ID   DPGD_AMYOR              Reviewed;         265 AA.
AC   G4V4T7;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   25-MAY-2022, entry version 29.
DE   RecName: Full=Enoyl-CoA-hydratase {ECO:0000303|PubMed:11752437};
DE            EC=4.2.1.17 {ECO:0000269|PubMed:11752437};
GN   Name=dpgD;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP   SPECIFICITY.
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       syn-addition of a water molecule across the double bond of a trans-2-
CC       enoyl-CoA thioester, resulting in the formation of a beta-hydroxyacyl-
CC       CoA thioester. Physiologically, DpgD could act as a dehydratase,
CC       facilitating the aromatization of the DPA-S-DgpA or DPA-S-CoA
CC       intermediate. It can use the non physiological substrates crotonyl-CoA
CC       and beta-methylcrotonyl-CoA. {ECO:0000269|PubMed:11752437}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:16105, ChEBI:CHEBI:15377, ChEBI:CHEBI:57318,
CC         ChEBI:CHEBI:58856; EC=4.2.1.17;
CC         Evidence={ECO:0000269|PubMed:11752437};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O;
CC         Xref=Rhea:RHEA:20724, ChEBI:CHEBI:15377, ChEBI:CHEBI:58521,
CC         ChEBI:CHEBI:137480; EC=4.2.1.17;
CC         Evidence={ECO:0000269|PubMed:11752437};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=20 uM for crotonyl-CoA {ECO:0000269|PubMed:11752437};
CC         KM=40 uM for beta-methylcrotonyl-CoA {ECO:0000269|PubMed:11752437};
CC         Note=kcat is 1.7 min(-1) for enoyl-CoA-hydratase activity.
CC         {ECO:0000269|PubMed:11752437};
CC   -!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
CC       {ECO:0000305|PubMed:11752437}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; HE589771; CCD33162.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4V4T7; -.
DR   SMR; G4V4T7; -.
DR   STRING; 1125971.ASJB01000062_gene4422; -.
DR   eggNOG; COG1024; Bacteria.
DR   UniPathway; UPA00162; -.
DR   GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
DR   GO; GO:0033072; P:vancomycin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.12.10; -; 1.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR018376; Enoyl-CoA_hyd/isom_CS.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   InterPro; IPR014748; Enoyl-CoA_hydra_C.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
DR   PROSITE; PS00166; ENOYL_COA_HYDRATASE; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Lyase.
FT   CHAIN           1..265
FT                   /note="Enoyl-CoA-hydratase"
FT                   /id="PRO_0000435606"
SQ   SEQUENCE   265 AA;  29008 MW;  ED6635B3A8CD0A12 CRC64;
     MSETRVRYEK KDHVAYVTMD RPAVLNAMDR RMHEELAGIW DDVEADDDVR AVVLTGAGDR
     AFSVGQDLKE RARLNESGVA PTTFGSGGQA GHPRLTDRFT LSKPVVARVR GYALGGGFEL
     VLACDIVIAA EDAVFALPEV RLGLIAGAGG VFRLPRQLPQ KVAMGYLLTG RRMDAATALR
     HGLVNEVVPA AELDQCVADW TDSLVRAAPL SVRAIKEAAL RSVDLPLEEA FTTSYHWEER
     RRRSADAIEG VRAFAEKRDP IWTGQ