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Enoyl-CoA-hydratase (EC 4.2.1.17)

 DPGB_AMYOR              Reviewed;         217 AA.
G4V4T5;
17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
14-DEC-2011, sequence version 1.
22-NOV-2017, entry version 14.
RecName: Full=Enoyl-CoA-hydratase {ECO:0000303|PubMed:11752437};
EC=4.2.1.17 {ECO:0000269|PubMed:11752437};
Name=dpgB;
Amycolatopsis orientalis (Nocardia orientalis).
Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
Amycolatopsis.
NCBI_TaxID=31958;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC19795;
Woertz T., Dietz S., Zerbe K., Robinson J.A.;
"The vancomycin biosynthetic gene cluster.";
Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
[2]
FUNCTION, AND CATALYTIC ACTIVITY.
STRAIN=NRRL18098;
PubMed=11752437; DOI=10.1073/pnas.221582098;
Chen H., Tseng C.C., Hubbard B.K., Walsh C.T.;
"Glycopeptide antibiotic biosynthesis: enzymatic assembly of the
dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.";
Proc. Natl. Acad. Sci. U.S.A. 98:14901-14906(2001).
-!- FUNCTION: Involved in the biosynthesis of the nonproteinogenic
amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg)
responsible of the production of vancomycin and teicoplanin
antibiotics. Catalyzes the syn-addition of a water molecule across
the double bond of a trans-2-enoyl-CoA thioester, resulting in the
formation of a beta-hydroxyacyl-CoA thioester. Physiologically,
DpgB could act as a dehydratase, facilitating the aromatization of
the DPA-S-DgpA or DPA-S-CoA intermediate.
{ECO:0000269|PubMed:11752437}.
-!- CATALYTIC ACTIVITY: (3S)-3-hydroxyacyl-CoA = trans-2(or 3)-enoyl-
CoA + H(2)O. {ECO:0000269|PubMed:11752437}.
-!- PATHWAY: Antibiotic biosynthesis; vancomycin biosynthesis.
{ECO:0000305|PubMed:11752437}.
-!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
{ECO:0000305}.
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EMBL; HE589771; CCD33160.1; -; Genomic_DNA.
SMR; G4V4T5; -.
UniPathway; UPA00162; -.
GO; GO:0004300; F:enoyl-CoA hydratase activity; IDA:UniProtKB.
GO; GO:0033072; P:vancomycin biosynthetic process; IEA:UniProtKB-UniPathway.
InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
SUPFAM; SSF52096; SSF52096; 1.
1: Evidence at protein level;
Antibiotic biosynthesis; Lyase.
CHAIN 1 217 Enoyl-CoA-hydratase.
/FTId=PRO_0000435605.
SEQUENCE 217 AA; 22686 MW; D6EDD164011B98CB CRC64;
MNGELVLRLD GARPLSPASV EELSALCDRA EDDREAGPVT VHVTGVPSAG WTAGLTVGLV
SKWERVVRRF ERLGRLTIAV ASGECAGTAL DLLLAADLRI VTPGTRLRLA PVGGSTWPGM
SVYRLTQQAG AAGIRRAVLL GTPIEVDRAL ALNLVDEVSD DPAKTLAGLA EAAAALDGAE
TAIRRQLIFE DGSTTFEDAL GAHLAAADRA LRREATS


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