RISB_HAEDU
ID RISB_HAEDU Reviewed; 153 AA.
AC Q7VM44;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=HD_1165;
OS Haemophilus ducreyi (strain 35000HP / ATCC 700724).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=233412;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=35000HP / ATCC 700724;
RA Munson R.S. Jr., Ray W.C., Mahairas G., Sabo P., Mungur R., Johnson L.,
RA Nguyen D., Wang J., Forst C., Hood L.;
RT "The complete genome sequence of Haemophilus ducreyi.";
RL Submitted (JUN-2003) 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 -!- 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; AE017143; AAP96019.1; -; Genomic_DNA.
DR RefSeq; WP_010945068.1; NC_002940.2.
DR AlphaFoldDB; Q7VM44; -.
DR SMR; Q7VM44; -.
DR STRING; 233412.HD_1165; -.
DR EnsemblBacteria; AAP96019; AAP96019; HD_1165.
DR KEGG; hdu:HD_1165; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_1_1_6; -.
DR OMA; CQGVTQG; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000001022; 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..153
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_0000134760"
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 153 AA; 16045 MW; 346D0AD3093E25EF CRC64;
MAKITGNLVA TGLKFSIVTA RFNDFINDKL LSGAVDTLVR HGAVESDIDT VWVPGAFEIP
LVAKKMAESG KYDAVICLGT VIRGSTTHYD YVCNEVAKGI GAVALQTGVP IMFGVLTTES
IEQAIERAGT KAGNKGAECA LGAIEMVNVL KAL
