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P50854 (RISA_ACTPL) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 64. 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

Short name=RS
EC=2.5.1.9
Gene names
Name:ribE
Synonyms:ribB
OrganismActinobacillus pleuropneumoniae (Haemophilus pleuropneumoniae)
Taxonomic identifier715 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeActinobacillus

Protein attributes

Sequence length215 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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

Homotrimer By similarity.

Sequence similarities

Contains 2 lumazine-binding repeats.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   DomainRepeat
   Molecular functionTransferase
Gene Ontology (GO)
   Biological_processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionoxidoreductase activity

Inferred from electronic annotation. Source: InterPro

riboflavin synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Riboflavin synthase
PRO_0000068156

Regions

Repeat1 – 9696Lumazine-binding 1
Repeat97 – 19397Lumazine-binding 2
Region4 – 63Substrate binding By similarity
Region47 – 493Substrate binding By similarity
Region61 – 666Substrate binding By similarity

Sequences

Sequence LengthMass (Da)Tools
P50854 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D66CFB7C37CFCF5E

FASTA21523,404
        10         20         30         40         50         60 
MFTGIIEEVG KIAQIHKQGE FAVVTINATK VLQDVHLGDT IAVNGVCLTV TSFSSNQFTA 

        70         80         90        100        110        120 
DVMSETLKRT SLGELKSNSP VNLERAMAAN GRFGGHIVSG HIDGTGEIAE ITPAHNSTWY 

       130        140        150        160        170        180 
RIKTSPKLMR YIIEKGSITI DGISLTVVDT DDESFRVSII PHTIKETNLG SKKIGSIVNL 

       190        200        210 
ENDIVGKYIE QFLLKKPADE PKSNLSLDFL KQAGF 

« Hide

References

[1]"Characterization of Actinobacillus pleuropneumoniae riboflavin biosynthesis genes."
Fuller T.E., Mulks M.H.
J. Bacteriol. 177:7265-7270(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ISU-178 / Serotype 5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U27202 Genomic DNA. Translation: AAA86523.1.
PIRT50547.

3D structure databases

ProteinModelPortalP50854.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayUPA00275; UER00405.

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...

Entry information

Entry nameRISA_ACTPL
AccessionPrimary (citable) accession number: P50854
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 64 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