DHPS_NEIMC
ID DHPS_NEIMC Reviewed; 283 AA.
AC P57696;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2001, sequence version 2.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Dihydropteroate synthase;
DE Short=DHPS;
DE EC=2.5.1.15;
DE AltName: Full=Dihydropteroate pyrophosphorylase;
GN Name=folP; Synonyms=dhpS;
OS Neisseria meningitidis serogroup C.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=135720;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BT054 / Serogroup C / Serotype 15,
RC BT227 / Serogroup C / Serotype 2a, and
RC CCUG 23102 / MO124 / Serogroup C / Serotype 15;
RX PubMed=1400191; DOI=10.1128/jb.174.20.6386-6393.1992;
RA Raadstroem P., Fermer C., Kristiansen B.-E., Jenkins A., Skoeld O.,
RA Swedberg G.;
RT "Transformational exchanges in the dihydropteroate synthase gene of
RT Neisseria meningitidis: a novel mechanism for acquisition of sulfonamide
RT resistance.";
RL J. Bacteriol. 174:6386-6393(1992).
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 -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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DR EMBL; X68063; CAA48200.1; -; Genomic_DNA.
DR EMBL; X68067; CAA48204.1; -; Genomic_DNA.
DR EMBL; X68064; CAA48201.1; -; Genomic_DNA.
DR PIR; A57423; A57423.
DR PIR; S25612; S25612.
DR AlphaFoldDB; P57696; -.
DR SMR; P57696; -.
DR UniPathway; UPA00077; UER00156.
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; -; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
DR InterPro; IPR000489; Pterin-binding_dom.
DR PANTHER; PTHR20941; PTHR20941; 1.
DR Pfam; PF00809; Pterin_bind; 1.
DR SUPFAM; SSF51717; SSF51717; 1.
DR TIGRFAMs; TIGR01496; DHPS; 1.
DR PROSITE; PS00792; DHPS_1; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 3: Inferred from homology;
KW Folate biosynthesis; Magnesium; Metal-binding; Transferase.
FT CHAIN 1..283
FT /note="Dihydropteroate synthase"
FT /id="PRO_0000168219"
FT DOMAIN 18..274
FT /note="Pterin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00334"
FT BINDING 25
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P9WND1"
FT BINDING 66
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 99
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 119
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 190
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 227
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT BINDING 262..264
FT /ligand="(7,8-dihydropterin-6-yl)methyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:72950"
FT /evidence="ECO:0000250|UniProtKB:P0AC13"
FT VARIANT 36
FT /note="V -> A (in strain: BT054)"
FT VARIANT 42..43
FT /note="QT -> RI (in strain: BT054)"
FT VARIANT 50
FT /note="Q -> R (in strain: BT054)"
FT VARIANT 68
FT /note="S -> P (in strain: BT054)"
FT VARIANT 96
FT /note="I -> V (in strain: BT054)"
FT VARIANT 104..105
FT /note="VI -> AV (in strain: BT054)"
FT VARIANT 107
FT /note="E -> G (in strain: BT054)"
FT VARIANT 125
FT /note="N -> T (in strain: BT054)"
FT VARIANT 137
FT /note="A -> T (in strain: BT054)"
FT VARIANT 151
FT /note="K -> E (in strain: BT054)"
FT VARIANT 152
FT /note="N -> T (in strain: MO124)"
FT VARIANT 174
FT /note="A -> S (in strain: MO124)"
FT VARIANT 178
FT /note="I -> V (in strain: BT054)"
FT VARIANT 188
FT /note="T -> I (in strain: MO124)"
FT VARIANT 194
FT /note="C -> G (in strain: BT054)"
FT VARIANT 194
FT /note="C -> GSG (in strain: MO124)"
FT VARIANT 198
FT /note="T -> P (in strain: MO124)"
FT VARIANT 204
FT /note="T -> A (in strain: BT054 and MO124)"
FT VARIANT 218
FT /note="Y -> F (in strain: BT054 and MO124)"
FT VARIANT 228
FT /note="S -> R (in strain: BT054)"
FT VARIANT 229
FT /note="M -> T (in strain: MO124)"
FT VARIANT 230
FT /note="I -> V (in strain: BT054)"
FT VARIANT 237..238
FT /note="TD -> AN (in strain: MO124)"
FT VARIANT 241
FT /note="A -> E (in strain: MO124)"
FT VARIANT 243
FT /note="G -> V (in strain: BT054 and MO124)"
FT VARIANT 253
FT /note="A -> S (in strain: BT054 and MO124)"
FT VARIANT 259
FT /note="K -> Q (in strain: BT054 and MO124)"
FT VARIANT 275
FT /note="A -> V (in strain: BT054 and MO124)"
SQ SEQUENCE 283 AA; 30167 MW; FE8D19EFA15FA034 CRC64;
MARHVWQAGR FEIGLDKPKI MGIVNLTPDS FSDGGVYSQN AQTALAHAEQ LLKEGADILD
IGGESTRSGA DYVSPEEEWA RVEPVLAEVA GWGVPISLDT RRTVIMEKAL ALGGIDIIND
VAALNDEGAV ELLARQADTG ICLMHMQGLP KNMQINPKYQ DVVGEVARYL KARAAECIAA
GIAPQRITLD PGFCFGKTLQ HNITLMRHLP ELMAETGYPL LIGVSRKSMI GELTGETDAA
ARGHGSVAAA LAAVARGAKI VRVHDVKATA DALKAWEALG INL
