00000398654.
PATRIC28908305. VBIBacThu130558_0254.

Family and domain databases

HAMAPMF_00178. Lumazine_synth.
[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]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
TIGRFAMsTIGR00114. Lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC3F6E2_BACTU
AccessionPrimary (citable) accession number: C3F6E2
Entry history
Integrated into UniProtKB/TrEMBL: June 16, 2009
Last sequence update: June 16, 2009
Last modified: December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)