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Reviewed, UniProtKB/Swiss-Prot P0AFU8 (RISA_ECOLI)

Last modified November 3, 2009. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Riboflavin synthase alpha chain
    EC=2.5.1.9
Gene names
Name: ribE
Synonyms: ribC
Ordered Locus Names: b1662, JW1654
OrganismEscherichia coli (strain K12) [Complete proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length213 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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 alpha subunit catalyzes the dismutation of 6,7-dimethyl-8-lumazine to riboflavin and 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione.

Catalytic activity

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

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil and riboflavin from 6,7-dimethyl-8-(1-D-ribityl)lumazine: step 1/1.

Subunit structure

Oligomer that consist of 3 alpha subunits and 60 beta subunits.

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

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

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 213213Riboflavin synthase alpha chain
PRO_0000068166

Regions

Repeat1 – 9797Lumazine-binding 1
Repeat98 – 19598Lumazine-binding 2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
P0AFU8-1 [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: 9022701] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: 9023191] [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: 9097039] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 11399071] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-97.
[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: 11377200] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
RefSeqAP_002284.1.
NP_416179.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1HZENMR-A/B1-97[»]
1I18NMR-A/B1-97[»]
1I8DX-ray2.00A/B/C1-213[»]
1PKVX-ray2.60A/B1-97[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGP0AFU8.

2-D gel databases

SWISS-2DPAGEP0AFU8.

Genome annotation databases

GeneID945848.
GenomeReviewsGene locus JW1654 in contig AP009048_GR.
Gene locus b1662 in contig U00096_GR.
KEGGecj:JW1654.
eco:b1662.

Organism-specific databases

EchoBASEEB1378.
EcoGeneEG11406. ribE.
CMRSearch...

Phylogenomic databases

HOGENOMP0AFU8.
OMACLTVTKI.

Enzyme and pathway databases

BioCycEcoCyc:RIBOFLAVIN-SYN-MON.
MetaCyc:RIBOFLAVIN-SYN-MON.

Gene expression databases

GenevestigatorP0AFU8.

Family and domain databases

InterProIPR001783. Lumazine_bd.
[Graphical view]
PANTHERPTHR21098. Lumazine_bd. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
ProDomPD004110. Lum_binding. 2 hits.
[Graphical view] [Entries sharing at least one domain]
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00140. Riboflavin.

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: November 3, 2009
This is version 40 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents