RISB2_BRUME
ID RISB2_BRUME Reviewed; 158 AA.
AC P61712; Q44668;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 2;
DE Short=DMRL synthase 2;
DE Short=LS 2;
DE Short=Lumazine synthase 2;
DE EC=2.5.1.78;
DE AltName: Full=Type II lumazine synthase;
GN Name=ribH2; OrderedLocusNames=BMEII0589;
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).
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 (By similarity). {ECO:0000250}.
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 -!- 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: Homodecamer, arranged as a dimer of pentamers. {ECO:0000250}.
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}.
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DR EMBL; AE008918; AAL53831.1; -; Genomic_DNA.
DR PIR; AD3583; AD3583.
DR RefSeq; WP_002965946.1; NZ_GG703779.1.
DR AlphaFoldDB; P61712; -.
DR SMR; P61712; -.
DR STRING; 224914.BMEII0589; -.
DR EnsemblBacteria; AAL53831; AAL53831; BMEII0589.
DR GeneID; 45126031; -.
DR GeneID; 55592351; -.
DR KEGG; bme:BMEII0589; -.
DR PATRIC; fig|224914.52.peg.2784; -.
DR eggNOG; COG0054; Bacteria.
DR OMA; PHHFHEH; -.
DR PhylomeDB; P61712; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000000419; Chromosome II.
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 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.
PE 3: Inferred from homology;
KW Riboflavin biosynthesis; Transferase.
FT CHAIN 1..158
FT /note="6,7-dimethyl-8-ribityllumazine synthase 2"
FT /id="PRO_0000134727"
FT ACT_SITE 86
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 20
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 54..56
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 78..80
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 111
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 125
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
SQ SEQUENCE 158 AA; 17356 MW; EE59C2C815E53A2B CRC64;
MNQSCPNKTS FKIAFIQARW HADIVDEARK SFVAELAAKT GGSVEVEIFD VPGAYEIPLH
AKTLARTGRY AAIVGAAFVI DGGIYRHDFV ATAVINGMMQ VQLETEVPVL SVVLTPHHFH
ESKEHHDFFH AHFKVKGVEA AHAALQIVSE RSRIAALV
