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Entry: A0A1B7N3E3_9AGAM
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ID   A0A1B7N3E3_9AGAM        Unreviewed;       210 AA.
AC   A0A1B7N3E3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=K503DRAFT_799711 {ECO:0000313|EMBL:OAX39373.1};
OS   Rhizopogon vinicolor AM-OR11-026.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Suillineae; Rhizopogonaceae; Rhizopogon.
OX   NCBI_TaxID=1314800 {ECO:0000313|EMBL:OAX39373.1, ECO:0000313|Proteomes:UP000092154};
RN   [1] {ECO:0000313|EMBL:OAX39373.1, ECO:0000313|Proteomes:UP000092154}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AM-OR11-026 {ECO:0000313|EMBL:OAX39373.1,
RC   ECO:0000313|Proteomes:UP000092154};
RG   DOE Joint Genome Institute;
RA   Mujic A.B., Kuo A., Tritt A., Lipzen A., Chen C., Johnson J., Sharma A.,
RA   Barry K., Grigoriev I.V., Spatafora J.W.;
RT   "Comparative genomics of the ectomycorrhizal sister species Rhizopogon
RT   vinicolor and Rhizopogon vesiculosus (Basidiomycota: Boletales) reveals a
RT   divergence of the mating type B locus.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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; KV448252; OAX39373.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B7N3E3; -.
DR   STRING; 1314800.A0A1B7N3E3; -.
DR   InParanoid; A0A1B7N3E3; -.
DR   OrthoDB; 276496at2759; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000092154; 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   NCBIfam; TIGR00114; lumazine-synth; 1.
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:UP000092154};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003795};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003795}.
SQ   SEQUENCE   210 AA;  22027 MW;  7D163B0972982B34 CRC64;
     MSSIKGPSST HFDGSNLRIA IVHARWNKSV IDALVAGTIN KLKECGVKDS NIIIQSVPGS
     FELPFACSKV IAGSHVQAST SSGDLIGLSF GGSSTSLPST KEPPILTSTV VNMPNAPFDA
     VVAIGVLIKG STMHFEYICD SVSHALMKIQ IDTGVPVIFG VLTALTEDQA LERAGLGKGS
     EKGHNHGEDW GLAAVEMGTH SKRWAEGVFI
//
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