(data stored in ACNUC7421 zone)

SWISSPROT: Q5LX59_RUEPO

ID   Q5LX59_RUEPO            Unreviewed;       245 AA.
AC   Q5LX59;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 95.
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=ribH-1 {ECO:0000313|EMBL:AAV93588.1};
GN   Synonyms=ribH {ECO:0000256|HAMAP-Rule:MF_00178};
GN   OrderedLocusNames=SPO0268 {ECO:0000313|EMBL:AAV93588.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93588.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93588.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93588.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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   -!- SIMILARITY: Belongs to the DMRL synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS00579181}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00178}.
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DR   EMBL; CP000031; AAV93588.1; -; Genomic_DNA.
DR   STRING; 246200.SPO0268; -.
DR   EnsemblBacteria; AAV93588; AAV93588; SPO0268.
DR   KEGG; sil:SPO0268; -.
DR   eggNOG; ENOG410908U; Bacteria.
DR   eggNOG; COG0054; LUCA.
DR   HOGENOM; HOG000229252; -.
DR   KO; K00794; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000001023; 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;
DR   PRODOM; Q5LX59.
DR   SWISS-2DPAGE; Q5LX59.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
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, ECO:0000313|EMBL:AAV93588.1}.
FT   REGION      141    143       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   REGION      165    167       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   ACT_SITE    173    173       Proton donor. {ECO:0000256|HAMAP-Rule:
FT                                MF_00178}.
FT   BINDING     112    112       5-amino-6-(D-ribitylamino)uracil.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   BINDING     198    198       5-amino-6-(D-ribitylamino)uracil; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   BINDING     217    217       1-deoxy-L-glycero-tetrulose 4-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
SQ   SEQUENCE   245 AA;  26405 MW;  3D79D98B3918C481 CRC64;
     MHDGPPVAPI SSCSGERSLA SSVSFSGRGE IPHRRYAGLD PASPRAAPAH VRGVSRSGER
     PEPTVTVRMK ENARPGHASA CARPFVIALG DVSKHKEITM THTRYAFIKA NWHADIVDRA
     LEGFLELIPP EQVDVYDVPG AFEMPLLARD LAQTGRYAAV ACAAFVVDGG IYRHDFVAQA
     VVDGLMRAGL DTGVPILSVS LTPHQYQETD HHNAIFRAHF VDKGREAARA ALQITATRSK
     LAQAA
//

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