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 abortus biovar 1 (strain 9-941)
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. Displays low catalytic activity in comparison with the isozyme RibH1. Is a highly immunogenic protein. Activates dendritic cells (DCs) in vitro, increasing the levels of costimulatory molecules and the secretion of proinflammatory cytokines, and recruits DCs, B cells and CD8+ T cells in vivo, both effects in a TLR4-dependent manner. Induces the cross presentation of covalently attached peptides and generates a strong and long-lasting humoral immune response without adjuvants; TLR4 signaling is necessary for the induction of the cytotoxic response but not for antigen cross presentation. Elicits a TLR4-mediated protective response against B16 melanoma in mice, slowing tumor growth and prolonging mice survival.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.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 sitei205-amino-6-(D-ribitylamino)uracilUniRule annotation1
Active sitei86Proton donorUniRule annotation1
Binding sitei1115-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygenUniRule annotation1
Binding sitei1251-deoxy-L-glycero-tetrulose 4-phosphateUniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionTransferase
Biological processRiboflavin biosynthesis

Enzyme and pathway databases

BRENDAi2.5.1.78 994
UniPathwayiUPA00275; UER00404

Names & Taxonomyi

Protein namesi
Recommended name:
6,7-dimethyl-8-ribityllumazine synthase 2UniRule annotation (EC:2.5.1.78UniRule annotation)
Short name:
DMRL synthase 2UniRule annotation
Short name:
LS 2UniRule annotation
Short name:
Lumazine synthase 2UniRule annotation
Alternative name(s):
BLSBy similarity
Type II lumazine synthaseBy similarity
Gene namesi
Name:ribH2
Synonyms:ribH, ribH-2
Ordered Locus Names:BruAb2_0535
OrganismiBrucella abortus biovar 1 (strain 9-941)
Taxonomic identifieri262698 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000540 Componenti: Chromosome II

Subcellular locationi

  • Cytoplasm By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Biotechnological usei

Could be useful as a specific antigen for the serological diagnosis of active infection of both human and bovine brucellosis. Has been used as a protein carrier of foreign peptides and proteins. The described characteristics of BLS make this protein an ideal antigen carrier for vaccine development. The antitumor effect of BLS could lead to a therapeutic strategy utilizing a TLR4 ligand; as the expression of TLR4 has been reported on a large number of tumors, BLS signaling via TLR4 could make a notable contribution to the success of cancer treatment when coadministered with other cancer vaccines or treatments like radiation or chemotherapy.By similarity

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001347251 – 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

Interactioni

Subunit structurei

Homodecamer, arranged as a dimer of pentamers.By similarity

Structurei

3D structure databases

ProteinModelPortaliP61711
SMRiP61711
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61711

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni54 – 565-amino-6-(D-ribitylamino)uracil bindingUniRule annotation3
Regioni78 – 805-amino-6-(D-ribitylamino)uracil bindingUniRule annotation3

Sequence similaritiesi

Belongs to the DMRL synthase family.UniRule annotation

Phylogenomic databases

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.

P61711-1 [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
Z46864 Genomic DNA Translation: CAA86936.1
AE017224 Genomic DNA Translation: AAX75953.1
PIRiS49918
RefSeqiWP_002965946.1, NC_006933.1

Genome annotation databases

EnsemblBacteriaiAAX75953; AAX75953; BruAb2_0535
GeneIDi29595676
KEGGibmb:BruAb2_0535

Similar proteinsi

Entry informationi

Entry nameiRISB2_BRUAB
AccessioniPrimary (citable) accession number: P61711
Secondary accession number(s): Q44668, Q578I1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: March 28, 2018
This is version 94 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health