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C5BCH5 (RISB_EDWI9) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:NT01EI_1057
OrganismEdwardsiella ictaluri (strain 93-146) [Complete proteome] [HAMAP]
Taxonomic identifier634503 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella

Protein attributes

Sequence length156 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

Subunit structure

Forms an icosahedral capsid composed of 60 subunits, arranged as a dodecamer of pentamers By similarity.

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 – 1561566,7-dimethyl-8-ribityllumazine synthase HAMAP-Rule MF_00178
PRO_1000203790

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 site2215-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
C5BCH5 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: EDD1FEFA5894EF20

FASTA15616,147
        10         20         30         40         50         60 
MKTIQGVVAA PQARVAIAIS RFNHFINDSL LEGAIDALKR IGQVSDENIT VVWVPGAYEL 

        70         80         90        100        110        120 
PLTVRALASS GRYDAVVALG TVIRGGTAHF EFVAGECSSG LASVALNTDV PVAFGVLTTE 

       130        140        150 
TIEQAIDRAG AKAGNKGAEA ALTALEMINV LKAIKA 

« Hide

References

[1]"Complete genome sequence of Edwardsiella ictaluri 93-146."
Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 93-146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001600 Genomic DNA. Translation: ACR68269.1.
RefSeqYP_002932504.1. NC_012779.2.

3D structure databases

ProteinModelPortalC5BCH5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING634503.NT01EI_1057.

Proteomic databases

PRIDEC5BCH5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACR68269; ACR68269; NT01EI_1057.
GeneID7959440.
KEGGeic:NT01EI_1057.
PATRIC21835282. VBIEdwIct114273_0957.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0054.
HOGENOMHOG000229250.
KOK00794.
OMAISRFNDF.
OrthoDBEOG6RC3WC.

Enzyme and pathway databases

BioCycEICT634503:GCMY-1046-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_EDWI9
AccessionPrimary (citable) accession number: C5BCH5
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: May 14, 2014
This is version 35 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