ID   RIB3_PYRO7              Reviewed;         233 AA.
AC   Q8TG90; G4NCK9;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   24-JAN-2024, entry version 121.
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   Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast
OS   fungus) (Magnaporthe 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}.
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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; 242507.Q8TG90; -.
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; 5489599at2759; -.
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   Gene3D; 3.90.870.10; DHBP synthase; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   NCBIfam; TIGR00506; ribB; 1.
DR   PANTHER; PTHR21327:SF18; 3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE; 1.
DR   PANTHER; PTHR21327; GTP CYCLOHYDROLASE II-RELATED; 1.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   SUPFAM; SSF55821; YrdC/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
//