ID Q2TBZ6_ASTYP Unreviewed; 293 AA.
AC Q2TBZ6;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:AAY45872.1};
OS Aster yellows phytoplasma.
OC Bacteria; Mycoplasmatota; Mollicutes; Acholeplasmatales;
OC Acholeplasmataceae; Phytoplasma; 16SrI (Aster yellows group).
OX NCBI_TaxID=35779 {ECO:0000313|EMBL:AAY45872.1};
RN [1] {ECO:0000313|EMBL:AAY45872.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AY1 {ECO:0000313|EMBL:AAY45872.1};
RX PubMed=16332180; DOI=10.1089/dna.2005.24.832;
RA Davis R.E., Jomantiene R., Zhao Y.;
RT "Lineage-specific decay of folate biosynthesis genes suggests ongoing host
RT adaptation in phytoplasmas.";
RL DNA Cell Biol. 24:832-840(2005).
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; AY998977; AAY45872.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2TBZ6; -.
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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 33..284
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 293 AA; 32774 MW; BADF4F73E6CE8B87 CRC64;
MMGLNNQTIN LYSKHPKIWK LAHNRQIEIS HKSLIMAIIN VTPDSFSDGN QHFTTQKAVN
HALRCLKEGV DIIDIGGEST RPGAIPITPL EEQKRILPVI KELSRHPKAI ISVDTYHFQT
AKLAIKAGAH IINDVCGLQQ NPQMAQTIAS LNAGVCIMHT GRNRKKLSNA LQDQFYFLNH
SLEIAKQAQI ATEAIVIDPG FGFEKNIDEN FDIIKEFEQL TKMELPILVG LSRKRFLKAI
IPTESLLQVE SLDAITATAN FLLRTKGASI FRVHNVKMNK NSLLLADTLM KKI
//
