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Protein

Riboflavin synthase

Gene

rib5

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: 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.

Pathwayi

GO - Molecular functioni

  • oxidoreductase activity Source: InterPro
  • riboflavin synthase activity Source: PomBase

GO - Biological processi

  • riboflavin biosynthetic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

BRENDAi2.5.1.9. 5613.
UniPathwayiUPA00275; UER00405.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin synthase (EC:2.5.1.9)
Short name:
RS
Gene namesi
Name:rib5
ORF Names:SPCC1450.13c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC1450.13c.
PomBaseiSPCC1450.13c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 208208Riboflavin synthasePRO_0000068173Add
BLAST

Proteomic databases

MaxQBiQ9Y7P0.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

MINTiMINT-4717668.
STRINGi4896.SPCC1450.13c-1.

Structurei

Secondary structure

1
208
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 1811Combined sources
Turni19 – 213Combined sources
Beta strandi22 – 287Combined sources
Helixi30 – 323Combined sources
Beta strandi41 – 444Combined sources
Beta strandi47 – 548Combined sources
Beta strandi56 – 638Combined sources
Helixi65 – 706Combined sources
Helixi73 – 753Combined sources
Beta strandi81 – 866Combined sources
Beta strandi94 – 963Combined sources
Beta strandi105 – 11511Combined sources
Beta strandi118 – 12710Combined sources
Helixi128 – 1336Combined sources
Beta strandi139 – 1424Combined sources
Beta strandi145 – 1528Combined sources
Beta strandi157 – 1615Combined sources
Helixi163 – 1664Combined sources
Helixi170 – 1734Combined sources
Beta strandi179 – 1846Combined sources
Helixi187 – 19812Combined sources
Turni199 – 2013Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZLX-ray2.10A1-208[»]
ProteinModelPortaliQ9Y7P0.
SMRiQ9Y7P0. Positions 1-202.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y7P0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1 – 9797Lumazine-binding 1Add
BLAST
Repeati98 – 19598Lumazine-binding 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni81 – 855Lumazine bindingCurated
Regioni179 – 1835Lumazine bindingCurated

Sequence similaritiesi

Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0307.
HOGENOMiHOG000151757.
InParanoidiQ9Y7P0.
KOiK00793.
OMAiMFSGIVA.
OrthoDBiEOG793BMH.
PhylomeDBiQ9Y7P0.

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.

Q9Y7P0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTGLVEAIG VVKDVQGTID NGFAMKIEAP QILDDCHTGD SIAVNGTCLT
60 70 80 90 100
VTDFDRYHFT VGIAPESLRL TNLGQCKAGD PVNLERAVLS STRMGGHFVQ
110 120 130 140 150
GHVDTVAEIV EKKQDGEAID FTFRPRDPFV LKYIVYKGYI ALDGTSLTIT
160 170 180 190 200
HVDDSTFSIM MISYTQSKVI MAKKNVGDLV NVEVDQIGKY TEKLVEAHIA

DWIKKTQA
Length:208
Mass (Da):22,861
Last modified:November 1, 1999 - v1
Checksum:i59C5065DDD4C7B8B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF505789 mRNA. Translation: AAM28201.1.
CU329672 Genomic DNA. Translation: CAB40180.1.
PIRiT40995.
RefSeqiNP_588312.1. NM_001023302.2.

Genome annotation databases

EnsemblFungiiSPCC1450.13c.1; SPCC1450.13c.1:pep; SPCC1450.13c.
GeneIDi2539183.
KEGGispo:SPCC1450.13c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF505789 mRNA. Translation: AAM28201.1.
CU329672 Genomic DNA. Translation: CAB40180.1.
PIRiT40995.
RefSeqiNP_588312.1. NM_001023302.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KZLX-ray2.10A1-208[»]
ProteinModelPortaliQ9Y7P0.
SMRiQ9Y7P0. Positions 1-202.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4717668.
STRINGi4896.SPCC1450.13c-1.

Proteomic databases

MaxQBiQ9Y7P0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC1450.13c.1; SPCC1450.13c.1:pep; SPCC1450.13c.
GeneIDi2539183.
KEGGispo:SPCC1450.13c.

Organism-specific databases

EuPathDBiFungiDB:SPCC1450.13c.
PomBaseiSPCC1450.13c.

Phylogenomic databases

eggNOGiCOG0307.
HOGENOMiHOG000151757.
InParanoidiQ9Y7P0.
KOiK00793.
OMAiMFSGIVA.
OrthoDBiEOG793BMH.
PhylomeDBiQ9Y7P0.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.
BRENDAi2.5.1.9. 5613.

Miscellaneous databases

EvolutionaryTraceiQ9Y7P0.
NextBioi20800354.
PROiQ9Y7P0.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Riboflavin synthase of Schizosaccharomyces pombe. Protein dynamics revealed by 19F NMR protein perturbation experiments."
    Fischer M., Schott A.-K., Kemter K., Feicht R., Richter G., Illarionov B., Eisenreich W., Gerhardt S., Cushman M., Steinbacher S., Huber R., Bacher A.
    BMC Biochem. 4:18-18(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Studies on the reaction mechanism of riboflavin synthase: X-ray crystal structure of a complex with 6-carboxyethyl-7-oxo-8-ribityllumazine."
    Gerhardt S., Schott A.-K., Kairies N., Cushman M., Illarionov B., Eisenreich W., Bacher A., Huber R., Steinbacher S., Fischer M.
    Structure 10:1371-1381(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

Entry informationi

Entry nameiRISA_SCHPO
AccessioniPrimary (citable) accession number: Q9Y7P0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: November 1, 1999
Last modified: May 27, 2015
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.