RISB1_BRUME
ID RISB1_BRUME Reviewed; 157 AA.
AC Q8YGH2;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 1;
DE Short=DMRL synthase 1;
DE Short=LS 1;
DE Short=Lumazine synthase 1;
DE EC=2.5.1.78;
DE AltName: Full=Type I lumazine synthase;
GN Name=ribH1; OrderedLocusNames=BMEI1187;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
RN [2]
RP GENE NAME.
RX PubMed=16923880; DOI=10.1128/jb.00207-06;
RA Zylberman V., Klinke S., Haase I., Bacher A., Fischer M., Goldbaum F.A.;
RT "Evolution of vitamin B2 biosynthesis: 6,7-dimethyl-8-ribityllumazine
RT synthases of Brucella.";
RL J. Bacteriol. 188:6135-6142(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG
RP INHIBITOR, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND SUBUNIT.
RX PubMed=17854827; DOI=10.1016/j.jmb.2007.08.021;
RA Klinke S., Zylberman V., Bonomi H.R., Haase I., Guimaraes B.G.,
RA Braden B.C., Bacher A., Fischer M., Goldbaum F.A.;
RT "Structural and kinetic properties of lumazine synthase isoenzymes in the
RT order Rhizobiales.";
RL J. Mol. Biol. 373:664-680(2007).
CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by
CC condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-
CC butanone 4-phosphate. This is the penultimate step in the biosynthesis
CC of riboflavin. {ECO:0000269|PubMed:17854827}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC Evidence={ECO:0000269|PubMed:17854827};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius
CC and pH 7.0) {ECO:0000269|PubMed:17854827};
CC KM=225 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17854827};
CC Note=kcat is 0.003 sec(-1) (at 37 degrees Celsius and pH 7.0).;
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:17854827}.
CC -!- INDUCTION: The two ribH genes may be differentially expressed during
CC the Brucella infection cycle. Brucella would use RibH1 for flavin
CC biosynthesis during the extracellular phase and RibH2 during
CC intracellular growth (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE008917; AAL52368.1; -; Genomic_DNA.
DR PIR; AE3400; AE3400.
DR PDB; 2O6H; X-ray; 2.70 A; A/B/C/D/E=1-157.
DR PDBsum; 2O6H; -.
DR AlphaFoldDB; Q8YGH2; -.
DR SMR; Q8YGH2; -.
DR STRING; 224914.BMEI1187; -.
DR EnsemblBacteria; AAL52368; AAL52368; BMEI1187.
DR KEGG; bme:BMEI1187; -.
DR eggNOG; COG0054; Bacteria.
DR OMA; CQGVTQG; -.
DR UniPathway; UPA00275; UER00404.
DR EvolutionaryTrace; Q8YGH2; -.
DR Proteomes; UP000000419; Chromosome I.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR Gene3D; 3.40.50.960; -; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR PANTHER; PTHR21058; PTHR21058; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR SUPFAM; SSF52121; SSF52121; 1.
DR TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Riboflavin biosynthesis; Transferase.
FT CHAIN 1..157
FT /note="6,7-dimethyl-8-ribityllumazine synthase 1"
FT /id="PRO_0000134726"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 22
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 53..55
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 82..84
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 87..88
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 129
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2O6H"
FT HELIX 24..41
FT /evidence="ECO:0007829|PDB:2O6H"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:2O6H"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2O6H"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2O6H"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:2O6H"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:2O6H"
FT HELIX 90..108
FT /evidence="ECO:0007829|PDB:2O6H"
FT STRAND 112..122
FT /evidence="ECO:0007829|PDB:2O6H"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:2O6H"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:2O6H"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:2O6H"
SQ SEQUENCE 157 AA; 16810 MW; 657DE105E3241275 CRC64;
MEFLMSKHEA DAPHLLIVEA RFYDDLADAL LDGAKAALDE AGATYDVVTV PGALEIPATI
SFALDGADNG GTEYDGFVAL GTVIRGETYH FDIVSNESCR ALTDLSVEES IAIGNGILTV
ENEEQAWVRA RREDKDKGGF AARAALTMIG LRKKFGA
