ID S8EF26_9LAMI Unreviewed; 157 AA.
AC S8EF26;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 13-SEP-2023, entry version 28.
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};
DE Flags: Fragment;
GN ORFNames=M569_00144 {ECO:0000313|EMBL:EPS74613.1};
OS Genlisea aurea.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Lentibulariaceae; Genlisea.
OX NCBI_TaxID=192259 {ECO:0000313|EMBL:EPS74613.1, ECO:0000313|Proteomes:UP000015453};
RN [1] {ECO:0000313|EMBL:EPS74613.1, ECO:0000313|Proteomes:UP000015453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23855885;
RA Leushkin E.V., Sutormin R.A., Nabieva E.R., Penin A.A., Kondrashov A.S.,
RA Logacheva M.D.;
RT "The miniature genome of a carnivorous plant Genlisea aurea contains a low
RT number of genes and short non-coding sequences.";
RL BMC Genomics 14:476-476(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}.
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:EPS74613.1}.
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DR EMBL; AUSU01000024; EPS74613.1; -; Genomic_DNA.
DR AlphaFoldDB; S8EF26; -.
DR OrthoDB; 276496at2759; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000015453; 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; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000015453};
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW ECO:0000256|RuleBase:RU003795};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003795}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EPS74613.1"
FT NON_TER 157
FT /evidence="ECO:0000313|EMBL:EPS74613.1"
SQ SEQUENCE 157 AA; 16348 MW; E8A6BC11699798D7 CRC64;
AVRQLAGSLT AAEGMRFAIV VARFNEFITE PLLKGALATF KQYSVKEEDI DVVWVPGSFE
IGIVAAQLGK SGKYQAVVCI GAVIRGDTSH YDAVVNSAAS GVLSAGLSSG VPCIFGVLTC
DTMEQAINRA GGKSGNKGSE AAITAIQMAS LFEHHLK
//
