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6,7-dimethyl-8-ribityllumazine synthase 2 (DMRL synthase 2) (LS 2) (Lumazine synthase 2) (EC 2.5.1.78) (BLS) (Type II lumazine synthase)

 RISB2_BRUA2             Reviewed;         158 AA.
Q2YKV1;
19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
20-DEC-2005, sequence version 1.
28-MAR-2018, entry version 80.
RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 2 {ECO:0000255|HAMAP-Rule:MF_00178};
Short=DMRL synthase 2 {ECO:0000255|HAMAP-Rule:MF_00178};
Short=LS 2 {ECO:0000255|HAMAP-Rule:MF_00178};
Short=Lumazine synthase 2 {ECO:0000255|HAMAP-Rule:MF_00178};
EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178, ECO:0000269|PubMed:10482294, ECO:0000269|PubMed:16165152, ECO:0000269|PubMed:20195542};
AltName: Full=BLS {ECO:0000303|PubMed:16455994};
AltName: Full=Type II lumazine synthase {ECO:0000303|PubMed:16923880};
Name=ribH2 {ECO:0000303|PubMed:16923880, ECO:0000303|PubMed:20195542};
Synonyms=ribH-2; OrderedLocusNames=BAB2_0545;
Brucella abortus (strain 2308).
Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
Brucellaceae; Brucella.
NCBI_TaxID=359391;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=2308;
PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
"Whole-genome analyses of speciation events in pathogenic Brucellae.";
Infect. Immun. 73:8353-8361(2005).
[2]
FUNCTION, CATALYTIC ACTIVITY, BIOTECHNOLOGY, AND SUBCELLULAR LOCATION.
PubMed=10482294; DOI=10.1099/00222615-48-9-833;
Goldbaum F.A., Velikovsky C.A., Baldi P.C., Moertl S., Bacher A.,
Fossati C.A.;
"The 18-kDa cytoplasmic protein of Brucella species -- an antigen
useful for diagnosis -- is a lumazine synthase.";
J. Med. Microbiol. 48:833-839(1999).
[3]
FUNCTION, AND BIOTECHNOLOGY.
PubMed=14500496; DOI=10.1128/IAI.71.10.5750-5755.2003;
Velikovsky C.A., Goldbaum F.A., Cassataro J., Estein S., Bowden R.A.,
Bruno L., Fossati C.A., Giambartolomei G.H.;
"Brucella lumazine synthase elicits a mixed Th1-Th2 immune response
and reduces infection in mice challenged with Brucella abortus 544
independently of the adjuvant formulation used.";
Infect. Immun. 71:5750-5755(2003).
[4]
SUBUNIT, AND BIOTECHNOLOGY.
PubMed=14660615; DOI=10.1074/jbc.M312035200;
Zylberman V., Craig P.O., Klinke S., Braden B.C., Cauerhff A.,
Goldbaum F.A.;
"High order quaternary arrangement confers increased structural
stability to Brucella sp. lumazine synthase.";
J. Biol. Chem. 279:8093-8101(2004).
[5]
BIOTECHNOLOGY.
PubMed=15390265; DOI=10.1002/prot.20248;
Laplagne D.A., Zylberman V., Ainciart N., Steward M.W., Sciutto E.,
Fossati C.A., Goldbaum F.A.;
"Engineering of a polymeric bacterial protein as a scaffold for the
multiple display of peptides.";
Proteins 57:820-828(2004).
[6]
GENE NAME, AND PATHWAY.
PubMed=16923880; DOI=10.1128/JB.00207-06;
Zylberman V., Klinke S., Haase I., Bacher A., Fischer M.,
Goldbaum F.A.;
"Evolution of vitamin B2 biosynthesis: 6,7-dimethyl-8-ribityllumazine
synthases of Brucella.";
J. Bacteriol. 188:6135-6142(2006).
[7]
FUNCTION AS AN IMMUNE MODULATOR, AND BIOTECHNOLOGY.
PubMed=16455994; DOI=10.4049/jimmunol.176.4.2366;
Berguer P.M., Mundinano J., Piazzon I., Goldbaum F.A.;
"A polymeric bacterial protein activates dendritic cells via TLR4.";
J. Immunol. 176:2366-2372(2006).
[8]
FUNCTION, CATALYTIC ACTIVITY, ROLE IN VIRULENCE, GENE NAME, DISRUPTION
PHENOTYPE, MUTAGENESIS OF TRP-20, INDUCTION, AND PATHWAY.
STRAIN=2308;
PubMed=20195542; DOI=10.1371/journal.pone.0009435;
Bonomi H.R., Marchesini M.I., Klinke S., Ugalde J.E., Zylberman V.,
Ugalde R.A., Comerci D.J., Goldbaum F.A.;
"An atypical riboflavin pathway is essential for Brucella abortus
virulence.";
PLoS ONE 5:E9435-E9435(2010).
[9]
FUNCTION AS AN IMMUNE MODULATOR, AND BIOTECHNOLOGY.
PubMed=23029192; DOI=10.1371/journal.pone.0045705;
Berguer P.M., Alzogaray V.A., Rossi A.H., Mundinano J., Piazzon I.,
Goldbaum F.A.;
"A polymeric protein induces specific cytotoxicity in a TLR4 dependent
manner in the absence of adjuvants.";
PLoS ONE 7:E45705-E45705(2012).
[10]
FUNCTION AS AN IMMUNE MODULATOR, AND BIOTECHNOLOGY.
PubMed=25973756; DOI=10.1371/journal.pone.0126827;
Rossi A.H., Farias A., Fernandez J.E., Bonomi H.R., Goldbaum F.A.,
Berguer P.M.;
"Brucella spp. lumazine synthase induces a TLR4-mediated protective
response against B16 melanoma in mice.";
PLoS ONE 10:E0126827-E0126827(2015).
[11]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
PubMed=10764570; DOI=10.1006/jmbi.2000.3640;
Braden B.C., Velikovsky C.A., Cauerhff A.A., Polikarpov I.,
Goldbaum F.A.;
"Divergence in macromolecular assembly: X-ray crystallographic
structure analysis of lumazine synthase from Brucella abortus.";
J. Mol. Biol. 297:1031-1036(2000).
[12]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF APOENZYME AND IN COMPLEX
WITH SUBSTRATE ANALOG INHIBITOR AND PHOSPHATE, FUNCTION, CATALYTIC
ACTIVITY, AND KINETIC PARAMETERS.
PubMed=16165152; DOI=10.1016/j.jmb.2005.08.017;
Klinke S., Zylberman V., Vega D.R., Guimaraes B.G., Braden B.C.,
Goldbaum F.A.;
"Crystallographic studies on decameric Brucella spp. lumazine
synthase: a novel quaternary arrangement evolved for a new function?";
J. Mol. Biol. 353:124-137(2005).
-!- FUNCTION: 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
(PubMed:10482294, PubMed:16165152, PubMed:20195542). This is the
penultimate step in the biosynthesis of riboflavin. The isozyme
RibH2 but not RibH1 is essential for Brucella intracellular
survival and replication inside macrophages or in mice
(PubMed:20195542). Displays low catalytic activity in comparison
with the isozyme RibH1 (PubMed:16165152). Is a highly immunogenic
protein (PubMed:14500496). 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
(PubMed:16455994). 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 (PubMed:23029192). Elicits a TLR4-mediated protective
response against B16 melanoma in mice, slowing tumor growth and
prolonging mice survival (PubMed:25973756).
{ECO:0000269|PubMed:10482294, ECO:0000269|PubMed:14500496,
ECO:0000269|PubMed:16165152, ECO:0000269|PubMed:16455994,
ECO:0000269|PubMed:20195542, ECO:0000269|PubMed:23029192,
ECO:0000269|PubMed:25973756}.
-!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-
amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-
ribityl)lumazine + 2 H(2)O + phosphate. {ECO:0000255|HAMAP-
Rule:MF_00178, ECO:0000269|PubMed:10482294,
ECO:0000269|PubMed:16165152, ECO:0000269|PubMed:20195542}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=10 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees
Celsius and pH 7.0) {ECO:0000269|PubMed:16165152};
KM=4000 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37
degrees Celsius and pH 7.0) {ECO:0000269|PubMed:16165152};
Vmax=20 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)
{ECO:0000269|PubMed:16165152};
-!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis;
riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
ribitylamino)uracil: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00178,
ECO:0000305|PubMed:16923880, ECO:0000305|PubMed:20195542}.
-!- SUBUNIT: Homodecamer, arranged as a dimer of pentamers.
{ECO:0000269|PubMed:10764570, ECO:0000269|PubMed:14660615,
ECO:0000269|PubMed:16165152}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10482294}.
-!- INDUCTION: 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. {ECO:0000305|PubMed:20195542}.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene are not auxotrophic
for riboflavin and grow at wild-type rates in both rich and
minimal media. But simultaneous disruption of ribH1 and ribH2 is
lethal. The ribH2 mutant shows a decrease in survival and
replication in macrophages at all time-points and is attenuated in
mice. {ECO:0000269|PubMed:20195542}.
-!- BIOTECHNOLOGY: Could be useful as a specific antigen for the
serological diagnosis of active infection of both human and bovine
brucellosis (PubMed:10482294). Has been used as a protein carrier
of foreign peptides and proteins (PubMed:15390265). The described
characteristics of BLS make this protein an ideal antigen carrier
for vaccine development (PubMed:14660615, PubMed:15390265,
PubMed:16455994, PubMed:23029192, PubMed:14500496). 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 (PubMed:25973756).
{ECO:0000269|PubMed:10482294, ECO:0000269|PubMed:14500496,
ECO:0000269|PubMed:14660615, ECO:0000269|PubMed:15390265,
ECO:0000269|PubMed:16455994, ECO:0000269|PubMed:23029192,
ECO:0000269|PubMed:25973756}.
-!- SIMILARITY: Belongs to the DMRL synthase family.
{ECO:0000255|HAMAP-Rule:MF_00178}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AM040265; CAJ12711.1; -; Genomic_DNA.
RefSeq; WP_002965946.1; NZ_KN046823.1.
PDB; 1DI0; X-ray; 2.70 A; A/B/C/D/E=1-158.
PDB; 1T13; X-ray; 2.90 A; A/B/C/D/E=1-158.
PDB; 1XN1; X-ray; 3.05 A; A/B/C/D/E/F/G/H/I/J=1-158.
PDBsum; 1DI0; -.
PDBsum; 1T13; -.
PDBsum; 1XN1; -.
ProteinModelPortal; Q2YKV1; -.
SMR; Q2YKV1; -.
PRIDE; Q2YKV1; -.
EnsemblBacteria; CAJ12711; CAJ12711; BAB2_0545.
GeneID; 29595676; -.
KEGG; bmf:BAB2_0545; -.
PATRIC; fig|359391.11.peg.2737; -.
HOGENOM; HOG000229252; -.
KO; K00794; -.
OMA; PHHFHEH; -.
UniPathway; UPA00275; UER00404.
Proteomes; UP000002719; Chromosome II.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-EC.
GO; GO:0009405; P:pathogenesis; IEA:UniProtKB-KW.
GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
Gene3D; 3.40.50.960; -; 1.
HAMAP; MF_00178; Lumazine_synth; 1.
InterPro; IPR034964; LS.
InterPro; IPR002180; LS/RS.
InterPro; IPR036467; LS/RS_sf.
PANTHER; PTHR21058; PTHR21058; 1.
Pfam; PF00885; DMRL_synthase; 1.
SUPFAM; SSF52121; SSF52121; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Reference proteome;
Riboflavin biosynthesis; Transferase; Virulence.
CHAIN 1 158 6,7-dimethyl-8-ribityllumazine synthase
2.
/FTId=PRO_0000425958.
REGION 54 56 5-amino-6-(D-ribitylamino)uracil binding.
{ECO:0000305|PubMed:16165152}.
REGION 78 80 5-amino-6-(D-ribitylamino)uracil binding.
{ECO:0000305|PubMed:16165152}.
ACT_SITE 86 86 Proton donor. {ECO:0000255|HAMAP-
Rule:MF_00178}.
BINDING 20 20 5-amino-6-(D-ribitylamino)uracil.
{ECO:0000305|PubMed:16165152}.
BINDING 111 111 5-amino-6-(D-ribitylamino)uracil; via
amide nitrogen and carbonyl oxygen.
{ECO:0000305|PubMed:16165152}.
BINDING 125 125 1-deoxy-L-glycero-tetrulose 4-phosphate.
{ECO:0000255|HAMAP-Rule:MF_00178}.
MUTAGEN 20 20 W->A: Loss of enzymatic activity.
{ECO:0000269|PubMed:20195542}.
STRAND 11 18 {ECO:0000244|PDB:1DI0}.
HELIX 22 40 {ECO:0000244|PDB:1DI0}.
STRAND 43 53 {ECO:0000244|PDB:1DI0}.
HELIX 54 56 {ECO:0000244|PDB:1DI0}.
HELIX 57 66 {ECO:0000244|PDB:1DI0}.
STRAND 71 78 {ECO:0000244|PDB:1DI0}.
STRAND 83 85 {ECO:0000244|PDB:1DI0}.
HELIX 88 105 {ECO:0000244|PDB:1DI0}.
STRAND 109 114 {ECO:0000244|PDB:1DI0}.
STRAND 116 118 {ECO:0000244|PDB:1DI0}.
HELIX 123 153 {ECO:0000244|PDB:1DI0}.
SEQUENCE 158 AA; 17356 MW; EE59C2C815E53A2B CRC64;
MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD VPGAYEIPLH
AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ VQLETEVPVL SVVLTPHHFH
ESKEHHDFFH AHFKVKGVEA AHAALQIVSE RSRIAALV


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