ID D1C584_SPHTD Unreviewed; 230 AA. AC D1C584; DT 19-JAN-2010, integrated into UniProtKB/TrEMBL. DT 19-JAN-2010, sequence version 1. DT 27-MAR-2024, entry version 88. DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; DE Short=DHBP synthase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; DE EC=4.1.99.12 {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; GN Name=ribB {ECO:0000256|HAMAP-Rule:MF_00180}; GN OrderedLocusNames=Sthe_1970 {ECO:0000313|EMBL:ACZ39401.1}; OS Sphaerobacter thermophilus (strain DSM 20745 / S 6022). OC Bacteria; Thermomicrobiota; Thermomicrobia; Sphaerobacterales; OC Sphaerobacterineae; Sphaerobacteraceae; Sphaerobacter. OX NCBI_TaxID=479434 {ECO:0000313|EMBL:ACZ39401.1, ECO:0000313|Proteomes:UP000002027}; RN [1] {ECO:0000313|Proteomes:UP000002027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49802 / DSM 20745 / S 6022 RC {ECO:0000313|Proteomes:UP000002027}; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N., RA Mikhailova N., LaButti K.M., Clum A., Sun H.I., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Markowitz V., Cheng J.F., RA Hugenholtz P., Woyke T., Wu D., Steenblock K., Schneider S., Pukall R., RA Goeker M., Klenk H.P., Eisen J.A.; RT "The complete chromosome 1 of Sphaerobacter thermophilus DSM 20745."; RL Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ACZ39401.1, ECO:0000313|Proteomes:UP000002027} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49802 / DSM 20745 / S 6022 RC {ECO:0000313|Proteomes:UP000002027}; RX PubMed=21304676; RA Spring S., Nolan M., Lapidus A., Glavina Del Rio T., Copeland A., Tice H., RA Cheng J.F., Lucas S., Land M., Chen F., Bruce D., Goodwin L., Pitluck S., RA Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., RA Hauser L., Chang Y.J., Jeffries C.D., Munk C., Kiss H., Chain P., Han C., RA Brettin T., Detter J.C., Schuler E., Goker M., Rohde M., Bristow J., RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.; RT "Complete genome sequence of Desulfohalobium retbaense type strain RT (HR(100))."; RL Stand. Genomic Sci. 2:38-48(2010). 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|HAMAP-Rule:MF_00180, CC 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|HAMAP-Rule:MF_00180, CC ECO:0000256|RuleBase:RU003843}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000256|HAMAP-Rule:MF_00180, CC 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|HAMAP-Rule:MF_00180, CC ECO:0000256|RuleBase:RU003843}. CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00180, CC ECO:0000256|RuleBase:RU003843}. CC -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000256|HAMAP- CC Rule:MF_00180, ECO:0000256|RuleBase:RU003843}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00180}. 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; CP001823; ACZ39401.1; -; Genomic_DNA. DR AlphaFoldDB; D1C584; -. DR STRING; 479434.Sthe_1970; -. DR KEGG; sti:Sthe_1970; -. DR eggNOG; COG0108; Bacteria. DR HOGENOM; CLU_020273_3_0_0; -. DR InParanoid; D1C584; -. DR UniPathway; UPA00275; UER00399. DR Proteomes; UP000002027; Chromosome 1. 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; 3.90.870.10; DHBP synthase; 1. DR HAMAP; MF_00180; RibB; 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 Lyase {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_00180, ECO:0000256|RuleBase:RU003843}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00180}; Reference proteome {ECO:0000313|Proteomes:UP000002027}; KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP- KW Rule:MF_00180}. FT REGION 208..230 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 27..28 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 28 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 32 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT BINDING 142..146 FT /ligand="D-ribulose 5-phosphate" FT /ligand_id="ChEBI:CHEBI:58121" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT SITE 128 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" FT SITE 166 FT /note="Essential for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00180" SQ SEQUENCE 230 AA; 24299 MW; 3E5AC3CC147F1D70 CRC64; MPLATIEQAI AALRAGRFVI IVDGPDRENE GDLCIAGQFI TPEAVNFIVR EARGLLCAAM APEWVDRLRL PLMVDPASNS APFGTAFTVS VEARQGVTTG ISAHDRARTI RTLADPASTP ADFAMPGHVF PLRARPGGVL ERPGQTEAAV DLARLAGLHP VVAICEIMAD DGTMARLPEL ERFATRHDIP IISVADLAAV RRAQADRHPA GVADHSPAGT AAREGTAYGC //