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Protein

Riboflavin synthase

Gene

ribE

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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.By similarity

Catalytic activityi

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

Pathwayi: riboflavin biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 6,7-dimethyl-8-ribityllumazine synthase (ribH)
  2. Riboflavin synthase (ribE)
This subpathway is part of the pathway riboflavin biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil, the pathway riboflavin biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei137 – 1371Substrate 2 bindingBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.

Names & Taxonomyi

Protein namesi
Recommended name:
Riboflavin synthase (EC:2.5.1.9)
Short name:
RS
Gene namesi
Name:ribE
Synonyms:ribC
Ordered Locus Names:SF1690, S1822
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Riboflavin synthasePRO_0000068172Add
BLAST

Proteomic databases

PaxDbiP0AFU9.
PRIDEiP0AFU9.

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi198214.SF1690.

Structurei

3D structure databases

ProteinModelPortaliP0AFU9.
SMRiP0AFU9. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

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
Regioni4 – 63Substrate 1 bindingBy similarity
Regioni48 – 503Substrate 2 binding; shared with one trimeric partnerBy similarity
Regioni62 – 676Substrate 2 binding; shared with one trimeric partnerBy similarity
Regioni101 – 1033Substrate 2 binding; shared with one trimeric partnerBy similarity
Regioni146 – 1483Substrate 1 bindingBy similarity
Regioni160 – 1656Substrate 1 bindingBy similarity

Sequence similaritiesi

Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108R6K. Bacteria.
COG0307. LUCA.
HOGENOMiHOG000151758.
KOiK00793.
OMAiHILSGHV.

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.

P0AFU9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT
60 70 80 90 100
VTEINGNHVS FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS
110 120 130 140 150
GHIMTTAEVA KILTSENNRQ IWFKVQDSQL MKYILYKGFI GIDGISLTVG
160 170 180 190 200
EVTPTRFCVH LIPETLERTT LGKKKLGARV NIEIDPQTQA VVDTVERVLA
210
ARENAMNQPG TEA
Length:213
Mass (Da):23,445
Last modified:December 20, 2005 - v1
Checksum:iCD1C7E40E4AC88B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43269.1.
AE014073 Genomic DNA. Translation: AAP17158.1.
RefSeqiNP_707562.1. NC_004337.2.
WP_000493947.1. NZ_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN43269; AAN43269; SF1690.
AAP17158; AAP17158; S1822.
GeneIDi1024885.
KEGGisfl:SF1690.
sft:NCTC1_01834.
sfx:S1822.
PATRICi18705046. VBIShiFle31049_2021.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43269.1.
AE014073 Genomic DNA. Translation: AAP17158.1.
RefSeqiNP_707562.1. NC_004337.2.
WP_000493947.1. NZ_LM651928.1.

3D structure databases

ProteinModelPortaliP0AFU9.
SMRiP0AFU9. Positions 1-206.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF1690.

Proteomic databases

PaxDbiP0AFU9.
PRIDEiP0AFU9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN43269; AAN43269; SF1690.
AAP17158; AAP17158; S1822.
GeneIDi1024885.
KEGGisfl:SF1690.
sft:NCTC1_01834.
sfx:S1822.
PATRICi18705046. VBIShiFle31049_2021.

Phylogenomic databases

eggNOGiENOG4108R6K. Bacteria.
COG0307. LUCA.
HOGENOMiHOG000151758.
KOiK00793.
OMAiHILSGHV.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.

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...

Entry informationi

Entry nameiRISA_SHIFL
AccessioniPrimary (citable) accession number: P0AFU9
Secondary accession number(s): P29015
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: September 7, 2016
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.