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O67604 (RISA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 86. 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:ribC
Ordered Locus Names:aq_1707
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length207 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
   Technical termComplete proteome
Reference proteome
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 – 207207Riboflavin synthase
PRO_0000068157

Regions

Repeat1 – 9494Lumazine-binding 1
Repeat95 – 19197Lumazine-binding 2
Region4 – 63Substrate binding By similarity
Region45 – 473Substrate binding By similarity
Region59 – 646Substrate binding By similarity

Sequences

Sequence LengthMass (Da)Tools
O67604 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 322A09FF7B15E432

FASTA20723,196
        10         20         30         40         50         60 
MFTGLVEDLG KVKNLTLSSK GAKLSVETKL EDVKLGDSVS VNGACLTVVD IKSSTLTFDV 

        70         80         90        100        110        120 
SPETLKRTNL GKLKTGDYVN LERALRVGER LGGHIVQGHV DFTAPVKSFN FLGEHYELVI 

       130        140        150        160        170        180 
EIPEEWSIYV VEKGSIALDG ISLTVNYVKE NKVFINIIPH TYKSTNLQFK KVGDLLNVET 

       190        200 
DILGKYVINY LNKLKKKEDI FKEFLKW 

« Hide

References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07572.1.
PIRB70447.
RefSeqNP_214170.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67604.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1707.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07572; AAC07572; aq_1707.
GeneID1193319.
KEGGaae:aq_1707.
PATRIC20960412. VBIAquAeo85532_1311.

Phylogenomic databases

eggNOGCOG0307.
HOGENOMHOG000151757.
KOK00793.
OMARIAFENS.
OrthoDBEOG6VMTQH.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1221-MONOMER.
RETL1328306-WGS:GSTH-1526-MONOMER.
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_AQUAE
AccessionPrimary (citable) accession number: O67604
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: July 9, 2014
This is version 86 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