ID J2D3R2_9SPHN Unreviewed; 374 AA.
AC J2D3R2;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458};
DE EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458};
GN ORFNames=PMI04_01520 {ECO:0000313|EMBL:EJK84289.1};
OS Sphingobium sp. AP49.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1144307 {ECO:0000313|EMBL:EJK84289.1};
RN [1] {ECO:0000313|EMBL:EJK84289.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP49 {ECO:0000313|EMBL:EJK84289.1};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJK84289.1}.
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DR EMBL; AJVL01000028; EJK84289.1; -; Genomic_DNA.
DR RefSeq; WP_007708466.1; NZ_CP124576.1.
DR AlphaFoldDB; J2D3R2; -.
DR STRING; 1144307.PMI04_01520; -.
DR PATRIC; fig|1144307.3.peg.1476; -.
DR eggNOG; COG0294; Bacteria.
DR OrthoDB; 9811744at2; -.
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; PS00792; DHPS_1; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 106..361
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 374 AA; 39038 MW; 5B40E126664579CB CRC64;
MLLPQIPADA RLYLKPTWFV PSPIGLPDGT VARMGNGLIW FQAYELTARG DGQRLVRMTV
PVADFDAVVA RLPDALAARA RQLATNISGT RAPLNLGGRT IRFDAPQLMA ILNITPDSFS
DGGKHMEDAQ AAADAGFAMA AAGAALIDVG GESTRPKAPR LWEGDEIARI VPVIEKLSAS
GVAISVDTRK AAVMEAALAA GAHVINDVSA LEHDPRSLEV AVRAGCPVIL MHAPSTGDDP
HDNPGGYGDV VADVFDYLDA RIAACLDAGI AREKIMVDPG LGFGKSLADN LALVNGLATF
QGLGVPLLFA GSRKRLIGAL SNEAPAADRL GGSVALAFRA AQLGAQMVRV HDVKESVQAL
HLWRGLADAG LSMV
//
