ID A0A1D8S0R5_9GAMM Unreviewed; 260 AA.
AC A0A1D8S0R5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:AOW78944.1};
GN ORFNames=A3Q34_01990 {ECO:0000313|EMBL:AOW78944.1};
OS Colwellia sp. PAMC 20917.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Colwelliaceae; Colwellia.
OX NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW78944.1, ECO:0000313|Proteomes:UP000177820};
RN [1] {ECO:0000313|EMBL:AOW78944.1, ECO:0000313|Proteomes:UP000177820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW78944.1,
RC ECO:0000313|Proteomes:UP000177820};
RA Kim H.-W.;
RT "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL Submitted (MAR-2016) 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; CP014944; AOW78944.1; -; Genomic_DNA.
DR RefSeq; WP_070376966.1; NZ_CP014944.1.
DR AlphaFoldDB; A0A1D8S0R5; -.
DR STRING; 1816218.A3Q34_01990; -.
DR KEGG; coz:A3Q34_01990; -.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000177820; 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; 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; PS00793; DHPS_2; 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:UP000177820};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..251
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 260 AA; 28093 MW; A3FD5D35C064BF37 CRC64;
MGILNVTPDS FSDGGQFSRI DSALRQAEQM IADGATIIDI GGESTRPGAK EVSVKDELAR
VIPVLKAINA RFNIIVSIDT SKAEVMSEGI TYGAGIINDV RALQNEGCLT VLAQDQGVGI
CLMHMQGLPR TMQHNPHYVN LIDDITTFFQ ERILACTQAG INRSSLILDP GFGFGKSLEQ
NYCLLANMAK FQCLDLPVLA GLSRKSMIGN LLNREVNERL AGSLATAIIA AQQGARIIRV
HDVKETVDAL KVLQATTINR
//
