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P16440

- RISA_BACSU

UniProt

P16440 - RISA_BACSU

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Protein

Riboflavin synthase

Gene

ribE

Organism
Bacillus subtilis (strain 168)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Enzyme regulationi

Is activated by sulfite ions.1 Publication

Kineticsi

  1. KM=14 µM for 6,7-dimethyl-8-(1-D-ribityl)lumazine1 Publication

pH dependencei

Optimum pH is 7.4.1 Publication

Pathwayi

GO - Molecular functioni

  1. oxidoreductase activity Source: InterPro
  2. riboflavin synthase activity Source: UniProtKB-EC

GO - Biological processi

  1. riboflavin biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

BioCyciBSUB:BSU23270-MONOMER.
MetaCyc:MONOMER-14608.
SABIO-RKP16440.
UniPathwayiUPA00275; UER00405.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin synthase (EC:2.5.1.9)
Short name:
RS
Alternative name(s):
Heavy riboflavin synthase alpha subunit
Short name:
HRS alpha subunit
Light riboflavin synthase
Gene namesi
Name:ribE
Synonyms:ribB
Ordered Locus Names:BSU23270
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
ProteomesiUP000001570: Chromosome

Organism-specific databases

GenoListiBSU23270. [Micado]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Riboflavin synthasePRO_0000068159Add
BLAST

Proteomic databases

PaxDbiP16440.

Interactioni

Subunit structurei

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.3 Publications

Protein-protein interaction databases

STRINGi224308.BSU23270.

Structurei

3D structure databases

ProteinModelPortaliP16440.
SMRiP16440. Positions 1-198.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 9696Lumazine-binding 1Add
BLAST
Repeati97 – 19397Lumazine-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4 – 63Substrate bindingBy similarity
Regioni47 – 493Substrate bindingBy similarity
Regioni61 – 666Substrate bindingBy similarity

Sequence similaritiesi

Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0307.
HOGENOMiHOG000151757.
InParanoidiP16440.
KOiK00793.
OMAiANAVYYE.
OrthoDBiEOG6VMTQH.
PhylomeDBiP16440.

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view]
PANTHERiPTHR21098. PTHR21098. 1 hit.
PfamiPF00677. Lum_binding. 2 hits.
[Graphical view]
PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMiSSF63380. SSF63380. 2 hits.
TIGRFAMsiTIGR00187. ribE. 1 hit.
PROSITEiPS51177. LUMAZINE_BIND. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P16440-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MFTGIIEETG TIESMKKAGH AMALTIKCSK ILEDVHLGDS IAVNGICLTV
60 70 80 90 100
TDFTKNQFTV DVMPETVKAT SLNDLTKGSK VNLERAMAAN GRFGGHFVSG
110 120 130 140 150
HVDGTAEITR IEEKSNAVYY DLKMDPSLTK TLVLKGSITV DGVSLTIFGL
160 170 180 190 200
TEDTVTISLI PHTISETIFS EKTIGSKVNI ECDMIGKYMY RFLHKANENK
210
TQQTITKAFL SENGF
Length:215
Mass (Da):23,481
Last modified:February 1, 1991 - v2
Checksum:i5B2A694C078B3600
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09228 Genomic DNA. Translation: AAA67482.1.
X51510 Genomic DNA. Translation: CAA35879.1.
AL009126 Genomic DNA. Translation: CAB14259.1.
PIRiS45544. A35711.
RefSeqiNP_390208.1. NC_000964.3.
WP_004398505.1. NZ_CM000487.1.

Genome annotation databases

EnsemblBacteriaiCAB14259; CAB14259; BSU23270.
GeneIDi938947.
KEGGibsu:BSU23270.
PATRICi18976471. VBIBacSub10457_2426.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L09228 Genomic DNA. Translation: AAA67482.1 .
X51510 Genomic DNA. Translation: CAA35879.1 .
AL009126 Genomic DNA. Translation: CAB14259.1 .
PIRi S45544. A35711.
RefSeqi NP_390208.1. NC_000964.3.
WP_004398505.1. NZ_CM000487.1.

3D structure databases

ProteinModelPortali P16440.
SMRi P16440. Positions 1-198.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 224308.BSU23270.

Proteomic databases

PaxDbi P16440.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAB14259 ; CAB14259 ; BSU23270 .
GeneIDi 938947.
KEGGi bsu:BSU23270.
PATRICi 18976471. VBIBacSub10457_2426.

Organism-specific databases

GenoListi BSU23270. [Micado ]

Phylogenomic databases

eggNOGi COG0307.
HOGENOMi HOG000151757.
InParanoidi P16440.
KOi K00793.
OMAi ANAVYYE.
OrthoDBi EOG6VMTQH.
PhylomeDBi P16440.

Enzyme and pathway databases

UniPathwayi UPA00275 ; UER00405 .
BioCyci BSUB:BSU23270-MONOMER.
MetaCyc:MONOMER-14608.
SABIO-RK P16440.

Family and domain databases

Gene3Di 2.40.30.20. 2 hits.
InterProi IPR023366. ATPase_asu-like.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
[Graphical view ]
PANTHERi PTHR21098. PTHR21098. 1 hit.
Pfami PF00677. Lum_binding. 2 hits.
[Graphical view ]
PIRSFi PIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMi SSF63380. SSF63380. 2 hits.
TIGRFAMsi TIGR00187. ribE. 1 hit.
PROSITEi PS51177. LUMAZINE_BIND. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiRISA_BACSU
AccessioniPrimary (citable) accession number: P16440
Secondary accession number(s): P17619
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: February 1, 1991
Last modified: October 29, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3