ID   DPGA_STRTO              Reviewed;         390 AA.
AC   Q8KLK5;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=3,5-dihydroxyphenylacetyl-CoA synthase {ECO:0000303|PubMed:22492619};
DE            EC=2.3.1.246 {ECO:0000269|PubMed:22492619};
DE   AltName: Full=3,5-dihydroxyphenylacetyl-CoA synthase polyketide synthase type III {ECO:0000305};
OS   Streptomyces toyocaensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=55952;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 15009;
RX   PubMed=9177243; DOI=10.1073/pnas.94.12.6480;
RA   Marshall C.G., Broadhead G., Leskiw B.K., Wright G.D.;
RT   "D-Ala-D-Ala ligases from glycopeptide antibiotic-producing organisms are
RT   highly homologous to the enterococcal vancomycin-resistance ligases VanA
RT   and VanB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:6480-6483(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NRRL 15009;
RX   PubMed=12060705; DOI=10.1073/pnas.102285099;
RA   Pootoolal J., Thomas M.G., Marshall C.G., Neu J.M., Hubbard B.K.,
RA   Walsh C.T., Wright G.D.;
RT   "Assembling the glycopeptide antibiotic scaffold: the biosynthesis of
RT   A47934 from Streptomyces toyocaensis NRRL15009.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8962-8967(2002).
RN   [3]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=22492619; DOI=10.1002/cbic.201200051;
RA   Wu H.C., Li Y.S., Liu Y.C., Lyu S.Y., Wu C.J., Li T.L.;
RT   "Chain elongation and cyclization in type III PKS DpgA.";
RL   ChemBioChem 13:862-871(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of the nonproteinogenic amino
CC       acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the
CC       production of vancomycin and teicoplanin antibiotics. Catalyzes the
CC       Claisen condensation of four molecules of malonyl-CoA to yield 3,5-
CC       dihydroxyphenylacetyl-CoA (DPA-CoA) and three free coenzyme A (CoA).
CC       DpgA requires the presence of the dehydratases DpgB and DpgD to
CC       facilitate the aromatization of the DPA-S-DgpA or DPA-S-CoA
CC       intermediate. {ECO:0000269|PubMed:22492619}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4 H(+) + 4 malonyl-CoA = (3,5-dihydroxyphenyl)acetyl-CoA + 4
CC         CO2 + 3 CoA + H2O; Xref=Rhea:RHEA:44744, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57384, ChEBI:CHEBI:84554; EC=2.3.1.246;
CC         Evidence={ECO:0000269|PubMed:22492619};
CC   -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC       {ECO:0000305|PubMed:22492619}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; U82965; AAM80548.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8KLK5; -.
DR   SMR; Q8KLK5; -.
DR   STRING; 55952.BU52_01210; -.
DR   eggNOG; COG3424; Bacteria.
DR   UniPathway; UPA00162; -.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IDA:UniProtKB.
DR   GO; GO:0033072; P:vancomycin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.47.10; -; 2.
DR   InterPro; IPR012328; Chalcone/stilbene_synt_C.
DR   InterPro; IPR001099; Chalcone/stilbene_synt_N.
DR   InterPro; IPR011141; Polyketide_synthase_type-III.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR11877; PTHR11877; 1.
DR   Pfam; PF02797; Chal_sti_synt_C; 1.
DR   Pfam; PF00195; Chal_sti_synt_N; 1.
DR   PIRSF; PIRSF000451; PKS_III; 1.
DR   SUPFAM; SSF53901; SSF53901; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Transferase.
FT   CHAIN           1..390
FT                   /note="3,5-dihydroxyphenylacetyl-CoA synthase"
FT                   /id="PRO_0000435604"
FT   ACT_SITE        173
FT                   /evidence="ECO:0000250|UniProtKB:Q939X3"
SQ   SEQUENCE   390 AA;  41526 MW;  0A5AEA4943D78E8D CRC64;
     MGVDLQVTVN LDHPELLDAP VLETGVLSAE GRALPTPPRP RIVGVGTAVT RTSYSQQEVL
     DAFGITDRKV RSIFLNSAIE RRNLTLPPMD SDSVRVSESQ GDLLDKHKKL AIEMGAEALH
     ACLKRCGAEL SDLRHLCCVT STGFLTPGLS ALLIRELGID RHCSRSDIVG MGCNAGLNAL
     NVVAGWSAAH PGELAVVLCA EACSAAYTMD STMRTAVVNS LFGDGAAAVA LLAGPGGATP
     ATSEGPTVLK FASCIIPEAV DAMRYDWDRT QGRFSFFLDP QIPYVVGAHA ETVVDRLLSG
     TGLRRSDIGH WLVHSGGKKV IDAVVVNLGL TRHDVRHTIG VLRDQGNVSS GSFLFSYERL
     LEEGITRPGE YGVLMTMGPG STIETALVQW