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Database: UniProt
Entry: A5EVR2_DICNV
LinkDB: A5EVR2_DICNV
Original site: A5EVR2_DICNV 
ID   A5EVR2_DICNV            Unreviewed;       160 AA.
AC   A5EVR2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   24-JAN-2024, entry version 103.
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   ECO:0000313|EMBL:ABQ13652.1};
GN   OrderedLocusNames=DNO_0471 {ECO:0000313|EMBL:ABQ13652.1};
OS   Dichelobacter nodosus (strain VCS1703A).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cardiobacteriales;
OC   Cardiobacteriaceae; Dichelobacter.
OX   NCBI_TaxID=246195 {ECO:0000313|EMBL:ABQ13652.1, ECO:0000313|Proteomes:UP000000248};
RN   [1] {ECO:0000313|EMBL:ABQ13652.1, ECO:0000313|Proteomes:UP000000248}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VCS1703A {ECO:0000313|EMBL:ABQ13652.1,
RC   ECO:0000313|Proteomes:UP000000248};
RX   PubMed=17468768; DOI=10.1038/nbt1302;
RA   Myers G.S., Parker D., Al-Hasani K., Kennan R.M., Seemann T., Ren Q.,
RA   Badger J.H., Selengut J.D., Deboy R.T., Tettelin H., Boyce J.D.,
RA   McCarl V.P., Han X., Nelson W.C., Madupu R., Mohamoud Y., Holley T.,
RA   Fedorova N., Khouri H., Bottomley S.P., Whittington R.J., Adler B.,
RA   Songer J.G., Rood J.I., Paulsen I.T.;
RT   "Genome sequence and identification of candidate vaccine antigens from the
RT   animal pathogen Dichelobacter nodosus.";
RL   Nat. Biotechnol. 25:569-575(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: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   -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, arranged
CC       as a dodecamer of pentamers. {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}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00178}.
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DR   EMBL; CP000513; ABQ13652.1; -; Genomic_DNA.
DR   RefSeq; WP_012030807.1; NC_009446.1.
DR   AlphaFoldDB; A5EVR2; -.
DR   STRING; 246195.DNO_0471; -.
DR   KEGG; dno:DNO_0471; -.
DR   eggNOG; COG0054; Bacteria.
DR   HOGENOM; CLU_089358_1_1_6; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 9809709at2; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000000248; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000000248};
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        93
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         27
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         61..63
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         85..87
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         90..91
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         132
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ   SEQUENCE   160 AA;  17164 MW;  099BD8F736036D84 CRC64;
     MNQEVNRIEG DFVVDESARF ALICARFNDL IVHKLETAAI DTLCRHGVKG KHIDVYYVPG
     AHELPLAAQR AAMLGKYDAI IALGAVIEGS TAHFDVVVNE QAKGLAQVAL KYDLPVITGV
     LTTHNIEQAI ERAGTKAGNK GADAARAAIE MVSLLKRMGS
//
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