RISB_ECOLI
ID RISB_ECOLI Reviewed; 156 AA.
AC P61714; P25540; P77114; Q2MC11;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase;
DE Short=DMRL synthase;
DE Short=LS;
DE Short=Lumazine synthase;
DE EC=2.5.1.78;
GN Name=ribE; Synonyms=ribH, ybaF; OrderedLocusNames=b0415, JW0405;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1406588; DOI=10.1007/bf00538702;
RA Taura T., Ueguchi C., Shiba K., Ito K.;
RT "Insertional disruption of the nusB (ssyB) gene leads to cold-sensitive
RT growth of Escherichia coli and suppression of the secY24 mutation.";
RL Mol. Gen. Genet. 234:429-432(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBUNIT, AND PATHWAY.
RC STRAIN=K12 / RR28;
RX PubMed=8969176; DOI=10.1074/jbc.271.52.33201;
RA Moertl S., Fischer M., Richter G., Tack J., Weinkauf S., Bacher A.;
RT "Biosynthesis of riboflavin. Lumazine synthase of Escherichia coli.";
RL J. Biol. Chem. 271:33201-33207(1996).
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:8969176}.
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:8969176};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=4.2 uM for 5-amino-6-(D-ribitylamino)uracil
CC {ECO:0000269|PubMed:8969176};
CC KM=62 uM for 3,4-dihydroxy-2-butanone 4-phosphate
CC {ECO:0000269|PubMed:8969176};
CC Vmax=11800 nmol/h/mg enzyme {ECO:0000269|PubMed:8969176};
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:0000269|PubMed:8969176}.
CC -!- SUBUNIT: Forms a hollow icosahedral capsid composed of 60 subunits,
CC probably arranged as a dodecamer of pentamers. Unlike in B.subtilis,
CC does not interact with riboflavin synthase, and the core of the
CC icosahedral capsid is empty. {ECO:0000269|PubMed:8969176}.
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; X64395; CAA45736.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40171.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73518.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76195.1; -; Genomic_DNA.
DR PIR; S26202; S26202.
DR RefSeq; NP_414949.1; NC_000913.3.
DR RefSeq; WP_001021161.1; NZ_STEB01000007.1.
DR AlphaFoldDB; P61714; -.
DR SMR; P61714; -.
DR BioGRID; 4259505; 92.
DR DIP; DIP-10711N; -.
DR IntAct; P61714; 16.
DR STRING; 511145.b0415; -.
DR SWISS-2DPAGE; P61714; -.
DR jPOST; P61714; -.
DR PaxDb; P61714; -.
DR PRIDE; P61714; -.
DR EnsemblBacteria; AAC73518; AAC73518; b0415.
DR EnsemblBacteria; BAE76195; BAE76195; BAE76195.
DR GeneID; 64296781; -.
DR GeneID; 67416510; -.
DR GeneID; 946453; -.
DR KEGG; ecj:JW0405; -.
DR KEGG; eco:b0415; -.
DR PATRIC; fig|1411691.4.peg.1862; -.
DR EchoBASE; EB1298; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_1_1_6; -.
DR InParanoid; P61714; -.
DR OMA; CQGVTQG; -.
DR PhylomeDB; P61714; -.
DR BioCyc; EcoCyc:LUMAZINESYN-MON; -.
DR BioCyc; MetaCyc:LUMAZINESYN-MON; -.
DR SABIO-RK; P61714; -.
DR UniPathway; UPA00275; UER00404.
DR PRO; PR:P61714; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IDA:EcoCyc.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
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 Reference proteome; Riboflavin biosynthesis; Transferase.
FT CHAIN 1..156
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_0000134754"
FT ACT_SITE 89
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 22
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 57..59
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 81..83
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 86..87
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 114
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 128
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
SQ SEQUENCE 156 AA; 16157 MW; 1F8504B2892195C7 CRC64;
MNIIEANVAT PDARVAITIA RFNNFINDSL LEGAIDALKR IGQVKDENIT VVWVPGAYEL
PLAAGALAKT GKYDAVIALG TVIRGGTAHF EYVAGGASNG LAHVAQDSEI PVAFGVLTTE
SIEQAIERAG TKAGNKGAEA ALTALEMINV LKAIKA
