ID I3TJ13_TISMK Unreviewed; 401 AA.
AC I3TJ13;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:AFK52751.1};
GN OrderedLocusNames=TMO_0912 {ECO:0000313|EMBL:AFK52751.1};
OS Tistrella mobilis (strain KA081020-065).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Geminicoccales;
OC Geminicoccaceae; Tistrella.
OX NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK52751.1, ECO:0000313|Proteomes:UP000005258};
RN [1] {ECO:0000313|EMBL:AFK52751.1, ECO:0000313|Proteomes:UP000005258}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK52751.1,
RC ECO:0000313|Proteomes:UP000005258};
RX PubMed=22458477; DOI=10.1021/ja301735a;
RA Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT agents.";
RL J. Am. Chem. Soc. 134:8625-8632(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}.
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DR EMBL; CP003236; AFK52751.1; -; Genomic_DNA.
DR AlphaFoldDB; I3TJ13; -.
DR STRING; 1110502.TMO_0912; -.
DR KEGG; tmo:TMO_0912; -.
DR PATRIC; fig|1110502.3.peg.943; -.
DR eggNOG; COG0294; Bacteria.
DR HOGENOM; CLU_008023_0_1_5; -.
DR Proteomes; UP000005258; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 138..391
FT /note="Pterin-binding"
FT /evidence="ECO:0000259|PROSITE:PS50972"
SQ SEQUENCE 401 AA; 41655 MW; 34AD4D79939C20CC CRC64;
MAHDLPANAA AASSDAAAAA SLETRIREGD AGLRLYARPF GFAPVAVTPG AGLLKPATRL
PGPGFRRLAG GWLAFDMVEL LWRGGEGRPG RVVLPVEAAL RLADRVMEYP GGRRLARRLR
ALEAPRQRFA GLDLQRRARV MAIVNVTPDS FSDGGDAFAP ADAAAAVRRA LADGADLLDL
GAESTRPGAA DIDPAEEIRR LDPALDEASA AGAVVSVDTR KGAVMHHAAG RGAAIANDVS
GFTYDPAAAG VVAQTGLSAV AMHMRGTPET MQQLTGYDDV VLDVFDELED RLVLLDEAGV
SPGQVAVDPG IGFSKTVDQN LALLHNLSIF HGLGRPLLIG VSRKSFIGRI TGEEAPRARV
PGSLAAALLA VGQGAQIVRV HDVAETVQAL VVGQAIGRGR A
//
