ID A0A1Z9TAX8_9PROT Unreviewed; 349 AA.
AC A0A1Z9TAX8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=CBE33_01680 {ECO:0000313|EMBL:OUX38130.1};
OS Candidatus Pelagibacter sp. TMED273.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae; Pelagibacter.
OX NCBI_TaxID=1986826 {ECO:0000313|EMBL:OUX38130.1, ECO:0000313|Proteomes:UP000195608};
RN [1] {ECO:0000313|EMBL:OUX38130.1, ECO:0000313|Proteomes:UP000195608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED273 {ECO:0000313|EMBL:OUX38130.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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:OUX38130.1}.
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DR EMBL; NHLS01000009; OUX38130.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9TAX8; -.
DR Proteomes; UP000195608; Unassembled WGS sequence.
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; 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}.
FT DOMAIN 89..342
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 349 AA; 40170 MW; 2A63B2B2E2E8F825 CRC64;
MDKYYTRACN FYFGKNSQEK IKKNLALPLG GNKNISFDNI EIISRKKKKK IYFKEVKSLS
KNLKKKIQHD LKFIIKKKRF KKLNLNETPL IMGIANLTPD SFSDGGLYNK GEKSFSHIKK
LLKQGCDILD VGGESTRPGS NEVEEKVEWK RIKNVLKKFK TNKIFLSLDT RKSMIMKKAI
KFNINLINDI SGLEDDKDTI EFLKKNKIPF VINHIKGTPK TMHKKPKYKN VLLDVYDYFS
NKINKLRKSG INHNNIILDP GIGFGKNLKH NITLLSKISI FHSLGFPIML GISRKKYIRD
LSRANDSKER IGGTTATSLF AITQGIQILR VHDVNEVKQS IKVFKSLYK
//
