IED ID | IndEnz0010001485 |
Enzyme Type ID | esterase001485 |
Protein Name |
Gluconolactonase EC 3.1.1.17 D-glucono-delta-lactone lactonohydrolase Cleaved into: Gluconolactonase; Gluconolactonase minor isoform |
Gene Name | gnl ZMO1649 |
Organism | Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Sphingomonadales Zymomonadaceae Zymomonas Zymomonas mobilis Zymomonas mobilis subsp. mobilis Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4) |
Enzyme Sequence | MTTGRMSRRECLSAAVMVPIAAMTATATITGSAQAAKNNMNGSTIGKITKFSPRLDAILDVSTPIEVIASDIQWSEGPVWVKNGNFLLFSDPPANIMRKWTPDAGVSIFLKPSGHAEPIPAGQFREPGSNGMKVGPDGKIWVADSGTRAIMKVDPVTRQRSVVVDNYKGKRFNSPNDLFFSKSGAVYFTDPPYGLTNLDESDIKEMNYNGVFRLSPDGRLDLIEAGLSRPNGLALSPDETKLYVSNSDRASPNIWVYSLDSNGLPTSRTLLRNFRKEYFDQGLAGLPDGMNIDKQGNLFASAPGGIYIFAPDGECLGLISGNPGQPLSNCCFGEKGQTLFISASHNVVRVRTKTFG |
Enzyme Length | 356 |
Uniprot Accession Number | Q01578 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-glucono-1,5-lactone + H2O = D-gluconate + H(+); Xref=Rhea:RHEA:10440, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:18391; EC=3.1.1.17; Evidence={ECO:0000305|PubMed:1482681}; |
DNA Binding | |
EC Number | 3.1.1.17 |
Enzyme Function | FUNCTION: Hydrolyzes the gluconolactone formed by glucose-fructose oxidoreductase, and that formed in aerobic conditions by the glucose dehydrogenase present. {ECO:0000305|PubMed:1482681}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: Carbohydrate acid metabolism; D-gluconate biosynthesis; D-gluconate from D-glucono-1,5-lactone: step 1/1. |
nucleotide Binding | |
Features | Chain (2); Sequence conflict (3); Signal peptide (1) |
Keywords | Direct protein sequencing;Hydrolase;Periplasm;Reference proteome;Serine esterase;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:1482681}. |
Modified Residue | |
Post Translational Modification | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. {ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:1482681}. |
Signal Peptide | SIGNAL 1..35; /note="Tat-type signal"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00648, ECO:0000269|PubMed:1482681" |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 38,453 |
Kinetics | |
Metal Binding | |
Rhea ID | RHEA:10440 |
Cross Reference Brenda | 3.1.1.17; |