ID A0A9Q3BYZ9_9BASI Unreviewed; 257 AA.
AC A0A9Q3BYZ9;
DT 13-SEP-2023, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2023, sequence version 1.
DT 28-JAN-2026, entry version 9.
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=O181_013598 {ECO:0000313|EMBL:MBW0473883.1};
OS Austropuccinia psidii MF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Sphaerophragmiaceae; Austropuccinia.
OX NCBI_TaxID=1389203 {ECO:0000313|EMBL:MBW0473883.1, ECO:0000313|Proteomes:UP000765509};
RN [1] {ECO:0000313|EMBL:MBW0473883.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MF-1 {ECO:0000313|EMBL:MBW0473883.1};
RA Quecine M.C., Pachon D.M.R., Bonatelli M.L., Correr F.H.,
RA Franceschini L.M., Leite T.F., Margarido G.R.A., Almeida C.A.,
RA Ferrarezi J.A., Labate C.A.;
RT "Draft genome sequence of rust myrtle Austropuccinia psidii MF-1, a
RT brazilian biotype.";
RL Submitted (MAR-2021) 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 +
CC phosphate + 2 H2O + H(+); 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:ARBA00048785,
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:MBW0473883.1}.
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DR EMBL; AVOT02003567; MBW0473883.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A9Q3BYZ9; -.
DR OrthoDB; 2965at2759; -.
DR Proteomes; UP000765509; Unassembled WGS sequence.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:TreeGrafter.
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-KW.
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; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000765509};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003795}.
SQ SEQUENCE 257 AA; 28230 MW; 536B6F9118E8563C CRC64;
MKSNHLGSWG SFGNGGLHVA CTCKKCVPST LLSACWLFSV GDKTSETQLE PTSFARSNAR
MKDNQHQGLE YAFLNQLPTS KPLQDLCKSL RILIVHTRWN QPIIDSLVQT AIETLTSSPI
NLQRQNVLIE SVVGSYELPW MCNAVLSNSD FHKNIDAIIS IGVLIKGETM HFEYIADSVS
TNLTKVSIDH NKPIIFGVLT CLNQDQALER AGLGSSPNSE SLAIGWAKTA VDCAIKGRWS
PTSFARQYTL MTPKDSS
//
