ID RIBB_CAMJE Reviewed; 339 AA. AC Q9PHU4; Q0PAU5; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 28-JAN-2026, entry version 127. DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; DE Short=DHBP synthase; DE EC=4.1.99.12; GN Name=ribB; OrderedLocusNames=Cj0572; OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / OS NCTC 11168). OC Bacteria; Pseudomonadati; Campylobacterota; Epsilonproteobacteria; OC Campylobacterales; Campylobacteraceae; Campylobacter. OX NCBI_TaxID=192222; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700819 / NCTC 11168; RX PubMed=10688204; DOI=10.1038/35001088; RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., RA Barrell B.G.; RT "The genome sequence of the food-borne pathogen Campylobacter jejuni RT reveals hypervariable sequences."; RL Nature 403:665-668(2000). 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}. 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; AL111168; CAL34718.1; -; Genomic_DNA. DR PIR; C81404; C81404. DR RefSeq; WP_002852104.1; NC_002163.1. DR AlphaFoldDB; Q9PHU4; -. DR SMR; Q9PHU4; -. DR IntAct; Q9PHU4; 68. DR STRING; 192222.Cj0572; -. DR PaxDb; 192222-Cj0572; -. DR EnsemblBacteria; CAL34718; CAL34718; Cj0572. DR KEGG; cje:Cj0572; -. DR PATRIC; fig|192222.6.peg.564; -. DR eggNOG; COG0108; Bacteria. DR eggNOG; COG0807; Bacteria. DR HOGENOM; CLU_020273_1_2_7; -. DR OrthoDB; 9793111at2; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000000799; 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-UniRule. DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:TreeGrafter. 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 FunFam; 3.90.870.10:FF:000001; Riboflavin biosynthesis protein RibBA; 1. DR Gene3D; 3.90.870.10; DHBP synthase; 1. DR Gene3D; 3.40.50.10990; GTP cyclohydrolase II; 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 NCBIfam; NF006804; PRK09314.1; 1. 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 Pfam; PF00925; GTP_cyclohydro2; 1. DR PIRSF; PIRSF001259; RibA; 1. DR SUPFAM; SSF142695; RibA-like; 1. DR SUPFAM; SSF55821; YrdC/RibB; 1. PE 3: Inferred from homology; KW Lyase; Magnesium; Manganese; Metal-binding; Reference proteome; KW Riboflavin biosynthesis. FT CHAIN 1..339 FT /note="3,4-dihydroxy-2-butanone 4-phosphate synthase" FT /id="PRO_0000151722" FT REGION 1..206 FT /note="DHBP synthase" FT REGION 207..339 FT /note="GTP cyclohydrolase II-like" FT BINDING 27..28 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000250" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 32 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000250" FT BINDING 139..143 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000250" FT BINDING 142 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 163 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000250" FT SITE 125 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000250" FT SITE 163 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000250" SQ SEQUENCE 339 AA; 37925 MW; 6D90CF5F6A3F3DD9 CRC64; MKFVSVEQAI KDLQAGKMLV MVDAEDRENE GDLIFPAQFS TQEKVNFMIK EARGVVCVAL DETLAKKFEL PLMVPKNTSN HETAFTITVD AKDATTGVSA YERNMTIQIF ADDNAKASDF VRPGHINPLI AKKGGVLERT GHTEGTVDLC KLAGLKGACV ICEIVKDNGD MARREDLEIF CQKHDLNMIA VSDLIEYRLK HESLIKLEEK SQSVLAGFKA EKFIFSDHNQ TQHIAFCFKD IKKCENVKFH ISGSDFELLT SDKFSKLLEQ IKFLSENGGV IVFMQGEKSS TTQYKNYGIG AQILRYFGIE EIKLLSQSCD KDYIGLEGFG LNLKACNFN //