ID A6EFV4_9SPHI Unreviewed; 286 AA.
AC A6EFV4;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=PBAL39_03939 {ECO:0000313|EMBL:EDM35663.1};
OS Pedobacter sp. BAL39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=391596 {ECO:0000313|EMBL:EDM35663.1, ECO:0000313|Proteomes:UP000003664};
RN [1] {ECO:0000313|EMBL:EDM35663.1, ECO:0000313|Proteomes:UP000003664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BAL39 {ECO:0000313|EMBL:EDM35663.1,
RC ECO:0000313|Proteomes:UP000003664};
RA Hagstrom A., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-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}.
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:EDM35663.1}.
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DR EMBL; ABCM01000012; EDM35663.1; -; Genomic_DNA.
DR RefSeq; WP_008243311.1; NZ_ABCM01000012.1.
DR AlphaFoldDB; A6EFV4; -.
DR STRING; 391596.PBAL39_03939; -.
DR eggNOG; COG0294; Bacteria.
DR OrthoDB; 9811744at2; -.
DR Proteomes; UP000003664; Unassembled WGS sequence.
DR GO; GO:0004156; F:dihydropteroate synthase activity; IEA:InterPro.
DR GO; GO:0009396; P:folic acid-containing compound biosynthetic process; IEA:InterPro.
DR CDD; cd00739; DHPS; 1.
DR Gene3D; 3.20.20.20; Dihydropteroate synthase-like; 1.
DR InterPro; IPR045031; DHP_synth.
DR InterPro; IPR006390; DHP_synth_dom.
DR InterPro; IPR011005; Dihydropteroate_synth-like.
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:UP000003664};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 25..277
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 286 AA; 31717 MW; 54960ECF53FAD8EF CRC64;
MAKDTFLNRK TTLNLKGKLV DLSKPAVMGI LNLTPDSFYE DSRADSAAEV LRRTENFLKD
GALFIDIGAY STRPGAAEVT EAEELKRMVP MVELISRNFP EAYLSTDTFR ASVAKATIEA
GADLINDVSG GEIDKEMFET VAALQVPYIL MHMRGTPQDM QQHTGYQDIG LDLVDYFSAK
VADLRGRGVK DIILDPGFGF AKSTAENYQL LNQLENFDLF ELPMLVGFSR KSMIYKFLNT
SPQEALNGTS VLNTIALMKG ANILRVHDVK AAMECIALVE QVQHQY
//