ID DHPS_CLOB8 Reviewed; 269 AA. AC Q05621; A6LPW6; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 27-MAR-2024, entry version 130. DE RecName: Full=Dihydropteroate synthase; DE Short=DHPS; DE EC=2.5.1.15; DE AltName: Full=Dihydropteroate pyrophosphorylase; GN OrderedLocusNames=Cbei_0206; OS Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium OS acetobutylicum). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=290402; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 51743 / NCIMB 8052; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G., RA Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W., RA Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B., RA Blaschek H., Richardson P.; RT "Complete sequence of Clostridium beijerinckii NCIMB 8052."; RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-205. RX PubMed=8396545; DOI=10.1016/0378-1119(93)90677-u; RA Oultram J.D., Burr I.D., Elmore M.J., Minton N.P.; RT "Cloning and sequence analysis of the genes encoding phosphotransbutyrylase RT and butyrate kinase from Clostridium acetobutylicum NCIMB 8052."; RL Gene 131:107-112(1993). CC -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with CC 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8- CC dihydropteroate (H2Pte), the immediate precursor of folate derivatives. CC {ECO:0000250|UniProtKB:P0AC13}. CC -!- CATALYTIC ACTIVITY: CC Reaction=(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = CC 7,8-dihydropteroate + diphosphate; Xref=Rhea:RHEA:19949, CC ChEBI:CHEBI:17836, ChEBI:CHEBI:17839, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:72950; EC=2.5.1.15; CC Evidence={ECO:0000250|UniProtKB:P0AC13}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P0AC13}; CC -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8- CC dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8- CC dihydropteridine diphosphate and 4-aminobenzoate: step 1/2. CC -!- SIMILARITY: Belongs to the DHPS 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; CP000721; ABR32396.1; -; Genomic_DNA. DR EMBL; L04468; AAA52083.1; -; Genomic_DNA. DR RefSeq; WP_011967558.1; NC_009617.1. DR AlphaFoldDB; Q05621; -. DR SMR; Q05621; -. DR KEGG; cbe:Cbei_0206; -. DR eggNOG; COG0294; Bacteria. DR HOGENOM; CLU_008023_0_2_9; -. DR UniPathway; UPA00077; UER00156. DR Proteomes; UP000000565; Chromosome. DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd00739; DHPS; 1. DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1. DR InterPro; IPR045031; DHP_synth-like. DR InterPro; IPR006390; DHP_synth_dom. DR InterPro; IPR011005; Dihydropteroate_synth-like_sf. DR InterPro; IPR000489; Pterin-binding_dom. DR NCBIfam; TIGR01496; DHPS; 1. DR PANTHER; PTHR20941; FOLATE SYNTHESIS PROTEINS; 1. DR PANTHER; PTHR20941:SF1; FOLIC ACID SYNTHESIS PROTEIN FOL1; 1. DR Pfam; PF00809; Pterin_bind; 1. DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1. DR PROSITE; PS00792; DHPS_1; 1. DR PROSITE; PS00793; DHPS_2; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Folate biosynthesis; Magnesium; Metal-binding; Transferase. FT CHAIN 1..269 FT /note="Dihydropteroate synthase" FT /id="PRO_0000168206" FT DOMAIN 14..261 FT /note="Pterin-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334" FT BINDING 21 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:P9WND1" FT BINDING 61 FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate" FT /ligand_id="ChEBI:CHEBI:72950" FT /evidence="ECO:0000250|UniProtKB:P0AC13" FT BINDING 95 FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate" FT /ligand_id="ChEBI:CHEBI:72950" FT /evidence="ECO:0000250|UniProtKB:P0AC13" FT BINDING 114 FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate" FT /ligand_id="ChEBI:CHEBI:72950" FT /evidence="ECO:0000250|UniProtKB:P0AC13" FT BINDING 178 FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate" FT /ligand_id="ChEBI:CHEBI:72950" FT /evidence="ECO:0000250|UniProtKB:P0AC13" FT BINDING 214 FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate" FT /ligand_id="ChEBI:CHEBI:72950" FT /evidence="ECO:0000250|UniProtKB:P0AC13" FT BINDING 249..251 FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate" FT /ligand_id="ChEBI:CHEBI:72950" FT /evidence="ECO:0000250|UniProtKB:P0AC13" SQ SEQUENCE 269 AA; 29948 MW; B66922317A603123 CRC64; MKIGSKEFNI GERTYIMGIL NFTPDSFSDG GKFNDIDVAV KHVKEMIDNG ADIIDVGGES TRPGYEIVSE EEEISRVVPI IKAIKEDFDI PVSIDTYKAK VAEQAIEAGA NLINDIWGFK KDKDMAKVAA KYNVPCCLMH NRDNTEYKNL MEDILNDLKE CINIAKDAGV KDENIILDPG IGFGKTYEQN LEAMNNLERI KELGYPILLG TSRKSMIGLA LNLPVEERIE GTVATTVIGI MKDACDFVRV HDVLENSRAA KMTDIIVRR //