RISB_SPIOL
ID RISB_SPIOL Reviewed; 222 AA.
AC Q9XH32;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 96.
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;
OS Spinacia oleracea (Spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Anserineae; Spinacia.
OX NCBI_TaxID=3562;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RC STRAIN=cv. Melody;
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).
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.
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 -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF147203; AAD44808.1; -; mRNA.
DR PDB; 1C2Y; X-ray; 3.30 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=67-222.
DR PDBsum; 1C2Y; -.
DR AlphaFoldDB; Q9XH32; -.
DR SMR; Q9XH32; -.
DR KEGG; ag:AAD44808; -.
DR OrthoDB; 1402810at2759; -.
DR UniPathway; UPA00275; UER00404.
DR EvolutionaryTrace; Q9XH32; -.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
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; -; 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 3D-structure; Chloroplast; Plastid; Riboflavin biosynthesis; Transferase;
KW Transit peptide.
FT TRANSIT 1..66
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 67..222
FT /note="6,7-dimethyl-8-ribityllumazine synthase,
FT chloroplastic"
FT /id="PRO_0000030439"
FT ACT_SITE 154
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 89
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 122..124
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 146..148
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 151..152
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1C2Y"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1C2Y"
FT STRAND 82..88
FT /evidence="ECO:0007829|PDB:1C2Y"
FT HELIX 91..107
FT /evidence="ECO:0007829|PDB:1C2Y"
FT STRAND 115..121
FT /evidence="ECO:0007829|PDB:1C2Y"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:1C2Y"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:1C2Y"
FT HELIX 154..173
FT /evidence="ECO:0007829|PDB:1C2Y"
FT STRAND 177..182
FT /evidence="ECO:0007829|PDB:1C2Y"
FT HELIX 187..193
FT /evidence="ECO:0007829|PDB:1C2Y"
FT STRAND 194..196
FT /evidence="ECO:0007829|PDB:1C2Y"
FT HELIX 201..219
FT /evidence="ECO:0007829|PDB:1C2Y"
SQ SEQUENCE 222 AA; 23397 MW; 4885037615A5B174 CRC64;
MASFAASQTC FLTTNPTCLK PNSPQKSSTF LPFSAPLSSS SSFPGCGLVH VASNKKNRAS
FVVTNAVREL EGYVTKAQSF RFAIVVARFN EFVTRRLMEG ALDTFKKYSV NEDIDVVWVP
GAYELGVTAQ ALGKSGKYHA IVCLGAVVKG DTSHYDAVVN SASSGVLSAG LNSGVPCVFG
VLTCDNMDQA INRAGGKAGN KGAESALTAI EMASLFEHHL KA
