DHPS_NEIMA
ID DHPS_NEIMA Reviewed; 283 AA.
AC Q9JT70; A1ITE8;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Dihydropteroate synthase;
DE Short=DHPS;
DE EC=2.5.1.15;
DE AltName: Full=Dihydropteroate pyrophosphorylase;
GN Name=folP; Synonyms=dhpS; OrderedLocusNames=NMA1950;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1014 / Serogroup A / Serotype 4/21, and
RC 418 / Serogroup A / Serotype 4/21;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(2000).
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}.
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; X68065; CAA48202.1; -; Genomic_DNA.
DR EMBL; X68068; CAA48205.1; -; Genomic_DNA.
DR EMBL; AL157959; CAM09062.1; -; Genomic_DNA.
DR PIR; D81823; D81823.
DR PIR; S25610; S25610.
DR PIR; S65838; S65838.
DR RefSeq; WP_002248109.1; NC_003116.1.
DR AlphaFoldDB; Q9JT70; -.
DR SMR; Q9JT70; -.
DR EnsemblBacteria; CAM09062; CAM09062; NMA1950.
DR KEGG; nma:NMA1950; -.
DR HOGENOM; CLU_008023_0_2_4; -.
DR OMA; FSIDTYH; -.
DR BioCyc; NMEN122587:NMA_RS09885-MON; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000000626; 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; -; 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; 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..283
FT /note="Dihydropteroate synthase"
FT /id="PRO_0000168217"
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 2..4
FT /note="VGC -> ARH (in strain: 1014 and 418)"
FT VARIANT 31
FT /note="L -> F (in strain: 1014 and 418)"
FT VARIANT 68
FT /note="P -> L (in strain: 418)"
FT VARIANT 75
FT /note="P -> S (in strain: 1014)"
FT VARIANT 84
FT /note="S -> P (in strain: 1014 and 418)"
FT VARIANT 87
FT /note="A -> E (in strain: 418)"
FT VARIANT 87
FT /note="A -> V (in strain: 1014)"
FT VARIANT 102
FT /note="H -> R (in strain: 1014 and 418)"
FT VARIANT 105
FT /note="V -> I (in strain: 418)"
FT VARIANT 115
FT /note="I -> V (in strain: 418)"
FT VARIANT 125
FT /note="T -> N (in strain: 418)"
FT VARIANT 130
FT /note="L -> V (in strain: 418)"
FT VARIANT 135
FT /note="C -> R (in strain: 418)"
FT VARIANT 147
FT /note="Q -> R (in strain: 1014)"
FT VARIANT 151
FT /note="K -> E (in strain: 1014)"
FT VARIANT 152
FT /note="N -> T (in strain: 418)"
FT VARIANT 174
FT /note="A -> S (in strain: 418)"
FT VARIANT 188
FT /note="T -> I (in strain: 418)"
FT VARIANT 194
FT /note="C -> G (in strain: 1014)"
FT VARIANT 194
FT /note="C -> GSG (in strain: 418)"
FT VARIANT 198
FT /note="T -> P (in strain: 418)"
FT VARIANT 204
FT /note="T -> A (in strain: 1014 and 418)"
FT VARIANT 218
FT /note="Y -> F (in strain: 1014 and 418)"
FT VARIANT 228
FT /note="S -> R (in strain: 1014)"
FT VARIANT 229
FT /note="M -> T (in strain: 418)"
FT VARIANT 230
FT /note="I -> V (in strain: 1014)"
FT VARIANT 237..238
FT /note="TD -> AN (in strain: 418)"
FT VARIANT 241
FT /note="A -> E (in strain: 418)"
FT VARIANT 243
FT /note="G -> V (in strain: 1014 and 418)"
FT VARIANT 253
FT /note="A -> S (in strain: 1014 and 418)"
FT VARIANT 255
FT /note="A -> R (in strain: 1014)"
FT VARIANT 259
FT /note="K -> Q (in strain: 1014 and 418)"
FT VARIANT 275
FT /note="A -> V (in strain: 1014 and 418)"
SQ SEQUENCE 283 AA; 29928 MW; 89A0976A527C9E27 CRC64;
MVGCVWQAGR FEIGLDKPKI MGIVNLTPDS LSDGGAYSQN AQTALAHAER LLKEGADILD
IGGESTRPGA DYVSPEEEWA RVESVLAEVA GWGVPVSLDT RHTVVMEKAL ALGGIDIIND
VAALTDEGAL ELLACQADTG ICLMHMQGLP KNMQINPKYQ DVVGEVARYL KARAAECIAA
GIAPQRITLD PGFCFGKTLQ HNITLMRHLP ELMAETGYPL LIGVSRKSMI GELTGETDAA
ARGHGSVAAA LAAVARGAKI VRVHDVKATA DALKAWEALG INL
