IED Industry Enzyme Database

Detail Information for IndEnz0010001538
IED ID IndEnz0010001538
Enzyme Type ID esterase001538
Protein Name Thioesterase 1/protease 1/lysophospholipase L1
TAP
Acyl-CoA thioesterase 1
TESA
EC 3.1.2.2
Acyl-CoA thioesterase I
Arylesterase
EC 3.1.1.2
Lysophospholipase L1
EC 3.1.1.5
Oleoyl-
acyl-carrier-protein hydrolase
EC 3.1.2.14
Phospholipid degradation C
Pldc
Protease 1
EC 3.4.21.-
Protease I
Thioesterase I/protease I
TEP-I
Gene Name tesA c0615
Organism Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Enzyme Sequence MMNFNNVFRWHLPFLFLVLLTFRAAAADTLLILGDSLSAGYRMSASAAWPALLNDKWQSKTSVVNASISGDTSQQGLARLPALLKQHQPRWVLVELGGNDGLRGFQPQQTEQTLRQILQDVKAANAEPLLMQIRLPANYGRRYNEAFSAIYPKLAKEFDVPLLPFFMEEVYLKPQWMQDDGIHPNRDAQPFIADWMAKQLQPLVNHDS
Enzyme Length 208
Uniprot Accession Number P0ADA2
Absorption
Active Site ACT_SITE 36; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P0ADA1; ACT_SITE 180; /evidence=ECO:0000250|UniProtKB:P0ADA1; ACT_SITE 183; /evidence=ECO:0000250|UniProtKB:P0ADA1
Activity Regulation
Binding Site BINDING 70; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0ADA1; BINDING 99; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0ADA1
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a fatty acyl-CoA + H2O = a fatty acid + CoA + H(+); Xref=Rhea:RHEA:16781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57287, ChEBI:CHEBI:77636; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16782; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate; Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=(9Z)-hexadecenoyl-CoA + H2O = (9Z)-hexadecenoate + CoA + H(+); Xref=Rhea:RHEA:40131, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372, ChEBI:CHEBI:57287, ChEBI:CHEBI:61540; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40132; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=H2O + octadecanoyl-CoA = CoA + H(+) + octadecanoate; Xref=Rhea:RHEA:30139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:57287, ChEBI:CHEBI:57394; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30140; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-CoA + H2O = (9Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:40139, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:57287, ChEBI:CHEBI:57387; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40140; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15058; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=(11Z)-octadecenoyl-CoA + H2O = (11Z)-octadecenoate + CoA + H(+); Xref=Rhea:RHEA:65240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30827, ChEBI:CHEBI:57287, ChEBI:CHEBI:75121; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65241; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=H2O + tetradecanoyl-CoA = CoA + H(+) + tetradecanoate; Xref=Rhea:RHEA:40119, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30807, ChEBI:CHEBI:57287, ChEBI:CHEBI:57385; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40120; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + CoA + H(+); Xref=Rhea:RHEA:40151, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395, ChEBI:CHEBI:57287, ChEBI:CHEBI:57368; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40152; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=dodecanoyl-CoA + H2O = CoA + dodecanoate + H(+); Xref=Rhea:RHEA:30135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18262, ChEBI:CHEBI:57287, ChEBI:CHEBI:57375; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30136; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=decanoyl-CoA + H2O = CoA + decanoate + H(+); Xref=Rhea:RHEA:40059, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:27689, ChEBI:CHEBI:57287, ChEBI:CHEBI:61430; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40060; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=H2O + hexanoyl-CoA = CoA + H(+) + hexanoate; Xref=Rhea:RHEA:40115, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:57287, ChEBI:CHEBI:62620; Evidence={ECO:0000250|UniProtKB:P0ADA1};PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40116; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+); Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=a butanoate ester + H2O = an aliphatic alcohol + butanoate + H(+); Xref=Rhea:RHEA:47348, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17968, ChEBI:CHEBI:50477; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=a hexanoate ester + H2O = an aliphatic alcohol + H(+) + hexanoate; Xref=Rhea:RHEA:47352, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17120, ChEBI:CHEBI:87656; Evidence={ECO:0000250|UniProtKB:P0ADA1}; CATALYTIC ACTIVITY: Reaction=an octanoate ester + H2O = an aliphatic alcohol + H(+) + octanoate; Xref=Rhea:RHEA:47356, ChEBI:CHEBI:2571, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:25646, ChEBI:CHEBI:87657; Evidence={ECO:0000250|UniProtKB:P0ADA1};
DNA Binding
EC Number 3.1.2.2; 3.1.1.2; 3.1.1.5; 3.1.2.14; 3.4.21.-
Enzyme Function FUNCTION: TesA is a multifunctional esterase that can act as a thioesterase, arylesterase, lysophospholipase and protease. {ECO:0000250|UniProtKB:P0ADA1}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Binding site (2); Chain (1); Erroneous initiation (1); Signal peptide (1)
Keywords Hydrolase;Periplasm;Protease;Signal
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Periplasm {ECO:0000250|UniProtKB:P0ADA1}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..26; /evidence=ECO:0000250|UniProtKB:P0ADA1
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 23,622
Kinetics
Metal Binding
Rhea ID RHEA:16781; RHEA:16782; RHEA:16645; RHEA:16646; RHEA:40131; RHEA:40132; RHEA:30139; RHEA:30140; RHEA:40139; RHEA:40140; RHEA:15057; RHEA:15058; RHEA:65240; RHEA:65241; RHEA:40119; RHEA:40120; RHEA:40151; RHEA:40152; RHEA:30135; RHEA:30136; RHEA:40059; RHEA:40060; RHEA:40115; RHEA:40116; RHEA:15177; RHEA:17309; RHEA:47348; RHEA:47352; RHEA:47356
Cross Reference Brenda