RISB1_RHILO
ID RISB1_RHILO Reviewed; 164 AA.
AC Q983B0;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 1;
DE Short=DMRL synthase 1;
DE Short=LS 1;
DE Short=Lumazine synthase 1;
DE EC=2.5.1.78;
DE AltName: Full=Type I lumazine synthase;
GN Name=ribH1; Synonyms=ribH; OrderedLocusNames=mlr8409;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
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).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND SUBUNIT.
RX PubMed=17854827; DOI=10.1016/j.jmb.2007.08.021;
RA Klinke S., Zylberman V., Bonomi H.R., Haase I., Guimaraes B.G.,
RA Braden B.C., Bacher A., Fischer M., Goldbaum F.A.;
RT "Structural and kinetic properties of lumazine synthase isoenzymes in the
RT order Rhizobiales.";
RL J. Mol. Biol. 373:664-680(2007).
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:0000269|PubMed:17854827}.
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:0000269|PubMed:17854827};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=2.5 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius
CC and pH 7.0) {ECO:0000269|PubMed:17854827};
CC KM=15 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:17854827};
CC Note=kcat is 0.040 sec(-1) (at 37 degrees Celsius and pH 7.0).;
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: Homopentamer. {ECO:0000269|PubMed:17854827}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BA000012; BAB54296.1; -; Genomic_DNA.
DR RefSeq; WP_010915596.1; NC_002678.2.
DR AlphaFoldDB; Q983B0; -.
DR SMR; Q983B0; -.
DR STRING; 266835.14027703; -.
DR EnsemblBacteria; BAB54296; BAB54296; BAB54296.
DR KEGG; mlo:mlr8409; -.
DR PATRIC; fig|266835.9.peg.6724; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_1_2_5; -.
DR OMA; CQGVTQG; -.
DR OrthoDB; 1680292at2; -.
DR BRENDA; 2.5.1.78; 3243.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000000552; 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 1: Evidence at protein level;
KW Riboflavin biosynthesis; Transferase.
FT CHAIN 1..164
FT /note="6,7-dimethyl-8-ribityllumazine synthase 1"
FT /id="PRO_0000134793"
FT ACT_SITE 95
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 27
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 58..60
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 87..89
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 92..93
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 134
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
SQ SEQUENCE 164 AA; 17196 MW; 9C9A7FADE8DC7C3C CRC64;
MAGISQHGKA FIRPKAKAHL LIVEARFHDD LADALLDGAT SALEEAGATY DVVTVPGSLE
IPAVITFALD GAAEGGTNYD GFVALGTIIR GDTYHFDIVA NESSRALMDM SVQDSVCIGN
GILTTENDAQ AWTRAKRSEG DKGGFAARAA LTMIALKEQL GARS
