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Database: UniProt
Entry: S3DBG5_GLAL2
LinkDB: S3DBG5_GLAL2
Original site: S3DBG5_GLAL2 
ID   S3DBG5_GLAL2            Unreviewed;       202 AA.
AC   S3DBG5;
DT   18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT   18-SEP-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|RuleBase:RU003795};
DE            Short=DMRL synthase {ECO:0000256|RuleBase:RU003795};
DE            EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|RuleBase:RU003795};
GN   ORFNames=GLAREA_00441 {ECO:0000313|EMBL:EPE29281.1};
OS   Glarea lozoyensis (strain ATCC 20868 / MF5171).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Helotiaceae; Glarea.
OX   NCBI_TaxID=1116229 {ECO:0000313|EMBL:EPE29281.1, ECO:0000313|Proteomes:UP000016922};
RN   [1] {ECO:0000313|EMBL:EPE29281.1, ECO:0000313|Proteomes:UP000016922}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 20868 / MF5171 {ECO:0000313|Proteomes:UP000016922};
RX   PubMed=23688303; DOI=10.1186/1471-2164-14-339;
RA   Chen L., Yue Q., Zhang X., Xiang M., Wang C., Li S., Che Y.,
RA   Ortiz-Lopez F.J., Bills G.F., Liu X., An Z.;
RT   "Genomics-driven discovery of the pneumocandin biosynthetic gene cluster in
RT   the fungus Glarea lozoyensis.";
RL   BMC Genomics 14:339-339(2013).
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:0000256|RuleBase:RU003795}.
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:0000256|ARBA:ARBA00001697,
CC         ECO:0000256|RuleBase:RU003795};
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:0000256|ARBA:ARBA00004917,
CC       ECO:0000256|RuleBase:RU003795}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family.
CC       {ECO:0000256|ARBA:ARBA00007424, ECO:0000256|RuleBase:RU003795}.
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DR   EMBL; KE145367; EPE29281.1; -; Genomic_DNA.
DR   RefSeq; XP_008083390.1; XM_008085199.1.
DR   AlphaFoldDB; S3DBG5; -.
DR   STRING; 1116229.S3DBG5; -.
DR   GeneID; 19459499; -.
DR   KEGG; glz:GLAREA_00441; -.
DR   eggNOG; KOG3243; Eukaryota.
DR   HOGENOM; CLU_089358_2_0_1; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 276496at2759; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000016922; Unassembled WGS sequence.
DR   GO; GO:0009349; C:riboflavin synthase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd09209; Lumazine_synthase-I; 1.
DR   Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 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:SF0; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE; 1.
DR   PANTHER; PTHR21058; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE; 1.
DR   Pfam; PF00885; DMRL_synthase; 2.
DR   SUPFAM; SSF52121; Lumazine synthase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000016922};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003795};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003795}.
SQ   SEQUENCE   202 AA;  20974 MW;  F713290F726D6D35 CRC64;
     MASLKGPGEA QQFDGSDLRI GIVHARWNTS IIEPLLKGTK DKLLASGVKE SNIVVQSVPG
     SWELPIACSK LFSASQVQST TTGSSLSAGD LLGSSTTDLT ALASSAPTAT GPFDALIAIG
     VLIKGETMHF EYIADAVSTG LMRVQLDTGC PLIFGLLTVL NEEQALARAG VVSGSHNHGE
     DWGLAAVELG VKRKEWAAGK IS
//
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