ID   DPGA_AMYOR              Reviewed;         370 AA.
AC   G4V4T4;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 25.
DE   RecName: Full=3,5-dihydroxyphenylacetyl-CoA synthase {ECO:0000303|PubMed:11752437};
DE            EC=2.3.1.246 {ECO:0000269|PubMed:11752437};
DE   AltName: Full=3,5-dihydroxyphenylacetyl-CoA synthase polyketide synthase type III {ECO:0000305};
GN   Name=dpgA;
OS   Amycolatopsis orientalis (Nocardia orientalis).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Amycolatopsis.
OX   NCBI_TaxID=31958;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC19795;
RA   Woertz T., Dietz S., Zerbe K., Robinson J.A.;
RT   "The vancomycin biosynthetic gene cluster.";
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=NRRL18098;
RX   PubMed=11752437; DOI=10.1073/pnas.221582098;
RA   Chen H., Tseng C.C., Hubbard B.K., Walsh C.T.;
RT   "Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated
RT   amino acid monomer (S)-3,5-dihydroxyphenylglycine.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:14901-14906(2001).
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:11752437}.
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:11752437};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=5 uM for malonyl-CoA {ECO:0000269|PubMed:11752437};
CC         Note=kcat is 1 min(-1) for transferase activity with malonyl-CoA as
CC         substrate. {ECO:0000269|PubMed:11752437};
CC   -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC       {ECO:0000305|PubMed:11752437}.
CC   -!- SIMILARITY: Belongs to the thiolase-like superfamily. Chalcone/stilbene
CC       synthases family. {ECO:0000305}.
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DR   EMBL; HE589771; CCD33159.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4V4T4; -.
DR   SMR; G4V4T4; -.
DR   STRING; 1125971.ASJB01000062_gene4419; -.
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..370
FT                   /note="3,5-dihydroxyphenylacetyl-CoA synthase"
FT                   /id="PRO_0000435602"
FT   ACT_SITE        158
FT                   /evidence="ECO:0000250|UniProtKB:Q939X3"
SQ   SEQUENCE   370 AA;  39582 MW;  1A08B816E38282F5 CRC64;
     MDVSMTTGIE LTEELSVLNG LTEITRFAGV GTAVSETSYS QTELLDILDV EDPKIRSVFL
     NSAIDRRFLT LPPENPGGGR LAEPQGDLLD KHKKIAVDMG CRALEACLKS AGATLSDLRH
     LCCVTSTGFL TPGLSALIIR EMGIDPHCSR SDIVGMGCNA GLNALNVVSG WSAAHPGELG
     VVLCSEACSA AYALDGTMRT AVVNSLFGDG SAALAVISGD GRVAGPRVLK FASYIITDAV
     DAMRYDWDRD QDRFSFFLDP QIPYVVGAHA EIVVDRLLSG TGLRRSDIGH WLVHSGGKKV
     VDAVVVNLGL SRHDVRHTTG VLRDYGNLSS GSFLFSYERL SEEDVTRPGD YGVLMTMGPG
     STIEMALIQW