ID X2JST2_AGGAC Unreviewed; 284 AA.
AC X2JST2;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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};
GN ORFNames=CF65_00635 {ECO:0000313|EMBL:AHN71172.1};
OS Aggregatibacter actinomycetemcomitans HK1651.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Aggregatibacter.
OX NCBI_TaxID=272556 {ECO:0000313|EMBL:AHN71172.1, ECO:0000313|Proteomes:UP000019758};
RN [1] {ECO:0000313|EMBL:AHN71172.1, ECO:0000313|Proteomes:UP000019758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HK1651 {ECO:0000313|EMBL:AHN71172.1,
RC ECO:0000313|Proteomes:UP000019758};
RA Gillaspy A.F., Griffin J., Najar F., Hinkle J., Lewis L.A.,
RA McLaughlin R.E., Hartman K., Nydick C., Gipson M., Conway B., Vaughn J.,
RA Thompson C., Gipson J., Maddera L., Carson M., Kenton S., Lai H., Roe B.A.,
RA Orvis J., Zaitshik J., Griffin J., Scott E., Dyer D.W.;
RT "Genome sequencing and closure of the periodontal pathogen, Aggregatibacter
RT actinomycetemcomitans.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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; CP007502; AHN71172.1; -; Genomic_DNA.
DR AlphaFoldDB; X2JST2; -.
DR SMR; X2JST2; -.
DR KEGG; aah:CF65_00635; -.
DR PATRIC; fig|272556.10.peg.439; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_3_6; -.
DR UniPathway; UPA00077; UER00156.
DR Proteomes; UP000019758; 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; 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};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT DOMAIN 24..276
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 284 AA; 31579 MW; 7B410C833EA0DF0F CRC64;
MHRQASEFLM KLTANNKVLD LSTPQIMGIL NFTPDSFSDS GKFFQLDKAL AQVEKMLRLG
ASIIDIGGES TRPMADEVTL EEELQRVVPL VEAVRQRFDC WISVDTSKPQ VMRETANAGM
DLINDIRALQ EPQALETAAQ LALPVCIMHM QGQPRTMQLN PHYEDVVADV LKFMQQRTEQ
CLAAGIKQDN IIWDPGFGFG KSVQHNYRLL QQLWVFCQQG YPVLAGISRK SMIGAVLDKP
VEQRTVGSVS AALIAAMNGA RILRVHDVGE TADALKIWQA TLNS
//
