Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

6,7-dimethyl-8-ribityllumazine synthase 1

Gene

ribH1

Organism
Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin.UniRule annotation

Catalytic activityi

1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate.UniRule annotation

Pathwayi: riboflavin biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 6,7-dimethyl-8-ribityllumazine synthase 1 (ribH1), 6,7-dimethyl-8-ribityllumazine synthase 2 (ribH2)
  2. no protein annotated in this organism
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 sitei165-amino-6-(D-ribitylamino)uracilUniRule annotation1
Active sitei84Proton donorUniRule annotation1
Binding sitei1095-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei1231-deoxy-L-glycero-tetrulose 4-phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Riboflavin biosynthesis

Enzyme and pathway databases

BRENDAi2.5.1.78. 5347.
UniPathwayiUPA00275; UER00404.

Names & Taxonomyi

Protein namesi
Recommended name:
6,7-dimethyl-8-ribityllumazine synthase 1UniRule annotation (EC:2.5.1.78UniRule annotation)
Short name:
DMRL synthase 1UniRule annotation
Short name:
LS 1UniRule annotation
Short name:
Lumazine synthase 1UniRule annotation
Gene namesi
Name:ribH1UniRule annotation
Ordered Locus Names:R01215
ORF Names:SMc01777
OrganismiRhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium meliloti)
Taxonomic identifieri266834 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeSinorhizobium/Ensifer groupSinorhizobium
Proteomesi
  • UP000001976 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001347941 – 1536,7-dimethyl-8-ribityllumazine synthase 1Add BLAST153

Interactioni

Protein-protein interaction databases

STRINGi266834.SMc01777.

Structurei

3D structure databases

ProteinModelPortaliQ92QU0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni47 – 495-amino-6-(D-ribitylamino)uracil bindingUniRule annotation3
Regioni76 – 785-amino-6-(D-ribitylamino)uracil bindingUniRule annotation3
Regioni81 – 821-deoxy-L-glycero-tetrulose 4-phosphate bindingUniRule annotation2

Sequence similaritiesi

Belongs to the DMRL synthase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4108UTT. Bacteria.
COG0054. LUCA.
HOGENOMiHOG000229250.
KOiK00794.
OMAiTVCNDSS.

Family and domain databases

Gene3Di3.40.50.960. 1 hit.
HAMAPiMF_00178. Lumazine_synth. 1 hit.
InterProiIPR002180. DMRL_synthase.
[Graphical view]
PANTHERiPTHR21058. PTHR21058. 1 hit.
PfamiPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52121. SSF52121. 1 hit.
TIGRFAMsiTIGR00114. lumazine-synth. 1 hit.

Sequencei

Sequence statusi: Complete.

Q92QU0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKIKPVHIL IVEARFYDDM ADAMLDGAKH ALDAAGATYD IVTVPGALEI
60 70 80 90 100
PAAIAMALDG ADEGGAEYDG FVALGMVIRG ETYHFDIVAN ESARALMDLA
110 120 130 140 150
VSESLALGNG ILTVENDEQA WARARRTEGD KGGFAARAAL TMIELKQRLG

AEK
Length:153
Mass (Da):16,193
Last modified:December 1, 2001 - v1
Checksum:i8F50CA43DC559856
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591688 Genomic DNA. Translation: CAC45794.1.
RefSeqiNP_385321.1. NC_003047.1.
WP_003529297.1. NC_003047.1.

Genome annotation databases

EnsemblBacteriaiCAC45794; CAC45794; SMc01777.
GeneIDi1232859.
KEGGisme:SMc01777.
PATRICi23631733. VBISinMel96828_2627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591688 Genomic DNA. Translation: CAC45794.1.
RefSeqiNP_385321.1. NC_003047.1.
WP_003529297.1. NC_003047.1.

3D structure databases

ProteinModelPortaliQ92QU0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi266834.SMc01777.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAC45794; CAC45794; SMc01777.
GeneIDi1232859.
KEGGisme:SMc01777.
PATRICi23631733. VBISinMel96828_2627.

Phylogenomic databases

eggNOGiENOG4108UTT. Bacteria.
COG0054. LUCA.
HOGENOMiHOG000229250.
KOiK00794.
OMAiTVCNDSS.

Enzyme and pathway databases

UniPathwayiUPA00275; UER00404.
BRENDAi2.5.1.78. 5347.

Family and domain databases

Gene3Di3.40.50.960. 1 hit.
HAMAPiMF_00178. Lumazine_synth. 1 hit.
InterProiIPR002180. DMRL_synthase.
[Graphical view]
PANTHERiPTHR21058. PTHR21058. 1 hit.
PfamiPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMiSSF52121. SSF52121. 1 hit.
TIGRFAMsiTIGR00114. lumazine-synth. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiRISB1_RHIME
AccessioniPrimary (citable) accession number: Q92QU0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: December 1, 2001
Last modified: November 2, 2016
This is version 85 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, Reference 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.