ID   Q83FM8_TROWT            Unreviewed;       215 AA.
AC   Q83FM8;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   02-SEP-2026, entry version 141.
DE   RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|RuleBase:RU003843};
DE            Short=DHBP synthase {ECO:0000256|RuleBase:RU003843};
DE            EC=4.1.99.12 {ECO:0000256|RuleBase:RU003843};
GN   OrderedLocusNames=TWT_689 {ECO:0000313|EMBL:AAO44786.1};
OS   Tropheryma whipplei (strain Twist) (Whipple's bacillus).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Tropherymataceae; Tropheryma.
OX   NCBI_TaxID=203267 {ECO:0000313|EMBL:AAO44786.1, ECO:0000313|Proteomes:UP000002200};
RN   [1] {ECO:0000313|EMBL:AAO44786.1, ECO:0000313|Proteomes:UP000002200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Twist {ECO:0000313|EMBL:AAO44786.1,
RC   ECO:0000313|Proteomes:UP000002200};
RX   PubMed=12902375; DOI=10.1101/gr.1474603;
RA   Raoult D., Ogata H., Audic S., Robert C., Suhre K., Drancourt M.,
RA   Claverie J.-M.;
RT   "Tropheryma whipplei twist: a human pathogenic Actinobacteria with a
RT   reduced genome.";
RL   Genome Res. 13:1800-1809(2003).
CC   -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to formate
CC       and 3,4-dihydroxy-2-butanone 4-phosphate.
CC       {ECO:0000256|ARBA:ARBA00002284, ECO:0000256|RuleBase:RU003843}.
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:0000256|RuleBase:RU003843};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU003843};
CC       Note=Binds 2 divalent metal cations per subunit. Magnesium or
CC       manganese. {ECO:0000256|RuleBase:RU003843};
CC   -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-
CC       oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004904, ECO:0000256|RuleBase:RU003843}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU003843}.
CC   -!- SIMILARITY: Belongs to the DHBP synthase family.
CC       {ECO:0000256|RuleBase:RU003843}.
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DR   EMBL; AE014184; AAO44786.1; -; Genomic_DNA.
DR   RefSeq; WP_011096645.1; NC_004572.3.
DR   AlphaFoldDB; Q83FM8; -.
DR   STRING; 203267.TWT_689; -.
DR   GeneID; 67388483; -.
DR   KEGG; twh:TWT_689; -.
DR   eggNOG; COG0108; Bacteria.
DR   HOGENOM; CLU_020273_3_1_11; -.
DR   OrthoDB; 9793111at2; -.
DR   UniPathway; UPA00275; UER00399.
DR   Proteomes; UP000002200; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Hydrolase {ECO:0000313|EMBL:AAO44786.1};
KW   Lyase {ECO:0000256|RuleBase:RU003843};
KW   Magnesium {ECO:0000256|RuleBase:RU003843};
KW   Manganese {ECO:0000256|RuleBase:RU003843};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003843};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002200};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619,
KW   ECO:0000256|RuleBase:RU003843}.
SQ   SEQUENCE   215 AA;  23847 MW;  DA2B8DCC048176B9 CRC64;
     MRHIPDALNA LRAGRPVVVL DDKNRENEAD VIMAAQFATQ EWVAWIIRHT SGFLCVPLSN
     QRADKLQLPS MVAANEDRFK TAYTISVDAA DAAITTGISA ADRSLTIRTL AARDSSAKHL
     VRPGHILPLR ARDGGLLERR GHTEAAIELM RQAQLEPVAV IAELVSDTGE LLRGRALDEF
     IRKNNLVLVE ISQIIEYMKM SDLKDISMNL NRDCL
//