ID   RIBB_SULMU              Reviewed;         356 AA.
AC   O68249;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase;
DE            Short=DHBP synthase;
DE            EC=4.1.99.12;
GN   Name=ribB;
OS   Sulfurospirillum multivorans (Dehalospirillum multivorans).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Sulfurospirillaceae; Sulfurospirillum.
OX   NCBI_TaxID=66821;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9696761; DOI=10.1128/jb.180.16.4140-4145.1998;
RA   Neumann A., Wohlfarth G., Diekert G.;
RT   "Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning,
RT   sequencing of the encoding genes, and expression of the pceA gene in
RT   Escherichia coli.";
RL   J. Bacteriol. 180:4140-4145(1998).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate. {ECO:0000250}.
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;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the DHBP synthase
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the GTP
CC       cyclohydrolase II family. {ECO:0000305}.
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DR   EMBL; AF022812; AAC60785.1; -; Genomic_DNA.
DR   RefSeq; WP_025344662.1; NZ_CP042966.1.
DR   AlphaFoldDB; O68249; -.
DR   SMR; O68249; -.
DR   STRING; 1150621.SMUL_1528; -.
DR   UniPathway; UPA00275; UER00399.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.10990; -; 1.
DR   HAMAP; MF_00180; RibB; 1.
DR   InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom.
DR   InterPro; IPR000422; DHBP_synthase_RibB.
DR   InterPro; IPR032677; GTP_cyclohydro_II.
DR   InterPro; IPR036144; RibA-like_sf.
DR   Pfam; PF00926; DHBP_synthase; 1.
DR   Pfam; PF00925; GTP_cyclohydro2; 1.
DR   SUPFAM; SSF142695; SSF142695; 1.
DR   SUPFAM; SSF55821; SSF55821; 1.
DR   TIGRFAMs; TIGR00506; ribB; 1.
PE   3: Inferred from homology;
KW   Lyase; Magnesium; Manganese; Metal-binding; Riboflavin biosynthesis.
FT   CHAIN           1..356
FT                   /note="3,4-dihydroxy-2-butanone 4-phosphate synthase"
FT                   /id="PRO_0000151796"
FT   REGION          1..211
FT                   /note="DHBP synthase"
FT   REGION          212..356
FT                   /note="GTP cyclohydrolase II-like"
FT   BINDING         38..39
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         39
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         43
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250"
FT   BINDING         150..154
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         174
FT                   /ligand="D-ribulose 5-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58121"
FT                   /evidence="ECO:0000250"
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"
SQ   SEQUENCE   356 AA;  39358 MW;  851685138C2F6512 CRC64;
     MNAILSDQKT FQAIIRVNQA IEDIRQGKMV VMVDDEDREN EGDLVYAASF STPQKVNFMA
     SHAKGLICVA ISKKIANRLQ LEPMVKKNDS SYETAFTITV DARTAATGIS AGERDMTIKI
     LADGGSHESE LVRPGHIFPL IAKEGGALVR IGHTEGSVDL CRLAGQGDSA VICEIMKEDG
     TMARRPDLDI FCAKHELNIV YISDIVEYRM MNESLIRVIA ESTTQFLGKD ARRYDFVDHN
     DNHHIAYAFG NIKNRSAVKF HSIMPDNELL ADTKKYNSLI QAIHYLQKSG GVLIFMDNGT
     QDMSKIREYG IGAQIIKHLG IENIELLSDS KNKEFVGISG FGLSVIKSTN VNETVA