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Protein

Riboflavin synthase

Gene

ribE

Organism
Shigella flexneri
Status
Reviewed-Annotation score: Annotation score: 2 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), 6,7-dimethyl-8-ribityllumazine synthase (ribH), 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)DescriptionActionsGraphical viewLength
Binding sitei137Lumazine 2By similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processRiboflavin 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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeShigella
Proteomesi
  • UP000002673 Componenti: Chromosome
  • UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000681721 – 213Riboflavin synthaseAdd BLAST213

Proteomic databases

PaxDbiP0AFU9.
PRIDEiP0AFU9.

Interactioni

Subunit structurei

Homotrimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliP0AFU9.
SMRiP0AFU9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1 – 97Lumazine-binding 1Add BLAST97
Repeati98 – 195Lumazine-binding 2Add BLAST98

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 6Lumazine 1 bindingBy similarity3
Regioni48 – 50Lumazine 2 binding; shared with one trimeric partnerBy similarity3
Regioni62 – 67Lumazine 2 binding; shared with one trimeric partnerBy similarity6
Regioni101 – 103Lumazine 2 binding; shared with one trimeric partnerBy similarity3
Regioni146 – 148Lumazine 1 bindingBy similarity3
Regioni160 – 165Lumazine 1 bindingBy similarity6

Keywords - Domaini

Repeat

Phylogenomic databases

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

Family and domain databases

CDDicd00402. Riboflavin_synthase_like. 1 hit.
Gene3Di2.40.30.20. 2 hits.
InterProiView protein in InterPro
IPR023366. ATP_synth_asu-like_sf.
IPR001783. Lumazine-bd.
IPR026017. Lumazine-bd_dom.
IPR017938. Riboflavin_synthase-like_b-brl.
PANTHERiPTHR21098. PTHR21098. 1 hit.
PfamiView protein in Pfam
PF00677. Lum_binding. 2 hits.
PIRSFiPIRSF000498. Riboflavin_syn_A. 1 hit.
SUPFAMiSSF63380. SSF63380. 2 hits.
TIGRFAMsiTIGR00187. ribE. 1 hit.
PROSITEiView protein in PROSITE
PS51177. LUMAZINE_BIND. 2 hits.

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_NMXZ01000062.1.

Genome annotation databases

EnsemblBacteriaiAAN43269; AAN43269; SF1690.
AAP17158; AAP17158; S1822.
GeneIDi1024885.
KEGGisfl:SF1690.
sfx:S1822.
PATRICifig|198214.7.peg.1999.

Similar proteinsi

Entry informationi

Entry nameiRISA_SHIFL
AccessioniPrimary (citable) accession number: P0AFU9
Secondary accession number(s): P29015
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: November 22, 2017
This is version 82 of the entry and version 1 of the sequence. See 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