RIB4_MAGO7
ID RIB4_MAGO7 Reviewed; 200 AA.
AC Q9UVT8; A4QVB0; G4MRQ0;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase;
DE Short=DMRL synthase;
DE Short=LS;
DE Short=Lumazine synthase;
DE EC=2.5.1.78;
GN ORFNames=MGG_04626;
OS Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS fungus) (Pyricularia oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Magnaporthales; Pyriculariaceae; Pyricularia.
OX NCBI_TaxID=242507;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) IN
RP COMPLEX WITH SUBSTRATE ANALOG INHIBITOR, AND SUBUNIT.
RX PubMed=10595538; DOI=10.1110/ps.8.11.2355;
RA Persson K., Schneider G., Jordan D.B., Viitanen P.V., Sandalova T.;
RT "Crystal structure analysis of a pentameric fungal and an icosahedral plant
RT lumazine synthase reveals the structural basis for differences in
RT assembly.";
RL Protein Sci. 8:2355-2365(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=70-15 / ATCC MYA-4617 / FGSC 8958;
RX PubMed=15846337; DOI=10.1038/nature03449;
RA Dean R.A., Talbot N.J., Ebbole D.J., Farman M.L., Mitchell T.K.,
RA Orbach M.J., Thon M.R., Kulkarni R., Xu J.-R., Pan H., Read N.D.,
RA Lee Y.-H., Carbone I., Brown D., Oh Y.Y., Donofrio N., Jeong J.S.,
RA Soanes D.M., Djonovic S., Kolomiets E., Rehmeyer C., Li W., Harding M.,
RA Kim S., Lebrun M.-H., Bohnert H., Coughlan S., Butler J., Calvo S.E.,
RA Ma L.-J., Nicol R., Purcell S., Nusbaum C., Galagan J.E., Birren B.W.;
RT "The genome sequence of the rice blast fungus Magnaporthe grisea.";
RL Nature 434:980-986(2005).
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: Homopentamer. {ECO:0000269|PubMed:10595538}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
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DR EMBL; AF148449; AAD55372.1; -; mRNA.
DR EMBL; CM001231; EHA58265.1; -; Genomic_DNA.
DR RefSeq; XP_003710877.1; XM_003710829.1.
DR PDB; 1C41; X-ray; 3.10 A; A/B/C/D/E/F/G/H/I/J=1-200.
DR PDBsum; 1C41; -.
DR AlphaFoldDB; Q9UVT8; -.
DR SMR; Q9UVT8; -.
DR STRING; 318829.MGG_04626T0; -.
DR PRIDE; Q9UVT8; -.
DR EnsemblFungi; MGG_04626T0; MGG_04626T0; MGG_04626.
DR GeneID; 2677942; -.
DR KEGG; mgr:MGG_04626; -.
DR VEuPathDB; FungiDB:MGG_04626; -.
DR eggNOG; KOG3243; Eukaryota.
DR HOGENOM; CLU_089358_2_0_1; -.
DR InParanoid; Q9UVT8; -.
DR OMA; CQGVTQG; -.
DR OrthoDB; 1402810at2759; -.
DR BRENDA; 2.5.1.78; 3152.
DR UniPathway; UPA00275; UER00404.
DR EvolutionaryTrace; Q9UVT8; -.
DR Proteomes; UP000009058; Chromosome 1.
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; 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 SUPFAM; SSF52121; SSF52121; 1.
DR TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Riboflavin biosynthesis; Transferase.
FT CHAIN 1..200
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_0000134855"
FT ACT_SITE 127
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 25
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 59..61
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 119..121
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 124..125
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT BINDING 166
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1C41"
FT HELIX 27..43
FT /evidence="ECO:0007829|PDB:1C41"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:1C41"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:1C41"
FT HELIX 61..75
FT /evidence="ECO:0007829|PDB:1C41"
FT STRAND 112..121
FT /evidence="ECO:0007829|PDB:1C41"
FT HELIX 127..146
FT /evidence="ECO:0007829|PDB:1C41"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:1C41"
FT HELIX 160..166
FT /evidence="ECO:0007829|PDB:1C41"
FT HELIX 176..195
FT /evidence="ECO:0007829|PDB:1C41"
SQ SEQUENCE 200 AA; 21072 MW; E079F049D32271B5 CRC64;
MHTKGPTPQQ HDGSALRIGI VHARWNETII EPLLAGTKAK LLACGVKESN IVVQSVPGSW
ELPIAVQRLY SASQLQTPSS GPSLSAGDLL GSSTTDLTAL PTTTASSTGP FDALIAIGVL
IKGETMHFEY IADSVSHGLM RVQLDTGVPV IFGVLTVLTD DQAKARAGVI EGSHNHGEDW
GLAAVEMGVR RRDWAAGKTE
