ID A0A0A2U1W0_9FIRM Unreviewed; 404 AA.
AC A0A0A2U1W0;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00016919};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|ARBA:ARBA00030193};
GN ORFNames=JT05_10095 {ECO:0000313|EMBL:KGP75555.1};
OS Desulfosporosinus sp. Tol-M.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfosporosinus.
OX NCBI_TaxID=1536651 {ECO:0000313|EMBL:KGP75555.1, ECO:0000313|Proteomes:UP000030439};
RN [1] {ECO:0000313|EMBL:KGP75555.1, ECO:0000313|Proteomes:UP000030439}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Abu Laban N., Tan B., Dao A., Foght J.;
RT "Draft genome of Desulfosporosinus sp. Tol-M obtained by stable isotope
RT probing of toluene- degrading methanogenic culture enriched from oil sands
RT tailing of Alberta, Canada.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
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 {ECO:0000256|ARBA:ARBA00004763}.
CC -!- SIMILARITY: Belongs to the DHPS family.
CC {ECO:0000256|ARBA:ARBA00009503}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGP75555.1}.
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; JQID01000127; KGP75555.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2U1W0; -.
DR STRING; 1536651.JT05_10095; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000030439; Unassembled WGS sequence.
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 {ECO:0000256|ARBA:ARBA00022909};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000030439};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 141..387
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 404 AA; 44023 MW; 918FE9A05B11FB74 CRC64;
MQTYGLRWVT LDNLAEAIMA LTQIGSTPEG IAHMAGKALG RGIKLEQVPL WVAHILKQEM
LAVGGDAAVH RDVIINKIDA TDVMLLGTVR QLGQLASKVL AQPFGLQKIG HDLKQLLAAL
EPSKTRLLKC RGKELKLGQR TLIMGILNIT PDSFSDGGRY YSLESAIAQA KRMVEEGADI
LDIGAESTRP QHEGVSAAEE WRRLEPVLKA LLELEEIPVS IDTSKASVAA KALEAGAHLI
NDQWGLQKDQ DMVRVVGEYQ VPVIVMHNQE DTTYHHLMGD ILTFLRRSIE LAEAHGLSGD
QIIVDPGIGF GKTTEQNLEI MARLAELRTL GHPVLLGTSR KSMIGKTLNR TVDERLEGTL
ATSVLGVVAG VDLIRVHDVQ ANRRAVQMAD TVVRGQRGVH YVGA
//
