(data stored in ACNUC29543 zone)

SWISSPROT: RISB_SYNR3

ID   RISB_SYNR3              Reviewed;         159 AA.
AC   A5GQ24;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE            Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE            Short=LS {ECO:0000255|HAMAP-Rule:MF_00178};
DE            Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE            EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178};
GN   Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178};
GN   OrderedLocusNames=SynRCC307_0080;
OS   Synechococcus sp. (strain RCC307).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus.
OX   NCBI_TaxID=316278;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RCC307;
RG   Genoscope;
RL   Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-
CC       ribityllumazine by condensation of 5-amino-6-(D-
CC       ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate.
CC       This is the penultimate step in the biosynthesis of riboflavin.
CC       {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 +
CC         H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830;
CC         EC=2.5.1.78; Evidence={ECO:0000255|HAMAP-Rule:MF_00178};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis;
CC       riboflavin 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.
CC       {ECO:0000255|HAMAP-Rule:MF_00178}.
DR   EMBL; CT978603; CAK26983.1; -; Genomic_DNA.
DR   RefSeq; WP_011934498.1; NC_009482.1.
DR   SMR; A5GQ24; -.
DR   STRING; 316278.SynRCC307_0080; -.
DR   EnsemblBacteria; CAK26983; CAK26983; SynRCC307_0080.
DR   KEGG; syr:SynRCC307_0080; -.
DR   eggNOG; ENOG4108UTT; Bacteria.
DR   eggNOG; COG0054; LUCA.
DR   HOGENOM; HOG000229249; -.
DR   KO; K00794; -.
DR   OMA; HGNKGTE; -.
DR   OrthoDB; 1680292at2; -.
DR   BioCyc; SSP316278:G1GJL-80-MONOMER; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000001115; 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   3: Inferred from homology;
DR   PRODOM; A5GQ24.
DR   SWISS-2DPAGE; A5GQ24.
KW   Complete proteome; Reference proteome; Riboflavin biosynthesis;
KW   Transferase.
FT   CHAIN         1    159       6,7-dimethyl-8-ribityllumazine synthase.
FT                                /FTId=PRO_1000040534.
FT   REGION       61     63       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   REGION       85     87       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   REGION       90     91       1-deoxy-L-glycero-tetrulose 4-phosphate
FT                                binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00178}.
FT   ACT_SITE     93     93       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00178}.
FT   BINDING      23     23       5-amino-6-(D-ribitylamino)uracil.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   BINDING     118    118       5-amino-6-(D-ribitylamino)uracil; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   BINDING     132    132       1-deoxy-L-glycero-tetrulose 4-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
SQ   SEQUENCE   159 AA;  16815 MW;  FBB506E84A308207 CRC64;
     MTVFEGRFTD AGGLRIAVVV ARFNDLVTGK LLSGCLDCLS RHGIDVAETS SQLDLAWVPG
     SFEIPLLAKR LASSGRYDVV ITLGAVIRGD TPHFDVVVAE VSKGVAAVAR ESGVPVIFGV
     LTTDTLQQAL ERAGIKSNLG WNYGLQALEM GSLMRSVPA
//

If you have problems or comments...

PBIL Back to PBIL home page