(data stored in ACNUC10821 zone)

SWISSPROT: C8U299_ECO10

ID   C8U299_ECO10            Unreviewed;       156 AA.
AC   C8U299;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 67.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078290};
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|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078290};
GN   Name=ribE {ECO:0000313|EMBL:BAI29257.1};
GN   Synonyms=ribH {ECO:0000256|HAMAP-Rule:MF_00178};
GN   OrderedLocusNames=ECO103_0389 {ECO:0000313|EMBL:BAI29257.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29257.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29257.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(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:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078298}.
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:0000256|HAMAP-Rule:MF_00178,
CC         ECO:0000256|SAAS:SAAS01115780};
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:0000256|HAMAP-Rule:MF_00178,
CC       ECO:0000256|SAAS:SAAS01078315}.
CC   -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits,
CC       arranged as a dodecamer of pentamers. {ECO:0000256|HAMAP-
CC       Rule:MF_00178}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS00579181}.
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; AP010958; BAI29257.1; -; Genomic_DNA.
DR   RefSeq; WP_001021161.1; NC_013353.1.
DR   SMR; C8U299; -.
DR   EnsemblBacteria; BAI29257; BAI29257; ECO103_0389.
DR   KEGG; eoh:ECO103_0389; -.
DR   HOGENOM; HOG000229250; -.
DR   KO; K00794; -.
DR   OMA; HGNKGTE; -.
DR   BioCyc; ECOL585395:ECO103_RS02040-MONOMER; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000000959; 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; C8U299.
DR   SWISS-2DPAGE; C8U299.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00178,
KW   ECO:0000256|SAAS:SAAS00470718};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00178,
KW   ECO:0000256|SAAS:SAAS00106446}.
FT   REGION       57     59       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   REGION       81     83       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   REGION       86     87       1-deoxy-L-glycero-tetrulose 4-phosphate
FT                                binding. {ECO:0000256|HAMAP-Rule:
FT                                MF_00178}.
FT   ACT_SITE     89     89       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00178}.
FT   BINDING      22     22       5-amino-6-(D-ribitylamino)uracil.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   BINDING     114    114       5-amino-6-(D-ribitylamino)uracil; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   BINDING     128    128       1-deoxy-L-glycero-tetrulose 4-phosphate.
FT                                {ECO:0000256|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
//

If you have problems or comments...

PBIL Back to PBIL home page