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Database: UniProt
Entry: A6EFV4_9SPHI
LinkDB: A6EFV4_9SPHI
Original site: A6EFV4_9SPHI 
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
//
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