ID A0A3N4PJ87_9BACT Unreviewed; 286 AA.
AC A0A3N4PJ87;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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:RPE08286.1};
GN ORFNames=EGT74_14590 {ECO:0000313|EMBL:RPE08286.1};
OS Chitinophaga lutea.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2488634 {ECO:0000313|EMBL:RPE08286.1, ECO:0000313|Proteomes:UP000278351};
RN [1] {ECO:0000313|EMBL:RPE08286.1, ECO:0000313|Proteomes:UP000278351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY74 {ECO:0000313|EMBL:RPE08286.1,
RC ECO:0000313|Proteomes:UP000278351};
RA Zong Y.;
RT "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RPE08286.1}.
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DR EMBL; RPDH01000002; RPE08286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4PJ87; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000278351; Unassembled WGS sequence.
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; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000278351};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RPE08286.1}.
FT DOMAIN 26..278
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 286 AA; 30896 MW; 83E8911503C28785 CRC64;
MKFKNTLLHK DFTICCRGKL VDLSTPAVMG IINVTDDSFY ANSRTRTLHH IVERAGQLLA
DGAVFLDIGA QSTRPGAEMV GAPEETERLL PAIHAILHHY PEALLSVDTF HASVAEKCIL
AGAAIVNDVS AGDMDPDMLA VTASLQAPYI AMHMQGTPAT MQQNPQYTDV TQEVLGYFLQ
KLHQCREAGI KDVILDPGFG FGKTLAHNHI LLQQLDLLQV AGAPILAGVS RKSMIYRLLG
GTPAEALNGT TVLHTIALLN GAAILRAHDV KEAVECVRIV SYQRSL
//
