RISB_ARATH
ID RISB_ARATH Reviewed; 227 AA.
AC O80575;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase, chloroplastic;
DE Short=DMRL synthase;
DE Short=LS;
DE Short=Lumazine synthase;
DE EC=2.5.1.78;
DE Flags: Precursor;
GN OrderedLocusNames=At2g44050; ORFNames=F6E13.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10419541; DOI=10.1074/jbc.274.31.22114;
RA Jordan D.B., Bacot K.O., Carlson T.J., Kessel M., Viitanen P.V.;
RT "Plant riboflavin biosynthesis. Cloning, chloroplast localization,
RT expression, purification, and partial characterization of spinach lumazine
RT synthase.";
RL J. Biol. Chem. 274:22114-22121(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
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 (By similarity). {ECO:0000250}.
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 -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2.
CC -!- SUBUNIT: Oligomer forming an icosahedral capsid. {ECO:0000305}.
CC -!- INTERACTION:
CC O80575; Q8L9Y3: ARR14; NbExp=3; IntAct=EBI-4473692, EBI-1100737;
CC O80575; A0A178W6S0: At1g51090; NbExp=3; IntAct=EBI-4473692, EBI-25518185;
CC O80575; O80575: At2g44050; NbExp=5; IntAct=EBI-4473692, EBI-4473692;
CC O80575; Q9M9W9: At3g05640; NbExp=3; IntAct=EBI-4473692, EBI-4436207;
CC O80575; Q9M223: At3g60360; NbExp=3; IntAct=EBI-4473692, EBI-4436982;
CC O80575; Q9LZW4: CIPK14; NbExp=4; IntAct=EBI-4473692, EBI-307576;
CC O80575; P92937: CIPK15; NbExp=3; IntAct=EBI-4473692, EBI-537592;
CC O80575; O80902: CIPK22; NbExp=3; IntAct=EBI-4473692, EBI-4453230;
CC O80575; Q84JC2: DOGL4; NbExp=3; IntAct=EBI-4473692, EBI-1238377;
CC O80575; Q42404: RNU1; NbExp=3; IntAct=EBI-4473692, EBI-1633812;
CC O80575; Q93WE4: SINAT6; NbExp=3; IntAct=EBI-4473692, EBI-4446419;
CC O80575; Q9FJJ3: SRO5; NbExp=3; IntAct=EBI-4473692, EBI-4434999;
CC O80575; Q0WT24: STOP2; NbExp=3; IntAct=EBI-4473692, EBI-4424123;
CC O80575; Q9SJA8: WRKY17; NbExp=5; IntAct=EBI-4473692, EBI-2365037;
CC O80575; O04336: WRKY21; NbExp=3; IntAct=EBI-4473692, EBI-1239118;
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
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DR EMBL; AF148649; AAD44810.1; -; mRNA.
DR EMBL; AC004005; AAC23413.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC10365.1; -; Genomic_DNA.
DR EMBL; AY050913; AAK93590.1; -; mRNA.
DR EMBL; AY091343; AAM14282.1; -; mRNA.
DR PIR; T00685; T00685.
DR RefSeq; NP_181933.1; NM_129967.4.
DR AlphaFoldDB; O80575; -.
DR SMR; O80575; -.
DR BioGRID; 4346; 16.
DR IntAct; O80575; 15.
DR STRING; 3702.AT2G44050.1; -.
DR PaxDb; O80575; -.
DR PRIDE; O80575; -.
DR ProteomicsDB; 236951; -.
DR EnsemblPlants; AT2G44050.1; AT2G44050.1; AT2G44050.
DR GeneID; 819010; -.
DR Gramene; AT2G44050.1; AT2G44050.1; AT2G44050.
DR KEGG; ath:AT2G44050; -.
DR Araport; AT2G44050; -.
DR TAIR; locus:2051739; AT2G44050.
DR eggNOG; KOG3243; Eukaryota.
DR HOGENOM; CLU_089358_4_0_1; -.
DR InParanoid; O80575; -.
DR OMA; CQGVTQG; -.
DR OrthoDB; 1402810at2759; -.
DR PhylomeDB; O80575; -.
DR BioCyc; ARA:AT2G44050-MON; -.
DR BioCyc; MetaCyc:AT2G44050-MON; -.
DR BRENDA; 2.5.1.78; 399.
DR UniPathway; UPA00275; UER00404.
DR PRO; PR:O80575; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; O80575; baseline and differential.
DR Genevisible; O80575; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009570; C:chloroplast stroma; HDA:TAIR.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR Gene3D; 3.40.50.960; -; 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 PANTHER; PTHR21058; PTHR21058; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR PIRSF; PIRSF038166; DMRL_synthase_cp; 1.
DR SUPFAM; SSF52121; SSF52121; 1.
DR TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE 1: Evidence at protein level;
KW Chloroplast; Plastid; Reference proteome; Riboflavin biosynthesis;
KW Transferase; Transit peptide.
FT TRANSIT 1..71
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 72..227
FT /note="6,7-dimethyl-8-ribityllumazine synthase,
FT chloroplastic"
FT /id="PRO_0000030438"
FT ACT_SITE 160
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 94
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 128..130
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 152..154
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 157..158
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 199
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
SQ SEQUENCE 227 AA; 24024 MW; B7C7DAE8A56CBBAE CRC64;
MKSLASPPCL RLIPTAHRQL NSRQSSSACY IHGGSSVNKS NNLSFSSSTS GFASPLAVEK
ELRSSFVQTA AVRHVTGSLI RGEGLRFAIV VARFNEVVTK LLLEGAIETF KKYSVREEDI
EVIWVPGSFE IGVVAQNLGK SGKFHAVLCI GAVIRGDTTH YDAVANSAAS GVLSASINSG
VPCIFGVLTC EDMDQALNRS GGKAGNKGAE TALTALEMAS LFEHHLK
