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P0AFU8 (RISA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Riboflavin synthase

Short name=RS
EC=2.5.1.9
Gene names
Name:ribC
Synonyms:ribE
Ordered Locus Names:b1662, JW1654
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil. Ref.1

Catalytic activity

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. Ref.1

Pathway

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

Subunit structure

Homotrimer. Unlike in B.subtilis, does not interact with 6,7-dimethyl-8-ribityllumazine synthase. Ref.1

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   DomainRepeat
   Molecular functionTransferase
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processriboflavin biosynthetic process

Inferred from direct assay Ref.1. Source: EcoCyc

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

riboflavin synthase activity

Inferred from direct assay Ref.1. Source: EcoCyc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 213213Riboflavin synthase
PRO_0000068166

Regions

Repeat1 – 9797Lumazine-binding 1
Repeat98 – 19598Lumazine-binding 2
Region4 – 63Substrate binding
Region48 – 503Substrate binding
Region62 – 676Substrate binding

Secondary structure

...................................... 213
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AFU8 [UniParc].

Last modified December 20, 2005. Version 1.
Checksum: CD1C7E40E4AC88B6

FASTA21323,445
        10         20         30         40         50         60 
MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT VTEINGNHVS 

        70         80         90        100        110        120 
FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS GHIMTTAEVA KILTSENNRQ 

       130        140        150        160        170        180 
IWFKVQDSQL MKYILYKGFI GIDGISLTVG EVTPTRFCVH LIPETLERTT LGKKKLGARV 

       190        200        210 
NIEIDPQTQA VVDTVERVLA ARENAMNQPG TEA 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, sequencing, mapping and hyperexpression of the ribC gene coding for riboflavin synthase of Escherichia coli."
Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A.
Eur. J. Biochem. 242:712-719(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
Strain: K12 / RR28.
[2]"Analysis of the boundaries of Salmonella pathogenicity island 2 and the corresponding chromosomal region of Escherichia coli K-12."
Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R., Holden D.W.
J. Bacteriol. 179:1105-1111(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The solution structure of the N-terminal domain of riboflavin synthase."
Truffault V., Coles M., Diercks T., Abelmann K., Eberhardt S., Luttgen H., Bacher A., Kessler H.
J. Mol. Biol. 309:949-960(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH RIBOFLAVIN.
[7]"Crystal structure of riboflavin synthase."
Liao D.I., Wawrzak Z., Calabrese J.C., Viitanen P.V., Jordan D.B.
Structure 9:399-408(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[8]"The structure of the N-terminal domain of riboflavin synthase in complex with riboflavin at 2.6A resolution."
Meining W., Eberhardt S., Bacher A., Ladenstein R.
J. Mol. Biol. 331:1053-1063(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-97 IN COMPLEX WITH RIBOFLAVIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X69109 Genomic DNA. Translation: CAA48861.1.
U68703 Genomic DNA. Translation: AAB47940.1.
U00096 Genomic DNA. Translation: AAC74734.1.
AP009048 Genomic DNA. Translation: BAA15429.1.
PIRS28526.
RefSeqNP_416179.1. NC_000913.3.
YP_489926.1. NC_007779.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1HZENMR-A/B1-97[»]
1I18NMR-A/B1-97[»]
1I8DX-ray2.00A/B/C1-213[»]
1PKVX-ray2.60A/B1-97[»]
ProteinModelPortalP0AFU8.
SMRP0AFU8. Positions 1-206.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-47865N.
IntActP0AFU8. 3 interactions.
STRING511145.b1662.

Chemistry

DrugBankDB00140. Riboflavin.

2D gel databases

SWISS-2DPAGEP0AFU8.

Proteomic databases

PaxDbP0AFU8.
PRIDEP0AFU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74734; AAC74734; b1662.
BAA15429; BAA15429; BAA15429.
GeneID12932660.
945848.
KEGGecj:Y75_p1639.
eco:b1662.
PATRIC32118630. VBIEscCol129921_1735.

Organism-specific databases

EchoBASEEB1378.
EcoGeneEG11406. ribC.

Phylogenomic databases

eggNOGCOG0307.
HOGENOMHOG000151758.
KOK00793.
OMANHQIWFR.
OrthoDBEOG6VMTQH.
PhylomeDBP0AFU8.

Enzyme and pathway databases

BioCycEcoCyc:RIBOFLAVIN-SYN-MONOMER.
ECOL316407:JW1654-MONOMER.
MetaCyc:RIBOFLAVIN-SYN-MONOMER.
UniPathwayUPA00275; UER00405.

Gene expression databases

GenevestigatorP0AFU8.

Family and domain databases

Gene3D2.40.30.20. 2 hits.
InterProIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERPTHR21098. PTHR21098. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMSSF63380. SSF63380. 2 hits.
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0AFU8.
PROP0AFU8.

Entry information

Entry nameRISA_ECOLI
AccessionPrimary (citable) accession number: P0AFU8
Secondary accession number(s): P29015
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: May 14, 2014
This is version 77 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene