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P0AFU9 (RISA_SHIFL) 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
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 alpha chain

EC=2.5.1.9
Gene names
Name:ribE
Synonyms:ribC
Ordered Locus Names:SF1690, S1822
OrganismShigella flexneri [Complete proteome] [HAMAP]
Taxonomic identifier623 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

Protein attributes

Sequence length213 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 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 By similarity.

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

Subunit structure

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

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   DomainRepeat
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

riboflavin 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_0000068172

Regions

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

Sequences

Sequence LengthMass (Da)Tools
P0AFU9 [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

[1]"Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. expand/collapse author list , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 301 / Serotype 2a.
[2]"Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T."
Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.
Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700930 / 2457T / Serotype 2a.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005674 Genomic DNA. Translation: AAN43269.1.
AE014073 Genomic DNA. Translation: AAP17158.1.
RefSeqNP_707562.1. NC_004337.2.
NP_837349.1. NC_004741.1.

3D structure databases

ProteinModelPortalP0AFU9.
SMRP0AFU9. Positions 1-206.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000087944; EBESCP00000084766; EBESCG00000086989.
EBESCT00000090932; EBESCP00000087568; EBESCG00000089976.
GeneID1024885.
1078160.
GenomeReviewsGene locus SF1690 in contig AE005674_GR.
Gene locus S1822 in contig AE014073_GR.
KEGGsfl:SF1690.
sfx:S1822.
PATRIC18705046. VBIShiFle31049_2021.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000011315.
HOGENOMHBG289809.
OMAHILSGHV.
ProtClustDBPRK09289.

Enzyme and pathway databases

BioCycSFLE198214:AAN43269.1-MONOMER.

Family and domain databases

InterProIPR023366. ATPase_F1/A1-cplx_a_su_N.
IPR001783. Lumazine-bd.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
Gene3DG3DSA:2.40.30.20. G3DSA:2.40.30.20. 2 hits.
KOK00793.
PANTHERPTHR21098. Lumazine_bd. 1 hit.
PfamPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMSSF63380. Riboflavin_synthase_like_b-brl. 2 hits.
TIGRFAMsTIGR00187. RibE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRISA_SHIFL
AccessionPrimary (citable) accession number: P0AFU9
Secondary accession number(s): P29015
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
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