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P16440 (RISA_BACSU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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
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
Alternative name(s):
Heavy riboflavin synthase alpha subunit
Short name=HRS alpha subunit
Light riboflavin synthase
Gene names
Name:ribE
Synonyms:ribB
Ordered Locus Names:BSU23270
OrganismBacillus subtilis (strain 168) [Reference proteome] [HAMAP]
Taxonomic identifier224308 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus ›

Protein attributes

Sequence length215 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.5

Catalytic activity

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

Enzyme regulation

Is activated by sulfite ions. Ref.5

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. Can interact with 6,7-dimethyl-8-ribityllumazine synthase, forming a lumazine synthase/riboflavin synthase complex, also designated as 'heavy riboflavin synthase complex', which consists of a trimer of riboflavin synthase enclosed within an icosahedral structure composed of 60 subunits of 6,7-dimethyl-8-ribityllumazine synthase. Ref.1 Ref.5 Ref.6

Sequence similarities

Contains 2 lumazine-binding repeats.

Biophysicochemical properties

Kinetic parameters:

KM=14 µM for 6,7-dimethyl-8-(1-D-ribityl)lumazine Ref.5

pH dependence:

Optimum pH is 7.4.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   DomainRepeat
   Molecular functionTransferase
   Technical termComplete proteome
Direct protein sequencing
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 215215Riboflavin synthase
PRO_0000068159

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
P16440 [UniParc].

Last modified February 1, 1991. Version 2.
Checksum: 5B2A694C078B3600

FASTA21523,481
        10         20         30         40         50         60 
MFTGIIEETG TIESMKKAGH AMALTIKCSK ILEDVHLGDS IAVNGICLTV TDFTKNQFTV 

        70         80         90        100        110        120 
DVMPETVKAT SLNDLTKGSK VNLERAMAAN GRFGGHFVSG HVDGTAEITR IEEKSNAVYY 

       130        140        150        160        170        180 
DLKMDPSLTK TLVLKGSITV DGVSLTIFGL TEDTVTISLI PHTISETIFS EKTIGSKVNI 

       190        200        210 
ECDMIGKYMY RFLHKANENK TQQTITKAFL SENGF

« Hide

References

« Hide 'large scale' references
[1]"Riboflavin synthases of Bacillus subtilis. Purification and amino acid sequence of the alpha subunit."
Schott K., Kellermann J., Lottspeich F., Bacher A.
J. Biol. Chem. 265:4204-4209(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-202, SUBUNIT.
[2]Mironov V.N.
Thesis (1989), USSR Academy of Sciences, Russia
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / SHGW.
[3]"The organization of the Bacillus subtilis 168 chromosome region between the spoVA and serA genetic loci, based on sequence data."
Sorokin A.V., Zumstein E., Azevedo V., Ehrlich S.D., Serror P.
Mol. Microbiol. 10:385-395(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB 3610 / VKM B-501.
[4]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[5]"Riboflavin synthases of Bacillus subtilis. Purification and properties."
Bacher A., Baur R., Eggers U., Harders H.D., Otto M.K., Schnepple H.
J. Biol. Chem. 255:632-637(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[6]"Heavy riboflavin synthase from Bacillus subtilis. Quaternary structure and reaggregation."
Bacher A., Ludwig H.C., Schnepple H., Ben-Shaul Y.
J. Mol. Biol. 187:75-86(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L09228 Genomic DNA. Translation: AAA67482.1.
X51510 Genomic DNA. Translation: CAA35879.1.
AL009126 Genomic DNA. Translation: CAB14259.1.
PIRA35711. S45544.
RefSeqNP_390208.1. NC_000964.3.

3D structure databases

ProteinModelPortalP16440.
SMRP16440. Positions 1-198.
ModBaseSearch...

Protein-protein interaction databases

STRING224308.BSU23270.

Proteomic databases

PaxDbP16440.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB14259; CAB14259; BSU23270.
GeneID938947.
KEGGbsu:BSU23270.
PATRIC18976471. VBIBacSub10457_2426.

Organism-specific databases

GenoListBSU23270. [Micado]

Phylogenomic databases

eggNOGCOG0307.
HOGENOMHOG000151757.
KOK00793.
OMASRYVVEK.
ProtClustDBPRK09289.

Enzyme and pathway databases

BioCycBSUB:BSU23270-MONOMER.
MetaCyc:MONOMER-14608.
SABIO-RKP16440.
UniPathwayUPA00275; UER00405.

Family and domain databases

Gene3D2.40.30.20. 2 hits.
InterProIPR023366. ATPase_F1/A1-cplx_a_su_N.
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. Riboflavin_synthase_like_b-brl. 2 hits.
TIGRFAMsTIGR00187. ribE. 1 hit.
PROSITEPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameRISA_BACSU
AccessionPrimary (citable) accession number: P16440
Secondary accession number(s): P17619
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents