(data stored in ACNUC7421 zone)

SWISSPROT: RISB_ECO27

ID   RISB_ECO27              Reviewed;         156 AA.
AC   B7UJN8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   08-MAY-2019, entry version 60.
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=E2348C_0350;
OS   Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=574521;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E2348/69 / EPEC;
RX   PubMed=18952797; DOI=10.1128/JB.01238-08;
RA   Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T.,
RA   Henderson I.R., Harris D., Asadulghani M., Kurokawa K., Dean P.,
RA   Kenny B., Quail M.A., Thurston S., Dougan G., Hayashi T., Parkhill J.,
RA   Frankel G.;
RT   "Complete genome sequence and comparative genome analysis of
RT   enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL   J. Bacteriol. 191:347-354(2009).
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   -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits,
CC       arranged as a dodecamer of pentamers. {ECO:0000255|HAMAP-
CC       Rule:MF_00178}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00178}.
DR   EMBL; FM180568; CAS07898.1; -; Genomic_DNA.
DR   RefSeq; WP_001021161.1; NC_011601.1.
DR   SMR; B7UJN8; -.
DR   EnsemblBacteria; CAS07898; CAS07898; E2348C_0350.
DR   KEGG; ecg:E2348C_0350; -.
DR   KO; K00794; -.
DR   OMA; HGNKGTE; -.
DR   BioCyc; ECOL574521:E2348C_RS01840-MONOMER; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000008205; 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; B7UJN8.
DR   SWISS-2DPAGE; B7UJN8.
KW   Complete proteome; Riboflavin biosynthesis; Transferase.
FT   CHAIN         1    156       6,7-dimethyl-8-ribityllumazine synthase.
FT                                /FTId=PRO_1000195484.
FT   REGION       57     59       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   REGION       81     83       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   REGION       86     87       1-deoxy-L-glycero-tetrulose 4-phosphate
FT                                binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00178}.
FT   ACT_SITE     89     89       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00178}.
FT   BINDING      22     22       5-amino-6-(D-ribitylamino)uracil.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   BINDING     114    114       5-amino-6-(D-ribitylamino)uracil; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
FT   BINDING     128    128       1-deoxy-L-glycero-tetrulose 4-phosphate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00178}.
SQ   SEQUENCE   156 AA;  16157 MW;  1F8504B2892195C7 CRC64;
     MNIIEANVAT PDARVAITIA RFNNFINDSL LEGAIDALKR IGQVKDENIT VVWVPGAYEL
     PLAAGALAKT GKYDAVIALG TVIRGGTAHF EYVAGGASNG LAHVAQDSEI PVAFGVLTTE
     SIEQAIERAG TKAGNKGAEA ALTALEMINV LKAIKA
//

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