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Database: UniProt
Entry: V4N1Q0_EUTSA
LinkDB: V4N1Q0_EUTSA
Original site: V4N1Q0_EUTSA 
ID   V4N1Q0_EUTSA            Unreviewed;       227 AA.
AC   V4N1Q0;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=EUTSA_v10001807mg {ECO:0000313|EMBL:ESQ39031.1};
OS   Eutrema salsugineum (Saltwater cress) (Sisymbrium salsugineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Eutremeae; Eutrema.
OX   NCBI_TaxID=72664 {ECO:0000313|EMBL:ESQ39031.1, ECO:0000313|Proteomes:UP000030689};
RN   [1] {ECO:0000313|EMBL:ESQ39031.1, ECO:0000313|Proteomes:UP000030689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23518688; DOI=10.3389/fpls.2013.00046;
RA   Yang R., Jarvis D.E., Chen H., Beilstein M.A., Grimwood J., Jenkins J.,
RA   Shu S., Prochnik S., Xin M., Ma C., Schmutz J., Wing R.A.,
RA   Mitchell-Olds T., Schumaker K.S., Wang X.;
RT   "The Reference Genome of the Halophytic Plant Eutrema salsugineum.";
RL   Front. Plant Sci. 4:46-46(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; KI517481; ESQ39031.1; -; Genomic_DNA.
DR   RefSeq; XP_006397578.1; XM_006397515.1.
DR   AlphaFoldDB; V4N1Q0; -.
DR   STRING; 72664.V4N1Q0; -.
DR   EnsemblPlants; ESQ39031; ESQ39031; EUTSA_v10001807mg.
DR   GeneID; 18015610; -.
DR   Gramene; ESQ39031; ESQ39031; EUTSA_v10001807mg.
DR   KEGG; eus:EUTSA_v10001807mg; -.
DR   eggNOG; KOG3243; Eukaryota.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 276496at2759; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000030689; 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:0042802; F:identical protein binding; IEA:EnsemblPlants.
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; IPR017420; DMRL_synthase_chloroplast.
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   PIRSF; PIRSF038166; DMRL_synthase_cp; 1.
DR   SUPFAM; SSF52121; Lumazine synthase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000030689};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003795};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003795}.
SQ   SEQUENCE   227 AA;  23944 MW;  310B206581812A74 CRC64;
     MESLASPPCL RLTPTAHRQL HSRQSSSACY THGGTSVTKS NSLSFSSSAS GFSSSLAVEK
     ELRSSFVQTA AVRHVTGSLI RGEGLRFAIV VARFNEVVTK LLLEGAIETF KKYSVREEDI
     EVIWVPGSFE IGVVAQNLGK SGKFHAVLCI GAVIRGDTTH YDAVANSAAS GVLSAGINSG
     VPCIFGVLTC EDMDQALNRS GGKAGNKGAE TALTALEMAS LFEHHLK
//
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