RIB3_MAGO7
ID RIB3_MAGO7 Reviewed; 233 AA.
AC Q8TG90; G4NCK9;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE Short=DHBP synthase;
DE Short=DS {ECO:0000303|PubMed:11053863};
DE EC=4.1.99.12 {ECO:0000269|PubMed:11053863};
GN Name=RIB3; ORFNames=MGG_01049;
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], PROTEIN SEQUENCE OF 2-17, FUNCTION, CATALYTIC
RP ACTIVITY, COFACTOR, MASS SPECTROMETRY, AND PATHWAY.
RX PubMed=11053863; DOI=10.1107/s0907444900011446;
RA Liao D.-I., Viitanen P.V., Jordan D.B.;
RT "Cloning, expression, purification and crystallization of dihydroxybutanone
RT phosphate synthase from Magnaporthe grisea.";
RL Acta Crystallogr. D 56:1495-1497(2000).
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).
RN [3] {ECO:0007744|PDB:1K49, ECO:0007744|PDB:1K4I, ECO:0007744|PDB:1K4L, ECO:0007744|PDB:1K4O, ECO:0007744|PDB:1K4P}
RP X-RAY CRYSTALLOGRAPHY (0.98 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM;
RP MANGANESE AND ZINC, COFACTOR, AND SUBUNIT.
RX PubMed=11827524; DOI=10.1021/bi015652u;
RA Liao D.-I., Zheng Y.-J., Viitanen P.V., Jordan D.B.;
RT "Structural definition of the active site and catalytic mechanism of 3,4-
RT dihydroxy-2-butanone-4-phosphate synthase.";
RL Biochemistry 41:1795-1806(2002).
CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC and 3,4-dihydroxy-2-butanone 4-phosphate.
CC {ECO:0000269|PubMed:11053863}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate +
CC formate + H(+); Xref=Rhea:RHEA:18457, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:58121, ChEBI:CHEBI:58830;
CC EC=4.1.99.12; Evidence={ECO:0000269|PubMed:11053863};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18458;
CC Evidence={ECO:0000305|PubMed:11053863};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11053863, ECO:0000269|PubMed:11827524};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000305|PubMed:11827524};
CC Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC manganese. {ECO:0000269|PubMed:11827524};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC {ECO:0000305|PubMed:11053863}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11827524}.
CC -!- PTM: S-glutathionylation is reversible and dependent on a glutaredoxin.
CC {ECO:0000250|UniProtKB:Q99258}.
CC -!- MASS SPECTROMETRY: Mass=24870.7; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11053863};
CC -!- SIMILARITY: Belongs to the DHBP 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; AF430214; AAL84175.1; -; mRNA.
DR EMBL; CM001235; EHA48306.1; -; Genomic_DNA.
DR RefSeq; XP_003717890.1; XM_003717842.1.
DR PDB; 1K49; X-ray; 1.50 A; A=1-233.
DR PDB; 1K4I; X-ray; 0.98 A; A=1-233.
DR PDB; 1K4L; X-ray; 1.60 A; A=1-233.
DR PDB; 1K4O; X-ray; 1.10 A; A=1-233.
DR PDB; 1K4P; X-ray; 1.00 A; A=1-233.
DR PDBsum; 1K49; -.
DR PDBsum; 1K4I; -.
DR PDBsum; 1K4L; -.
DR PDBsum; 1K4O; -.
DR PDBsum; 1K4P; -.
DR AlphaFoldDB; Q8TG90; -.
DR SMR; Q8TG90; -.
DR STRING; 318829.MGG_01049T0; -.
DR EnsemblFungi; MGG_01049T0; MGG_01049T0; MGG_01049.
DR GeneID; 2674307; -.
DR KEGG; mgr:MGG_01049; -.
DR VEuPathDB; FungiDB:MGG_01049; -.
DR eggNOG; KOG1284; Eukaryota.
DR HOGENOM; CLU_020273_3_1_1; -.
DR InParanoid; Q8TG90; -.
DR OMA; DAGGLIC; -.
DR OrthoDB; 1382176at2759; -.
DR UniPathway; UPA00275; UER00399.
DR EvolutionaryTrace; Q8TG90; -.
DR Proteomes; UP000009058; Chromosome 5.
DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR InterPro; IPR000422; DHBP_synthase_RibB.
DR Pfam; PF00926; DHBP_synthase; 1.
DR SUPFAM; SSF55821; SSF55821; 1.
DR TIGRFAMs; TIGR00506; ribB; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glutathionylation; Lyase;
KW Magnesium; Manganese; Metal-binding; Reference proteome;
KW Riboflavin biosynthesis.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11053863"
FT CHAIN 2..233
FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT /id="PRO_0000296686"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11827524,
FT ECO:0007744|PDB:1K4I"
FT BINDING 37
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11827524,
FT ECO:0007744|PDB:1K4I"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11827524,
FT ECO:0007744|PDB:1K4L"
FT BINDING 37
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11827524,
FT ECO:0007744|PDB:1K4L"
FT BINDING 41
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:Q5A3V6"
FT BINDING 92
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:Q5A3V6"
FT BINDING 150..154
FT /ligand="D-ribulose 5-phosphate"
FT /ligand_id="ChEBI:CHEBI:58121"
FT /evidence="ECO:0000250|UniProtKB:Q5A3V6"
FT BINDING 153
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11827524,
FT ECO:0007744|PDB:1K4I"
FT BINDING 153
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11827524,
FT ECO:0007744|PDB:1K4L"
FT SITE 136
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 174
FT /note="Essential for catalytic activity"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="S-glutathionyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q99258"
FT HELIX 15..23
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:1K4I"
FT TURN 34..37
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 40..45
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 51..60
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 66..69
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 71..76
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 106..108
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 111..122
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 128..130
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 131..141
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 168..177
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:1K4P"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 196..205
FT /evidence="ECO:0007829|PDB:1K4I"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:1K4I"
FT HELIX 213..224
FT /evidence="ECO:0007829|PDB:1K4I"
SQ SEQUENCE 233 AA; 25003 MW; 5C83AA5C49DFD07E CRC64;
MPSTDSIPKS NFDAIPDVIQ AFKNGEFVVV LDDPSRENEA DLIIAAESVT TEQMAFMVRH
SSGLICAPLT PERTTALDLP QMVTHNADPR GTAYTVSVDA EHPSTTTGIS AHDRALACRM
LAAPDAQPSH FRRPGHVFPL RAVAGGVRAR RGHTEAGVEL CRLAGKRPVA VISEIVDDGQ
EVEGRAVRAA PGMLRGDECV AFARRWGLKV CTIEDMIAHV EKTEGKLETN GSG
