| IED ID | IndEnz0010001039 |
| Enzyme Type ID | esterase001039 |
| Protein Name |
1,4-dihydroxy-2-naphthoyl-CoA hydrolase DHNA-CoA hydrolase EC 3.1.2.28 DHNA-CoA thioesterase |
| Gene Name | menI ydiI b1686 JW1676 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MIWKRKITLEALNAMGEGNMVGFLDIRFEHIGDDTLEATMPVDSRTKQPFGLLHGGASVVLAESIGSVAGYLCTEGEQKVVGLEINANHVRSAREGRVRGVCKPLHLGSRHQVWQIEIFDEKGRLCCSSRLTTAIL |
| Enzyme Length | 136 |
| Uniprot Accession Number | P77781 |
| Absorption | |
| Active Site | ACT_SITE 63; /note="Nucleophile or proton acceptor"; /evidence="ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000303|PubMed:25010423" |
| Activity Regulation | |
| Binding Site | BINDING 82; /note="Substrate; via carbonyl oxygen"; /evidence="ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000269|PubMed:25010423" |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=1,4-dihydroxy-2-naphthoyl-CoA + H2O = 1,4-dihydroxy-2-naphthoate + CoA + H(+); Xref=Rhea:RHEA:26309, ChEBI:CHEBI:11173, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:58897; EC=3.1.2.28; Evidence={ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000269|PubMed:23564174, ECO:0000269|PubMed:24992697}; |
| DNA Binding | |
| EC Number | 3.1.2.28 |
| Enzyme Function | FUNCTION: Catalyzes the hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA). Also shows significant activity toward a wide range of acyl-CoA thioesters, and minimal activity toward benzoyl-holoEntB. {ECO:0000269|PubMed:15808744, ECO:0000269|PubMed:23564174, ECO:0000269|PubMed:24992697}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Quinol/quinone metabolism; 1,4-dihydroxy-2-naphthoate biosynthesis; 1,4-dihydroxy-2-naphthoate from chorismate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000269|PubMed:23564174, ECO:0000269|PubMed:24992697}.; PATHWAY: Quinol/quinone metabolism; menaquinone biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01936, ECO:0000269|PubMed:23564174, ECO:0000269|PubMed:24992697}. |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (7); Binding site (1); Chain (1); Helix (3); Mutagenesis (14); Region (2); Turn (2) |
| Keywords | 3D-structure;Hydrolase;Menaquinone biosynthesis;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (6) |
| Cross Reference PDB | 1SBK; 1VH5; 1VI8; 4K49; 4K4A; 4K4B; |
| Mapped Pubmed ID | 15690043; 16606699; |
| Motif | |
| Gene Encoded By | |
| Mass | 14,945 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.5 uM for 1,4-dihydroxy-2-naphthoyl-CoA {ECO:0000269|PubMed:23564174}; KM=8 uM for 1,4-dihydroxy-2-naphthoyl-CoA {ECO:0000269|PubMed:24992697}; KM=1.3 uM for oleoyl-CoA {ECO:0000269|PubMed:24992697}; KM=1.5 uM for myristoyl-CoA {ECO:0000269|PubMed:24992697}; KM=1.559 uM for acetyl-CoA {ECO:0000269|PubMed:23564174}; KM=1.9 uM for palmitoyl-CoA {ECO:0000269|PubMed:24992697}; KM=2.2 uM for lauroyl-CoA {ECO:0000269|PubMed:24992697}; KM=8.0 uM for 1-hydroxy-2-naphthoyl-CoA {ECO:0000269|PubMed:23564174}; KM=9 uM for 4-hydroxybenzoyl-CoA {ECO:0000269|PubMed:24992697}; KM=21 uM for hexanoyl-CoA {ECO:0000269|PubMed:24992697}; KM=25 uM for benzoyl-CoA {ECO:0000269|PubMed:24992697}; KM=26.5 uM for 3,5-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:23564174}; KM=26.9 uM for 3,4-dihydroxybenzoyl-CoA {ECO:0000269|PubMed:23564174}; KM=30 uM for coumaroyl-CoA {ECO:0000269|PubMed:24992697}; KM=54 uM for benzoyl-ACP {ECO:0000269|PubMed:24992697}; KM=69.4 uM for beta-methylcrotonyl-CoA {ECO:0000269|PubMed:24992697}; KM=73 uM for salicylyl-CoA {ECO:0000269|PubMed:23564174}; KM=115 uM for beta-methylmalonyl-CoA {ECO:0000269|PubMed:24992697}; KM=120 uM for propionyl-CoA {ECO:0000269|PubMed:24992697}; KM=200 uM for 2,4-dihydroxybenzoyl-EntB {ECO:0000269|PubMed:24992697}; Note=kcat is 6.2 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:23564174). kcat is 1.6 sec(-1) with 1,4-dihydroxy-2-naphthoyl-CoA (PubMed:24992697). kcat is 0.12 sec(-1) with oleoyl-CoA. kcat is 0.62 sec(-1) with myristoyl-CoA. kcat is 0.0044 sec(-1) with acetyl-CoA. kcat is 0.58 sec(-1) with palmitoyl-CoA. kcat is 0.74 sec(-1) with lauroyl-CoA. kcat is 14.8 sec(-1) with 1-hydroxy-2-naphthoyl-CoA. kcat is 5.2 sec(-1) with 4-hydroxybenzoyl-CoA. kcat is 0.3 sec(-1) with hexanoyl-CoA. kcat is 17.7 sec(-1) with benzoyl-CoA. kcat is 12.6 sec(-1) with 3,5-dihydroxybenzoyl-CoA. kcat is 23.2 sec(-1) with 3,4-dihydroxybenzoyl-CoA. kcat is 8.4 sec(-1) with coumaroyl-CoA. kcat is 0.083 sec(-1) with benzoyl-ACP. kcat is 0.5 sec(-1) with beta-methylcrotonyl-CoA. kcat is 93.0 sec(-1) with salicylyl-CoA. kcat is 0.67 sec(-1) with beta-methylmalonyl-CoA. kcat is 0.21 sec(-1) with propionyl-CoA. kcat is 0.0036 sec(-1) with 2,4-dihydroxybenzoyl-EntB. {ECO:0000269|PubMed:23564174, ECO:0000269|PubMed:24992697}; |
| Metal Binding | |
| Rhea ID | RHEA:26309 |
| Cross Reference Brenda | 3.1.2.2;3.1.2.28; |