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RISB_AZOC5
ID   RISB_AZOC5              Reviewed;         162 AA.
AC   A8I0J5;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 76.
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=AZC_1265;
OS   Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS   6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Xanthobacteraceae; Azorhizobium.
OX   NCBI_TaxID=438753;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / NCIMB
RC   13405 / ORS 571;
RA   Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA   Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA   Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT   "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT   caulinodans ORS571.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00178}.
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DR   EMBL; AP009384; BAF87263.1; -; Genomic_DNA.
DR   RefSeq; WP_012169796.1; NC_009937.1.
DR   AlphaFoldDB; A8I0J5; -.
DR   SMR; A8I0J5; -.
DR   STRING; 438753.AZC_1265; -.
DR   EnsemblBacteria; BAF87263; BAF87263; AZC_1265.
DR   KEGG; azc:AZC_1265; -.
DR   eggNOG; COG0054; Bacteria.
DR   HOGENOM; CLU_089358_1_2_5; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 1680292at2; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000000270; 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   Reference proteome; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..162
FT                   /note="6,7-dimethyl-8-ribityllumazine synthase"
FT                   /id="PRO_1000071642"
FT   ACT_SITE        95
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         27
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         58..60
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         87..89
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         92..93
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         120
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         134
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ   SEQUENCE   162 AA;  16778 MW;  3F264E3F3E4DA2A2 CRC64;
     MVSTRKEGAS AGEPVTGARV LIVEGRYYEA LADELLAGAR AALEAAGATV DVITVPGALE
     IPIAAEIALE AAEEEDEPYE AVVALGCVIR GETYHFEIVA GESSRGLMDL ALAHALPLGN
     GILTVETEAQ AWERARVGEG NKGGGAAEAA LSLVRLKRRG LK
 
 
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