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Protein

Riboflavin synthase

Gene

ribE

Organism
Bacillus amyloliquefaciens (Bacillus velezensis)
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), 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 sitei135Substrate 2 bindingBy similarity1

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:ribB
OrganismiBacillus amyloliquefaciens (Bacillus velezensis)
Taxonomic identifieri1390 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000681581 – 215Riboflavin synthaseAdd BLAST215

Interactioni

Subunit structurei

Homotrimer.By similarity

Protein-protein interaction databases

STRINGi326423.RBAM_021410.

Structurei

3D structure databases

ProteinModelPortaliQ44680.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1 – 96Lumazine-binding 1Add BLAST96
Repeati97 – 193Lumazine-binding 2Add BLAST97

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni4 – 6Substrate 1 bindingBy similarity3
Regioni47 – 49Substrate 2 binding; shared with one trimeric partnerBy similarity3
Regioni61 – 66Substrate 2 binding; shared with one trimeric partnerBy similarity6
Regioni100 – 102Substrate 2 binding; shared with one trimeric partnerBy similarity3
Regioni144 – 146Substrate 1 bindingBy similarity3
Regioni158 – 163Substrate 1 bindingBy similarity6

Sequence similaritiesi

Contains 2 lumazine-binding repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4108R6K. Bacteria.
COG0307. LUCA.

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATP_synth_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.

Q44680-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFTGIVEETG TIQAIKKTGL SMALTIAASK VTSDVRLGDS IAVNGICLTV
60 70 80 90 100
TGFSDNQFTV DVMPETVKAT SLNGLSKGSK VNLERAMSAN GRFGGHFVSG
110 120 130 140 150
HVDGTAEITR IEKKSNAVYY DLKLSPELTK TLVLKGSITV DGVSSTIFGL
160 170 180 190 200
SDESVTVSVI PHTISETIFR TKAVGSIVNI ECDMIGKYLY RFLHKTEQTK
210
SNQTITEAFF SENGF
Length:215
Mass (Da):23,089
Last modified:November 1, 1996 - v1
Checksum:i5A5174315DFE0033
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95955 Genomic DNA. Translation: CAA65190.1.
PIRiT50542.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95955 Genomic DNA. Translation: CAA65190.1.
PIRiT50542.

3D structure databases

ProteinModelPortaliQ44680.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326423.RBAM_021410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4108R6K. Bacteria.
COG0307. LUCA.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00405.

Family and domain databases

Gene3Di2.40.30.20. 2 hits.
InterProiIPR023366. ATP_synth_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_BACAM
AccessioniPrimary (citable) accession number: Q44680
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 30, 2016
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.