ID C1IUN6_ENTCL Unreviewed; 308 AA.
AC C1IUN6;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
OS Enterobacter cloacae.
OG Plasmid pEC-IMP {ECO:0000313|EMBL:ACO54027.1}, and
OG Plasmid pEC-IMPQ {ECO:0000313|EMBL:ACO54337.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX NCBI_TaxID=550 {ECO:0000313|EMBL:ACO54027.1};
RN [1] {ECO:0000313|EMBL:ACO54027.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pEC-IMP {ECO:0000313|EMBL:ACO54027.1}, and pEC-IMPQ
RC {ECO:0000313|EMBL:ACO54337.1};
RA Chen Y.-T., Liau T.-L., Liu Y.-M., Lauderdale T.-L., Yan J.-J., Tsai S.-F.;
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACO54027.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pEC-IMP {ECO:0000313|EMBL:ACO54027.1}, and pEC-IMPQ
RC {ECO:0000313|EMBL:ACO54337.1};
RX PubMed=19075060; DOI=10.1128/AAC.00970-08;
RA Chen Y.T., Liao T.L., Liu Y.M., Lauderdale T.L., Yan J.J., Tsai S.F.;
RT "Mobilization of qnrB2 and ISCR1 in plasmids.";
RL Antimicrob. Agents Chemother. 53:1235-1237(2009).
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:0000256|RuleBase:RU361205}.
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 ECO:0000256|RuleBase:RU361205};
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, ECO:0000256|RuleBase:RU361205}.
CC -!- SIMILARITY: Belongs to the DHPS family.
CC {ECO:0000256|RuleBase:RU361205}.
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DR EMBL; EU855787; ACO54027.1; -; Genomic_DNA.
DR EMBL; EU855788; ACO54337.1; -; Genomic_DNA.
DR RefSeq; YP_002791403.1; NC_012555.1.
DR RefSeq; YP_002791713.1; NC_012556.1.
DR AlphaFoldDB; C1IUN6; -.
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; 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 ECO:0000256|RuleBase:RU361205};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361205};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU361205}; Plasmid {ECO:0000313|EMBL:ACO54027.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 31..287
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 308 AA; 33182 MW; 83E86275D5A83C2C CRC64;
MGLCRYGAHN CCLFARPIPI VEVAAEADAM VTVFGILNLT EDSFFDESRR LDPAGAVTAA
IEMLRVGSDV VDVGPAASHP DARPVSPADE IRRIAPLLDA LSDQMHRVSI DSFQPETQRY
ALKRGVGYLN DIQGFPDPAL YPDIAEADCR LVVMHSAQRD GIATRTGHLR PEDALDEIVR
FFEARVSALR RSGVAADRLI LDPGLGFFLS PAPETSLHVL SNLQKLKSAL GLPLLVSVSR
KSFLGATVGL PVKDLGPASL AAELHAIGNG ADYVRTHAPG DLRSAITFSE TLAKFRSRDA
RDRGLDHA
//
