ID D7DBA1_STAHD Unreviewed; 150 AA.
AC D7DBA1;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|HAMAP-Rule:MF_00178};
GN Name=ribH {ECO:0000256|HAMAP-Rule:MF_00178};
GN OrderedLocusNames=Shell_0315 {ECO:0000313|EMBL:ADI31448.1};
OS Staphylothermus hellenicus (strain DSM 12710 / JCM 10830 / BK20S6-10-b1 /
OS P8).
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Staphylothermus.
OX NCBI_TaxID=591019 {ECO:0000313|EMBL:ADI31448.1, ECO:0000313|Proteomes:UP000002573};
RN [1] {ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Larimer F.,
RA Land M., Hauser L., Kyrpides N., Mikhailova N., Anderson I.J., Woyke T.;
RT "Complete sequence of Staphylothermus hellenicus DSM 12710.";
RL Submitted (MAY-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADI31448.1, ECO:0000313|Proteomes:UP000002573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12710 / JCM 10830 / BK20S6-10-b1 / P8
RC {ECO:0000313|Proteomes:UP000002573};
RX PubMed=22180806; DOI=10.4056/sigs.2054696;
RA Anderson I., Wirth R., Lucas S., Copeland A., Lapidus A., Cheng J.F.,
RA Goodwin L., Pitluck S., Davenport K., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Pati A., Mikhailova N., Woyke T., Klenk H.P.,
RA Kyrpides N., Ivanova N.;
RT "Complete genome sequence of Staphylothermus hellenicus P8.";
RL Stand. Genomic Sci. 5:12-20(2011).
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:0000256|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:0000256|ARBA:ARBA00001697, ECO:0000256|HAMAP-
CC 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:0000256|ARBA:ARBA00004917,
CC ECO:0000256|HAMAP-Rule:MF_00178}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424, ECO:0000256|HAMAP-Rule:MF_00178}.
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DR EMBL; CP002051; ADI31448.1; -; Genomic_DNA.
DR RefSeq; WP_013142646.1; NC_014205.1.
DR AlphaFoldDB; D7DBA1; -.
DR STRING; 591019.Shell_0315; -.
DR GeneID; 9233604; -.
DR KEGG; shc:Shell_0315; -.
DR eggNOG; arCOG01323; Archaea.
DR HOGENOM; CLU_089358_3_1_2; -.
DR OrthoDB; 7610at2157; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000002573; 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; cd09211; Lumazine_synthase_archaeal; 1.
DR Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR NCBIfam; TIGR00114; lumazine-synth; 1.
DR PANTHER; PTHR21058:SF0; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE; 1.
DR PANTHER; PTHR21058; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
PE 3: Inferred from homology;
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00178}.
FT ACT_SITE 75
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 11
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 43..45
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 67..69
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 72..73
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 100
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 115
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ SEQUENCE 150 AA; 16566 MW; D80C2423339E2AE7 CRC64;
MARIGIVVSE FNYDITYLML QKALSHAKFL GLEVTYVFKV PGTYEIPFAV ASLLKRNDVD
GVVALGAVIK GATKHDELVA GQTARKLMDL MIQYGKPVGL GIIGPGATRM QALERVEDYA
RRAVEAVAKM INRSRSLEEK KFTSETVFIE
//
