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Entry: C9YXA2_STRSW
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Original site: C9YXA2_STRSW 
ID   C9YXA2_STRSW            Unreviewed;       307 AA.
AC   C9YXA2;
DT   24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   24-NOV-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
DE   RecName: Full=Dihydropteroate synthase {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE            Short=DHPS {ECO:0000256|RuleBase:RU361205};
DE            EC=2.5.1.15 {ECO:0000256|ARBA:ARBA00012458, ECO:0000256|RuleBase:RU361205};
DE   AltName: Full=Dihydropteroate pyrophosphorylase {ECO:0000256|RuleBase:RU361205};
GN   Name=folP {ECO:0000313|EMBL:CBG67882.1};
GN   OrderedLocusNames=SCAB_6911 {ECO:0000313|EMBL:CBG67882.1};
OS   Streptomyces scabiei (strain 87.22).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=680198 {ECO:0000313|EMBL:CBG67882.1, ECO:0000313|Proteomes:UP000001444};
RN   [1] {ECO:0000313|EMBL:CBG67882.1, ECO:0000313|Proteomes:UP000001444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=87.22 {ECO:0000313|EMBL:CBG67882.1,
RC   ECO:0000313|Proteomes:UP000001444};
RX   PubMed=20064060; DOI=10.1094/MPMI-23-2-0161;
RA   Bignell D.R., Seipke R.F., Huguet-Tapia J.C., Chambers A.H., Parry R.J.,
RA   Loria R.;
RT   "Streptomyces scabies 87-22 contains a coronafacic acid-like biosynthetic
RT   cluster that contributes to plant-microbe interactions.";
RL   Mol. Plant Microbe Interact. 23:161-175(2010).
CC   -!- FUNCTION: Catalyzes the condensation of para-aminobenzoate (pABA) with
CC       6-hydroxymethyl-7,8-dihydropterin diphosphate (DHPt-PP) to form 7,8-
CC       dihydropteroate (H2Pte), the immediate precursor of folate derivatives.
CC       {ECO:0000256|RuleBase:RU361205}.
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         ECO:0000256|RuleBase:RU361205};
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, ECO:0000256|RuleBase:RU361205}.
CC   -!- SIMILARITY: Belongs to the DHPS family.
CC       {ECO:0000256|RuleBase:RU361205}.
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DR   EMBL; FN554889; CBG67882.1; -; Genomic_DNA.
DR   AlphaFoldDB; C9YXA2; -.
DR   STRING; 680198.SCAB_6911; -.
DR   KEGG; scb:SCAB_6911; -.
DR   eggNOG; COG0294; Bacteria.
DR   HOGENOM; CLU_008023_0_1_11; -.
DR   OMA; EAPMNKS; -.
DR   UniPathway; UPA00077; UER00156.
DR   Proteomes; UP000001444; Chromosome.
DR   GO; GO:0004156; F:dihydropteroate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniPathway.
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; PS00792; DHPS_1; 1.
DR   PROSITE; PS00793; DHPS_2; 1.
DR   PROSITE; PS50972; PTERIN_BINDING; 1.
PE   3: Inferred from homology;
KW   Folate biosynthesis {ECO:0000256|ARBA:ARBA00022909,
KW   ECO:0000256|RuleBase:RU361205};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU361205};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU361205};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001444};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361205}.
FT   DOMAIN          30..289
FT                   /note="Pterin-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50972"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  32009 MW;  193FB27CD1ABA44E CRC64;
     MTVTIHAPAT PAHPGTPDLH PHGLPRPGRT LVMGVVNVTP DSFSDGGLSF AADAAVAHGR
     ALLEQGADLV DVGGESTRPG AARPPVEEEL RRVLPVVRAL AADGAVVSVD TMRAEVAARA
     LEAGARLVND VSGGLADPGM LPLMARAGVP YVLMHWRGHS AGMQANALYR DVVDEVLGEV
     RLRIDAALEA GVPPGSLIVD PGLGFAKTPE HNWELLARLG EVRALGRPVL LGASRKAFLG
     RLLADRTTGE PRPARERDAA TAAVSVLAAA QGVWCLRVHD VVSTLDAVRV TARWGAEASV
     AVRAPLR
//
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