(data stored in SCRATCH zone)

SWISSPROT: A8LGD1_FRASN

ID   A8LGD1_FRASN            Unreviewed;       156 AA.
AC   A8LGD1;
DT   04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT   04-DEC-2007, sequence version 1.
DT   08-MAY-2019, entry version 74.
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 {ECO:0000256|HAMAP-Rule:MF_00178};
GN   OrderedLocusNames=Franean1_0404 {ECO:0000313|EMBL:ABW09870.1};
OS   Frankia sp. (strain EAN1pec).
OC   Bacteria; Actinobacteria; Frankiales; Frankiaceae; Frankia.
OX   NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW09870.1, ECO:0000313|Proteomes:UP000001313};
RN   [1] {ECO:0000313|Proteomes:UP000001313}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EAN1pec {ECO:0000313|Proteomes:UP000001313};
RX   PubMed=17151343; DOI=10.1101/gr.5798407;
RA   Normand P., Lapierre P., Tisa L.S., Gogarten J.P., Alloisio N.,
RA   Bagnarol E., Bassi C.A., Berry A.M., Bickhart D.M., Choisne N.,
RA   Couloux A., Cournoyer B., Cruveiller S., Daubin V., Demange N.,
RA   Francino M.P., Goltsman E., Huang Y., Kopp O.R., Labarre L.,
RA   Lapidus A., Lavire C., Marechal J., Martinez M., Mastronunzio J.E.,
RA   Mullin B.C., Niemann J., Pujic P., Rawnsley T., Rouy Z.,
RA   Schenowitz C., Sellstedt A., Tavares F., Tomkins J.P., Vallenet D.,
RA   Valverde C., Wall L.G., Wang Y., Medigue C., Benson D.R.;
RT   "Genome characteristics of facultatively symbiotic Frankia sp. strains
RT   reflect host range and host plant biogeography.";
RL   Genome Res. 17:7-15(2007).
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}.
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; CP000820; ABW09870.1; -; Genomic_DNA.
DR   RefSeq; WP_012157846.1; NC_009921.1.
DR   STRING; 298653.Franean1_0404; -.
DR   EnsemblBacteria; ABW09870; ABW09870; Franean1_0404.
DR   KEGG; fre:Franean1_0404; -.
DR   eggNOG; ENOG410908U; Bacteria.
DR   eggNOG; COG0054; LUCA.
DR   HOGENOM; HOG000229252; -.
DR   KO; K00794; -.
DR   OMA; PHHFHEH; -.
DR   OrthoDB; 1680292at2; -.
DR   BioCyc; FSP298653:G1G9X-402-MONOMER; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000001313; 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; A8LGD1.
DR   SWISS-2DPAGE; A8LGD1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001313};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001313};
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       54     56       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   REGION       78     80       5-amino-6-(D-ribitylamino)uracil binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   ACT_SITE     86     86       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     111    111       5-amino-6-(D-ribitylamino)uracil; via
FT                                amide nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
FT   BINDING     125    125       1-deoxy-L-glycero-tetrulose 4-phosphate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00178}.
SQ   SEQUENCE   156 AA;  16805 MW;  166018D689117117 CRC64;
     MPSTPTGARP DTVRVAIVAA RWHADIVGQA VASFRSALAE RGVGEVDEYQ VPGAFEIPLH
     TRRLALTGRY DAIATCAFVV DGGIYRHDFV AGTVVDALMR VQLDTDVPVF SAVLTPQAFH
     EHAEHQEFFA RHFQVKGREL ADAVVTTIAG LAALPA
//

If you have problems or comments...

PBIL Back to PBIL home page