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 2

Gene

ribH2

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Status
Reviewed-Annotation score: -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 (By similarity).By similarity

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.

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.
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 sitei205-amino-6-(D-ribitylamino)uracilBy similarity1
Active sitei86Proton donorSequence analysis1
Binding sitei1115-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei1251-deoxy-L-glycero-tetrulose 4-phosphateBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processRiboflavin biosynthesis

Enzyme and pathway databases

UniPathwayiUPA00275; UER00404

Names & Taxonomyi

Protein namesi
Recommended name:
6,7-dimethyl-8-ribityllumazine synthase 2 (EC:2.5.1.78)
Short name:
DMRL synthase 2
Short name:
LS 2
Short name:
Lumazine synthase 2
Alternative name(s):
Type II lumazine synthase
Gene namesi
Name:ribH2
Ordered Locus Names:BMEII0589
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome II

Subcellular locationi

GO - Cellular componenti

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001347271 – 1586,7-dimethyl-8-ribityllumazine synthase 2Add BLAST158

Expressioni

Inductioni

The two ribH genes may be differentially expressed during the Brucella infection cycle. Brucella would use RibH1 for flavin biosynthesis during the extracellular phase and RibH2 during intracellular growth (By similarity).By similarity

Interactioni

Subunit structurei

Homodecamer, arranged as a dimer of pentamers.By similarity

Protein-protein interaction databases

STRINGi224914.BAWG_1983

Structurei

3D structure databases

ProteinModelPortaliP61712
SMRiP61712
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 565-amino-6-(D-ribitylamino)uracil bindingBy similarity3
Regioni78 – 805-amino-6-(D-ribitylamino)uracil bindingBy similarity3

Sequence similaritiesi

Belongs to the DMRL synthase family.Curated

Phylogenomic databases

eggNOGiENOG410908U Bacteria
COG0054 LUCA
HOGENOMiHOG000229252
KOiK00794
OMAiPHHFHEH

Family and domain databases

Gene3Di3.40.50.960, 1 hit
HAMAPiMF_00178 Lumazine_synth, 1 hit
InterProiView protein in InterPro
IPR034964 LS
IPR002180 LS/RS
IPR036467 LS/RS_sf
PANTHERiPTHR21058 PTHR21058, 1 hit
PfamiView protein in Pfam
PF00885 DMRL_synthase, 1 hit
SUPFAMiSSF52121 SSF52121, 1 hit

Sequencei

Sequence statusi: Complete.

P61712-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD
60 70 80 90 100
VPGAYEIPLH AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ
110 120 130 140 150
VQLETEVPVL SVVLTPHHFH ESKEHHDFFH AHFKVKGVEA AHAALQIVSE

RSRIAALV
Length:158
Mass (Da):17,356
Last modified:June 7, 2004 - v1
Checksum:iEE59C2C815E53A2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008918 Genomic DNA Translation: AAL53831.1
PIRiAD3583
RefSeqiWP_002965946.1, NZ_GG703779.1

Genome annotation databases

EnsemblBacteriaiAAL53831; AAL53831; BMEII0589
GeneIDi29595676
KEGGibme:BMEII0589
bmel:DK63_2656
PATRICifig|224914.52.peg.2784

Similar proteinsi

Entry informationi

Entry nameiRISB2_BRUME
AccessioniPrimary (citable) accession number: P61712
Secondary accession number(s): Q44668
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: March 28, 2018
This is version 81 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. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

Cookie policy

We would like to use anonymized google analytics cookies to gather statistics on how uniprot.org is used in aggregate. Learn more

UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health