DB code: S00919

RLCP classification 1.14.30000.10 : Hydrolysis
CATH domain 3.40.50.1820 : Rossmann fold Catalytic domain
E.C. 3.1.2.-
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.50.1820 : Rossmann fold S00544 S00344 S00517 S00525 S00526 S00720 S00723 S00724 S00725 S00057 S00374 S00345 S00347 S00348 S00346 S00350 S00352 S00353 S00355 S00356 S00358 D00189 D00210 D00539 T00253

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
O54157
Thioesterase
NP_630015.1 (Protein)
NC_003888.3 (DNA/RNA sequence)
PF00975 (Thioesterase)
[Graphical View]

KEGG enzyme name
Thioesterase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O54157 O54157_STRCO

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id L00098 C00001 C00060 C16736 I00147 I00085 I00086
E.C.
Compound Thioester H2O Carboxylate R-SH Peptidyl-Ser-tetrahedral intermediate (with previous thioester) Acyl-enzyme(Peptidyl-Ser-acyl group) Peptidyl-Ser-tetrahedral-intermediate
Type carbohydrate,sulfide group H2O carboxyl group sulfhydryl group
ChEBI 15377
 15377
PubChem 22247451
 962
 22247451
 962
3qmvA Unbound Unbound Unbound Unbound Unbound Unbound
3qmvB Unbound Unbound Unbound Unbound Unbound Unbound
3qmvC Unbound Unbound Unbound Unbound Unbound Unbound
3qmvD Unbound Unbound Unbound Unbound Unbound Unbound
3qmwA Unbound Unbound Unbound Unbound Unbound Unbound
3qmwB Unbound Unbound Unbound Unbound Unbound Unbound
3qmwC Unbound Unbound Unbound Unbound Unbound Unbound
3qmwD Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [1]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
3qmvA SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmvB SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmvC SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmvD SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmwA SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmwB SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmwC SER 107;ASP 213;HIS 241 ALA 41;MET 108
3qmwD SER 107;ASP 213;HIS 241 ALA 41;MET 108

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.22564

References
[1]
Resource
Comments
Medline ID
PubMed ID 21543318
Journal J Biol Chem
Year 2011
Volume 286
Pages 22558-69
Authors Whicher JR, Florova G, Sydor PK, Singh R, Alhamadsheh M, Challis GL, Reynolds KA, Smith JL
Title Structure and function of the RedJ protein, a thioesterase from the prodiginine biosynthetic pathway in Streptomyces coelicolor.
Related PDB 3qmv 3qmw
Related UniProtKB O54157

Comments
This enzyme is homologous to Palmitoyl-protein thioesterase (S00350 in EzCatDB) with a similar active site. This enzyme must catalyze a similar hydrolysis reaction of thioester group to that by the homologous enzyme.
According to the literature [1], this enzyme is involved in polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs). This enzyme catalyzes thioester cleavage, which releases the assembled polyketide/peptide from phosphopantetheine arms of acyl/peptidyl carrier protein (ACP/PCP; see U00001 in EzCatDB) as the final reaction step (see [1]).

Created Updated
2012-10-04 2012-10-05