| IED ID | IndEnz0002005234 |
| Enzyme Type ID | protease005234 |
| Protein Name |
Glucose-6-phosphate 1-dehydrogenase G6PD EC 1.1.1.49 Cleaved into: Extracellular death factor EDF |
| Gene Name | zwf b1852 JW1841 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MAVTQTAQACDLVIFGAKGDLARRKLLPSLYQLEKAGQLNPDTRIIGVGRADWDKAAYTKVVREALETFMKETIDEGLWDTLSARLDFCNLDVNDTAAFSRLGAMLDQKNRITINYFAMPPSTFGAICKGLGEAKLNAKPARVVMEKPLGTSLATSQEINDQVGEYFEECQVYRIDHYLGKETVLNLLALRFANSLFVNNWDNRTIDHVEITVAEEVGIEGRWGYFDKAGQMRDMIQNHLLQILCMIAMSPPSDLSADSIRDEKVKVLKSLRRIDRSNVREKTVRGQYTAGFAQGKKVPGYLEEEGANKSSNTETFVAIRVDIDNWRWAGVPFYLRTGKRLPTKCSEVVVYFKTPELNLFKESWQDLPQNKLTIRLQPDEGVDIQVLNKVPGLDHKHNLQITKLDLSYSETFNQTHLADAYERLLLETMRGIQALFVRRDEVEEAWKWVDSITEAWAMDNDAPKPYQAGTWGPVASVAMITRDGRSWNEFE |
| Enzyme Length | 491 |
| Uniprot Accession Number | P0AC53 |
| Absorption | |
| Active Site | ACT_SITE 239; /note=Proton acceptor; /evidence=ECO:0000255|HAMAP-Rule:MF_00966 |
| Activity Regulation | |
| Binding Site | BINDING 50; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 147; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 177; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 181; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 215; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 234; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 339; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00966; BINDING 344; /note=Substrate; /evidence=ECO:0000255|HAMAP-Rule:MF_00966 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000255|HAMAP-Rule:MF_00966}; |
| DNA Binding | |
| EC Number | 1.1.1.49 |
| Enzyme Function | FUNCTION: Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone. {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:15113569, ECO:0000269|PubMed:17962566}.; FUNCTION: Probable source of extracellular death factor (EDF, sequence Asn-Asn-Trp-Asn-Asn, NNWNN) following processing and amidation. This pentapeptide stimulates cell death mediated by MazF (PubMed:17962566). Artificial peptides with altered sequence show that NNGNN, GNWNG and NWN no longer stimulate MazF's endoribonuclease activity; other peptides (NNGN, GNWMM, NNWNG, NNNWNNN) retain MazF-stimulating activity. NNWNN, NNGN, GNWMM and NNWNG prevent cognate antitoxin MazE from inhibiting MazF; although NNNWNNN stimulates MazF it does not do so in the presence of MazE. EDF also stimulates ChpB's endoribonuclease activity in vitro; in this case NWN partially stimulates ChpB, whereas NNGNN, GNWNN, NNWNG, GNWNG and NNNWNNN do not. Only the wild-type EDF peptide prevents cognate antitoxin ChpS from inhibiting ChpB (PubMed:21419338). {ECO:0000269|PubMed:17962566, ECO:0000269|PubMed:21419338}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000255|HAMAP-Rule:MF_00966, ECO:0000269|PubMed:15113569}. |
| nucleotide Binding | NP_BIND 92..93; /note=NADP; /evidence=ECO:0000255|HAMAP-Rule:MF_00966 |
| Features | Active site (1); Binding site (8); Chain (2); Natural variant (1); Nucleotide binding (1); Sequence conflict (1) |
| Keywords | Carbohydrate metabolism;Glucose metabolism;NADP;Oxidoreductase;Quorum sensing;Reference proteome |
| Interact With | P0A988; Itself |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | PTM: Probably processed by the ClpPX protease to generate the extracellular death factor (EDF). It is thought that processing produces Asn-Asn-Trp-Asp-Asn which is amidated to generate Asn-Asn-Trp-Asn-Asn (Probable). {ECO:0000305|PubMed:17962566}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 15690043; 16606699; 16858726; 19698713; |
| Motif | |
| Gene Encoded By | |
| Mass | 55,704 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:15841 |
| Cross Reference Brenda |