ID A0A0E4C7T2_9FIRM Unreviewed; 397 AA.
AC A0A0E4C7T2;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-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=483 {ECO:0000313|EMBL:CFX10831.1};
OS Syntrophomonas zehnderi OL-4.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Syntrophomonadaceae;
OC Syntrophomonas.
OX NCBI_TaxID=690567 {ECO:0000313|EMBL:CFX10831.1, ECO:0000313|Proteomes:UP000045545};
RN [1] {ECO:0000313|EMBL:CFX10831.1, ECO:0000313|Proteomes:UP000045545}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OL-4 {ECO:0000313|EMBL:CFX10831.1,
RC ECO:0000313|Proteomes:UP000045545};
RA Murphy D.;
RL Submitted (MAR-2015) 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}.
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DR EMBL; CGIH01000005; CFX10831.1; -; Genomic_DNA.
DR RefSeq; WP_046495368.1; NZ_CGIH01000005.1.
DR AlphaFoldDB; A0A0E4C7T2; -.
DR STRING; 690567.483; -.
DR OrthoDB; 9811744at2; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000045545; 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:UP000045545};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 138..387
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 397 AA; 42846 MW; BB51FC56796C811F CRC64;
MNGHHAVFIS NRDEARGFLE KIGASPPGIE YMLPKAVFRC LKLKDIPSRA ANLIKQEMLA
KGGEAAVAKN VAVGEGSSDV LLLGTLRQYQ LLIEKLKLQP FGLRALAEEI ENILLALENK
SGNLKLPHGR VLEFGQKTLI MGILNVTPDS FTDGGRYLNT DAAVAHALEM KAEGADIIDV
GGASSRPDST MAAAEEELKR ILPVIKKLAQ EDIIISVDTF RAEVARQVLA EGAHIINDIG
GLQLDHELAG VLAEWQSPAV LMHNRLQLNQ GQPYFDLIAD IIAELSNSID TAVAAGLPLE
QIIIDPGLGF GKSVAENRLL IKNLQDFKSL GRPILLGASR KAFIGRTLGL EVEERLEGSL
AAVALGIMNG ADIVRVHDVK QSKRVAQMTD AVRNEYG
//
