ID A7ZEE0_CAMC1 Unreviewed; 379 AA.
AC A7ZEE0;
DT 23-OCT-2007, integrated into UniProtKB/TrEMBL.
DT 23-OCT-2007, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN Name=folP {ECO:0000313|EMBL:EAT98726.1};
GN ORFNames=CCC13826_2021 {ECO:0000313|EMBL:EAT98726.1};
OS Campylobacter concisus (strain 13826).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360104 {ECO:0000313|EMBL:EAT98726.1, ECO:0000313|Proteomes:UP000001121};
RN [1] {ECO:0000313|Proteomes:UP000001121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13826 {ECO:0000313|Proteomes:UP000001121};
RA Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G.,
RA Mandrell R.E., On S., Nelson K.E.;
RT "Genome sequence of Campylobacter concisus 13826 isolated from human
RT feces.";
RL Submitted (OCT-2007) 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; CP000792; EAT98726.1; -; Genomic_DNA.
DR RefSeq; WP_012140058.1; NC_009802.2.
DR AlphaFoldDB; A7ZEE0; -.
DR STRING; 360104.CCC13826_2021; -.
DR KEGG; cco:CCC13826_2021; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_1_0_7; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000001121; 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 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, ECO:0000313|EMBL:EAT98726.1}.
FT DOMAIN 118..368
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 379 AA; 42666 MW; D2C15CA86B695127 CRC64;
MKFYKINNKS DFDQICKAIS PSPAGAKLMQ KKSEINFIFI DEIKTPAANI LKQDALSVGA
ELVTHNDTIL GKESLNKALL MATNAQLRQL AKKEKLQDFG LKKLAGFLET KFTKPTKPLI
MGVANINRDS FNEQSRINTQ NGIAKIEAMI EAGADYIDLG GVSSRPGSEY CGREEEFRRI
KDIVEEIYRL NLHEKAKFSL DSFDEYCLEF ALNHGFKMIN DITANANLAP LAARYDAEFC
MMHMQGDPAT MQIAPKYNDL IGEISDFFEQ KIVLARELGA KKIVLDVGIG FGKTAEQNLL
LIKHLEHFLK FGCPLLVGAS RKSVINHYYK SEVKERLPGS LYLHLKAFEN GAQIIRTHDV
AEHKQLFDMH EAMSQATLW
//
