RISB2_RHIME
ID RISB2_RHIME Reviewed; 157 AA.
AC Q92NI1;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 2 {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase 2 {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=LS 2 {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase 2 {ECO:0000255|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178};
GN Name=ribH2 {ECO:0000255|HAMAP-Rule:MF_00178}; OrderedLocusNames=R02221;
GN ORFNames=SMc01609;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC46800.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL591688; CAC46800.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_386327.1; NC_003047.1.
DR RefSeq; WP_013844648.1; NC_003047.1.
DR AlphaFoldDB; Q92NI1; -.
DR SMR; Q92NI1; -.
DR STRING; 266834.SMc01609; -.
DR EnsemblBacteria; CAC46800; CAC46800; SMc01609.
DR GeneID; 61603685; -.
DR KEGG; sme:SMc01609; -.
DR PATRIC; fig|266834.11.peg.3690; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_0_0_5; -.
DR BRENDA; 2.5.1.78; 5347.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000001976; 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 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.
PE 3: Inferred from homology;
KW Reference proteome; Riboflavin biosynthesis; Transferase.
FT CHAIN 1..157
FT /note="6,7-dimethyl-8-ribityllumazine synthase 2"
FT /id="PRO_0000134795"
FT ACT_SITE 84
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 18
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 52..54
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 76..78
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 109
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ SEQUENCE 157 AA; 16935 MW; 90FA9171C982C039 CRC64;
MTILSHPSAK IAIVRARWHA DIVDRCVDAF VAQWTKLGGS AADVEIFDVP GALEIPLHAQ
ALARTGRYAA ILGTAFVVNG GIYRHDFVSG TVLDGMMRVQ LDTDVPVLSA VLTPHNFQES
EPLIAFFRDH FVVKGEEAAN ACAQILDARA KLALVDA
