RISB_XYLFT
ID RISB_XYLFT Reviewed; 154 AA.
AC Q87AS7;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178};
GN Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178}; OrderedLocusNames=PD_1744;
OS Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=183190;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Temecula1 / ATCC 700964;
RX PubMed=12533478; DOI=10.1128/jb.185.3.1018-1026.2003;
RA Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA Furlan L.R., Camargo L.E.A., da Silva A.C.R., Moon D.H., Takita M.A.,
RA Lemos E.G.M., Machado M.A., Ferro M.I.T., da Silva F.R., Goldman M.H.S.,
RA Goldman G.H., Lemos M.V.F., El-Dorry H., Tsai S.M., Carrer H.,
RA Carraro D.M., de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L.,
RA Kimura E.T., Ferro E.S., Harakava R., Kuramae E.E., Marino C.L.,
RA Giglioti E., Abreu I.L., Alves L.M.C., do Amaral A.M., Baia G.S.,
RA Blanco S.R., Brito M.S., Cannavan F.S., Celestino A.V., da Cunha A.F.,
RA Fenille R.C., Ferro J.A., Formighieri E.F., Kishi L.T., Leoni S.G.,
RA Oliveira A.R., Rosa V.E. Jr., Sassaki F.T., Sena J.A.D., de Souza A.A.,
RA Truffi D., Tsukumo F., Yanai G.M., Zaros L.G., Civerolo E.L.,
RA Simpson A.J.G., Almeida N.F. Jr., Setubal J.C., Kitajima J.P.;
RT "Comparative analyses of the complete genome sequences of Pierce's disease
RT and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL J. Bacteriol. 185:1018-1026(2003).
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:0000255|HAMAP-Rule:MF_00178}.
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:0000255|HAMAP-Rule:MF_00178};
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. {ECO:0000255|HAMAP-Rule:MF_00178}.
CC -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, arranged
CC as a dodecamer of pentamers. {ECO:0000255|HAMAP-Rule:MF_00178}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00178}.
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DR EMBL; AE009442; AAO29579.1; -; Genomic_DNA.
DR RefSeq; WP_004086411.1; NC_004556.1.
DR AlphaFoldDB; Q87AS7; -.
DR SMR; Q87AS7; -.
DR EnsemblBacteria; AAO29579; AAO29579; PD_1744.
DR GeneID; 58017269; -.
DR KEGG; xft:PD_1744; -.
DR HOGENOM; CLU_089358_1_2_6; -.
DR OMA; CQGVTQG; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000002516; Chromosome.
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 3: Inferred from homology;
KW Riboflavin biosynthesis; Transferase.
FT CHAIN 1..154
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_0000134837"
FT ACT_SITE 88
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 22
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 56..58
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 80..82
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 85..86
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 113
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 127
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ SEQUENCE 154 AA; 16165 MW; 6984994E5B3545AE CRC64;
MSHYEGDLRP AGARFVIVCS RWNARITDAL VAGACHSLVD NGVPDDAVDV VRVPGAWEIP
IVANLLAQAG QHAAIIALGC VVRGDTRHYE HVADLCAEGM MSVQMQTGVP VLNGVLAVEC
IKDAEMRAGG SHGNKGAETA LAALEMVSLL EKLP
