(data stored in SCRATCH3701 zone)

SWISSPROT: RISB_SYNS3

ID   RISB_SYNS3              Reviewed;         160 AA.
AC   Q0IE03;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   11-DEC-2019, entry version 84.
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}; OrderedLocusNames=sync_0081;
OS   Synechococcus sp. (strain CC9311).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=64471;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CC9311;
RX   PubMed=16938853; DOI=10.1073/pnas.0602963103;
RA   Palenik B., Ren Q., Dupont C.L., Myers G.S., Heidelberg J.F., Badger J.H.,
RA   Madupu R., Nelson W.C., Brinkac L.M., Dodson R.J., Durkin A.S.,
RA   Daugherty S.C., Sullivan S.A., Khouri H., Mohamoud Y., Halpin R.,
RA   Paulsen I.T.;
RT   "Genome sequence of Synechococcus CC9311: insights into adaptation to a
RT   coastal environment.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:13555-13559(2006).
CC   -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by
CC       condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-
CC       butanone 4-phosphate. This is the penultimate step in the biosynthesis
CC       of riboflavin. {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 + H(+) + 2
CC         H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00178};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC       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. {ECO:0000255|HAMAP-
CC       Rule:MF_00178}.
DR   EMBL; CP000435; ABI46309.1; -; Genomic_DNA.
DR   RefSeq; WP_011618069.1; NC_008319.1.
DR   SMR; Q0IE03; -.
DR   STRING; 64471.sync_0081; -.
DR   PRIDE; Q0IE03; -.
DR   EnsemblBacteria; ABI46309; ABI46309; sync_0081.
DR   KEGG; syg:sync_0081; -.
DR   eggNOG; ENOG4108UTT; Bacteria.
DR   eggNOG; COG0054; LUCA.
DR   HOGENOM; HOG000229249; -.
DR   KO; K00794; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 1680292at2; -.
DR   BioCyc; SSP64471:G1G72-84-MONOMER; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000001961; 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; Q0IE03.
DR   SWISS-2DPAGE; Q0IE03.
KW   Reference proteome; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..160
FT                   /note="6,7-dimethyl-8-ribityllumazine synthase"
FT                   /id="PRO_1000040535"
FT   REGION          61..63
FT                   /note="5-amino-6-(D-ribitylamino)uracil binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   REGION          85..87
FT                   /note="5-amino-6-(D-ribitylamino)uracil binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   REGION          90..91
FT                   /note="1-deoxy-L-glycero-tetrulose 4-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   ACT_SITE        93
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         23
FT                   /note="5-amino-6-(D-ribitylamino)uracil"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         118
FT                   /note="5-amino-6-(D-ribitylamino)uracil; via amide nitrogen
FT                   and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT   BINDING         132
FT                   /note="1-deoxy-L-glycero-tetrulose 4-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
SQ   SEQUENCE   160 AA;  16987 MW;  D9D9FE8C3B4B1245 CRC64;
     MATFEGRFTD LGQVRIAVVV ARFNDLVTAK LLSGCLDCLS RHGVDTTAES SQLDVAWVPG
     SFELPLVSQN LARSGLYQVV ITLGAVIRGD TPHFDVVVAE ASKGIAAVAR DTGVPVIFGV
     LTTDTMQQAL ERAGIKSNLG WSYGLEALEM ASLMKVLPGH
//

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