ID I0EJ35_HELPX Unreviewed; 380 AA.
AC I0EJ35;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=HPPC18_06130 {ECO:0000313|EMBL:AFI02954.1};
OS Helicobacter pylori PeCan18.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=1163742 {ECO:0000313|EMBL:AFI02954.1, ECO:0000313|Proteomes:UP000005006};
RN [1] {ECO:0000313|EMBL:AFI02954.1, ECO:0000313|Proteomes:UP000005006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PeCan18 {ECO:0000313|EMBL:AFI02954.1,
RC ECO:0000313|Proteomes:UP000005006};
RA Kersulyte D., Ramirez Ramos A., Recarvarren S., Barua R.L., Watanabe J.,
RA Gilman R.H., Berg D.E.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; CP003475; AFI02954.1; -; Genomic_DNA.
DR RefSeq; WP_000636094.1; NC_017742.1.
DR AlphaFoldDB; I0EJ35; -.
DR KEGG; hca:HPPC18_06130; -.
DR PATRIC; fig|1163742.3.peg.1255; -.
DR HOGENOM; CLU_008023_1_0_7; -.
DR Proteomes; UP000005006; Chromosome.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
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; IPR016227; Dihydropteroate_synthase_prd.
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 PIRSF; PIRSF000501; DHPS_Campy_prd; 1.
DR SUPFAM; SSF51717; Dihydropteroate synthetase-like; 1.
DR PROSITE; PS50972; PTERIN_BINDING; 1.
PE 4: Predicted;
KW Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 119..371
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 380 AA; 43159 MW; 67D468FFF7CA9A6F CRC64;
MIVKRLNPDA LKSALQKIGP EKIAQTHMHQ KGVSFVFEIQ HLPLSAALIL KQEAISVGGD
FATPRDCILA KEPFYDGVLI ASAKQLERLI VKCHSQPFGL KHLAQELKSH LKAPKPNTPQ
IMAVLNLTPD SFYEKSRFDS KKALEEIYQW LEKGITLIDI GAASSRPQSE IIDPKVEQDR
LKEVLLEIKS QKLYQYAHFS IDTYHAKTAQ MALEHCFSIL NDVSGFNSIE MLEVARDYKP
TCILMHAQKT PKDMQENVFY HNLFDEMDRF FKEKLEVLEK YALQDIILDI GFGFAKLKEH
NLALIKHLSH FLKFKKPLLV GASRKNTIGL ITGREVQNRL AGTLSLHLMA LQNGASILRA
HDIDEHIDLI KVFKSLEEAD
//
