EzCatDB: S00919
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeS00919
RLCP classification1.14.30000.10 : Hydrolysis
CATH domainDomain 13.40.50.1820 : Rossmann foldCatalytic domain
E.C.3.1.2.-

CATH domainRelated DB codes (homologues)
3.40.50.1820 : Rossmann foldS00544,S00344,S00517,S00525,S00526,S00720,S00723,S00724,S00725,S00057,S00374,S00345,S00347,S00348,S00346,S00350,S00352,S00353,S00355,S00356,S00358,D00189,D00210,D00539,T00253

Enzyme Name
UniProtKBKEGG

O54157
Protein name
Thioesterase
SynonymsThioesterase
RefSeqNP_630015.1 (Protein)
NC_003888.3 (DNA/RNA sequence)
PfamPF00975 (Thioesterase)
[Graphical view]


UniProtKB:Accession NumberO54157
Entry nameO54157_STRCO
Activity
Subunit
Subcellular location
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProductsintermediates
KEGG-idL00098C00001C00060C16736I00147I00085I00086
CompoundThioesterH2OCarboxylateR-SHPeptidyl-Ser-tetrahedral intermediate (with previous thioester)Acyl-enzyme(Peptidyl-Ser-acyl group)Peptidyl-Ser-tetrahedral-intermediate
Typecarbohydrate,sulfide groupH2Ocarboxyl groupsulfhydryl group


ChEBI
15377





PubChem
962
22247451





               
3qmvAUnbound UnboundUnboundUnboundUnboundUnbound
3qmvBUnbound UnboundUnboundUnboundUnboundUnbound
3qmvCUnbound UnboundUnboundUnboundUnboundUnbound
3qmvDUnbound UnboundUnboundUnboundUnboundUnbound
3qmwAUnbound UnboundUnboundUnboundUnboundUnbound
3qmwBUnbound UnboundUnboundUnboundUnboundUnbound
3qmwCUnbound UnboundUnboundUnboundUnboundUnbound
3qmwDUnbound UnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [1]
pdbCatalytic residuesMain-chain involved in catalysis
          
3qmvASER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmvBSER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmvCSER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmvDSER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmwASER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmwBSER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmwCSER 107;ASP 213;HIS 241
ALA 41;MET 108
3qmwDSER 107;ASP 213;HIS 241
ALA 41;MET 108

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]p.22564

references
[1]
PubMed ID21543318
JournalJ Biol Chem
Year2011
Volume286
Pages22558-69
AuthorsWhicher JR, Florova G, Sydor PK, Singh R, Alhamadsheh M, Challis GL, Reynolds KA, Smith JL
TitleStructure and function of the RedJ protein, a thioesterase from the prodiginine biosynthetic pathway in Streptomyces coelicolor.
Related PDB3qmv,3qmw
Related UniProtKBO54157

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]).

createdupdated
2012-10-042012-10-05
Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.