ID   DPGC_AMYOR              Reviewed;         434 AA.
AC   G4V4T6;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   14-DEC-2011, sequence version 1.
DT   03-AUG-2022, entry version 26.
DE   RecName: Full=(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase {ECO:0000303|PubMed:11752437};
DE            EC=1.13.11.80 {ECO:0000269|PubMed:11752437};
GN   Name=dpgC;
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       unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-
CC       dihydroxyphenylglyoxylate. DpgC performed a net four-electron oxidation
CC       of the benzylic carbon of DPA-CoA and the hydrolysis of the thioester
CC       bond to generate free CoA. It can also use phenylacetyl-CoA (PA-CoA) as
CC       substrate. {ECO:0000269|PubMed:11752437}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-
CC         dihydroxyphenyl)-2-oxoacetate + CoA + H(+); Xref=Rhea:RHEA:44632,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:75210, ChEBI:CHEBI:84554; EC=1.13.11.80;
CC         Evidence={ECO:0000269|PubMed:11752437};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=6 uM for DPA-CoA {ECO:0000269|PubMed:11752437};
CC         KM=300 uM for PA-CoA {ECO:0000269|PubMed:11752437};
CC         Note=kcat is 10 min(-1) for dioxygenase activity.
CC         {ECO:0000269|PubMed:11752437};
CC   -!- SUBUNIT: Homohexamer; dimer of trimers. {ECO:0000250|UniProtKB:Q8KLK7}.
CC   -!- SIMILARITY: Belongs to the enoyl-CoA hydratase/isomerase family.
CC       {ECO:0000305}.
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DR   EMBL; HE589771; CCD33161.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4V4T6; -.
DR   SMR; G4V4T6; -.
DR   STRING; 1125971.ASJB01000062_gene4421; -.
DR   eggNOG; COG1024; Bacteria.
DR   BRENDA; 1.13.11.80; 315.
DR   GO; GO:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IDA:UniProtKB.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR   InterPro; IPR001753; Enoyl-CoA_hydra/iso.
DR   Pfam; PF00378; ECH_1; 1.
DR   SUPFAM; SSF52096; SSF52096; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Oxidoreductase.
FT   CHAIN           1..434
FT                   /note="(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase"
FT                   /id="PRO_0000435522"
FT   BINDING         184
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
FT   BINDING         190
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
FT   BINDING         223..226
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
FT   BINDING         234..239
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
FT   BINDING         322..324
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
FT   BINDING         413
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q8KLK7"
SQ   SEQUENCE   434 AA;  47089 MW;  6AACB8A601BDED25 CRC64;
     MTTDSPTLSL SPGLDHRALA KAAQRVDELL DGLPSPSART PAQREAASSA LDEIRAARTE
     YVEAHAEEIY DRLTDGRTRY LRLDELVRAA ASAYPGLVPT EAQMAAERSR RQAEKEGREI
     DQGIFLRGIL SAPKAGPHLL DAMLRPTARA LELLPEFVET GVVRMEAASL ERRDGVAYLT
     LCRDDCLNAE DAQQVDDMET AVDLALLDPA VRVGMLRGGV MSHPRYAGRR VFCAGINLKK
     LSSGDIPLVD FLLRRELGYI HKIVRGVATD GSWRARVIDK PWLAAVDSFA IGGGAQLLLV
     FDHVVAASDA YFSLPAATEG IIPGAANYRL SRFTGPRLAR QVILGGRRIT ADEPDARLLV
     DQVVPPEEMD AAIESALAAL DGDAVRANRR MVNLAEEPPD GFRRYMAEFA LQQALRIYGA
     DVIGKVGGFA AGSR