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Dihydropteroate synthase (DHPS) (EC 2.5.1.15) (Dihydropteroate pyrophosphorylase)

 DHPS_NEIMC              Reviewed;         283 AA.
P57696;
08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
25-OCT-2017, entry version 84.
RecName: Full=Dihydropteroate synthase;
Short=DHPS;
EC=2.5.1.15;
AltName: Full=Dihydropteroate pyrophosphorylase;
Name=folP; Synonyms=dhpS;
Neisseria meningitidis serogroup C.
Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
Neisseriaceae; Neisseria.
NCBI_TaxID=135720;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=BT054 / Serogroup C / Serotype 15,
BT227 / Serogroup C / Serotype 2a, and
CCUG 23102 / MO124 / Serogroup C / Serotype 15;
PubMed=1400191; DOI=10.1128/jb.174.20.6386-6393.1992;
Raadstroem P., Fermer C., Kristiansen B.-E., Jenkins A., Skoeld O.,
Swedberg G.;
"Transformational exchanges in the dihydropteroate synthase gene of
Neisseria meningitidis: a novel mechanism for acquisition of
sulfonamide resistance.";
J. Bacteriol. 174:6386-6393(1992).
-!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA)
with 6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to
form 7,8-dihydropteroate (H2Pte), the immediate precursor of
folate derivatives. {ECO:0000250|UniProtKB:P0AC13}.
-!- CATALYTIC ACTIVITY: 6-hydroxymethyl-7,8-dihydropterin diphosphate
+ 4-aminobenzoate = diphosphate + dihydropteroate.
{ECO:0000250|UniProtKB:P0AC13}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P0AC13};
-!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis;
7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-
dihydropteridine diphosphate and 4-aminobenzoate: step 1/2.
-!- SUBUNIT: Homodimer.
-!- SIMILARITY: Belongs to the DHPS family. {ECO:0000305}.
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EMBL; X68063; CAA48200.1; -; Genomic_DNA.
EMBL; X68067; CAA48204.1; -; Genomic_DNA.
EMBL; X68064; CAA48201.1; -; Genomic_DNA.
PIR; A57423; A57423.
PIR; S25612; S25612.
ProteinModelPortal; P57696; -.
SMR; P57696; -.
UniPathway; UPA00077; UER00156.
GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
CDD; cd00739; DHPS; 1.
Gene3D; 3.20.20.20; -; 1.
InterPro; IPR006390; DHP_synth.
InterPro; IPR011005; Dihydropteroate_synth-like.
InterPro; IPR000489; Pterin-binding_dom.
Pfam; PF00809; Pterin_bind; 1.
SUPFAM; SSF51717; SSF51717; 1.
TIGRFAMs; TIGR01496; DHPS; 1.
PROSITE; PS00792; DHPS_1; 1.
PROSITE; PS50972; PTERIN_BINDING; 1.
3: Inferred from homology;
Folate biosynthesis; Magnesium; Metal-binding; Transferase.
CHAIN 1 283 Dihydropteroate synthase.
/FTId=PRO_0000168219.
DOMAIN 18 274 Pterin-binding. {ECO:0000255|PROSITE-
ProRule:PRU00334}.
REGION 262 264 6-hydroxymethyl-7,8-dihydropterin
diphosphate binding.
{ECO:0000250|UniProtKB:P0AC13}.
METAL 25 25 Magnesium.
{ECO:0000250|UniProtKB:P9WND1}.
BINDING 66 66 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 99 99 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 119 119 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 190 190 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
BINDING 227 227 6-hydroxymethyl-7,8-dihydropterin
diphosphate.
{ECO:0000250|UniProtKB:P0AC13}.
VARIANT 36 36 V -> A (in strain: BT054).
VARIANT 42 43 QT -> RI (in strain: BT054).
VARIANT 50 50 Q -> R (in strain: BT054).
VARIANT 68 68 S -> P (in strain: BT054).
VARIANT 96 96 I -> V (in strain: BT054).
VARIANT 104 105 VI -> AV (in strain: BT054).
VARIANT 107 107 E -> G (in strain: BT054).
VARIANT 125 125 N -> T (in strain: BT054).
VARIANT 137 137 A -> T (in strain: BT054).
VARIANT 151 151 K -> E (in strain: BT054).
VARIANT 152 152 N -> T (in strain: MO124).
VARIANT 174 174 A -> S (in strain: MO124).
VARIANT 178 178 I -> V (in strain: BT054).
VARIANT 188 188 T -> I (in strain: MO124).
VARIANT 194 194 C -> G (in strain: BT054).
VARIANT 194 194 C -> GSG (in strain: MO124).
VARIANT 198 198 T -> P (in strain: MO124).
VARIANT 204 204 T -> A (in strain: BT054 and MO124).
VARIANT 218 218 Y -> F (in strain: BT054 and MO124).
VARIANT 228 228 S -> R (in strain: BT054).
VARIANT 229 229 M -> T (in strain: MO124).
VARIANT 230 230 I -> V (in strain: BT054).
VARIANT 237 238 TD -> AN (in strain: MO124).
VARIANT 241 241 A -> E (in strain: MO124).
VARIANT 243 243 G -> V (in strain: BT054 and MO124).
VARIANT 253 253 A -> S (in strain: BT054 and MO124).
VARIANT 259 259 K -> Q (in strain: BT054 and MO124).
VARIANT 275 275 A -> V (in strain: BT054 and MO124).
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


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