| IED ID | IndEnz0010001036 |
| Enzyme Type ID | esterase001036 |
| Protein Name |
Glutamyl-tRNA reductase GluTR EC 1.2.1.70 |
| Gene Name | hemA b1210 JW1201 |
| Organism | Escherichia coli (strain K12) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Enterobacterales Enterobacteriaceae Escherichia Escherichia coli Escherichia coli (strain K12) |
| Enzyme Sequence | MTLLALGINHKTAPVSLRERVSFSPDKLDQALDSLLAQPMVQGGVVLSTCNRTELYLSVEEQDNLQEALIRWLCDYHNLNEEDLRKSLYWHQDNDAVSHLMRVASGLDSLVLGEPQILGQVKKAFADSQKGHMKASELERMFQKSFSVAKRVRTETDIGASAVSVAFAACTLARQIFESLSTVTVLLVGAGETIELVARHLREHKVQKMIIANRTRERAQILADEVGAEVIALSDIDERLREADIIISSTASPLPIIGKGMVERALKSRRNQPMLLVDIAVPRDVEPEVGKLANAYLYSVDDLQSIISHNLAQRKAAAVEAETIVAQETSEFMAWLRAQSASETIREYRSQAEQVRDELTAKALAALEQGGDAQAIMQDLAWKLTNRLIHAPTKSLQQAARDGDNERLNILRDSLGLE |
| Enzyme Length | 418 |
| Uniprot Accession Number | P0A6X1 |
| Absorption | |
| Active Site | ACT_SITE 50; /note=Nucleophile |
| Activity Regulation | ACTIVITY REGULATION: Activated by Mg(2+) ions. Inhibited by metal-chelating agents such as EDTA, EGTA, 1,10-phenanthroline, 2,2'-dipyridyl, and by PtCl4 and KPdCl4 as well as Ni(2+) and Co(2+). Also inhibited by iodoacetamide, N-tosyl-L-phenylalanine chloromethyl ketone, and 5,5'-dithiobis(2-nitrobenzoic acid), as well as glutamycin. {ECO:0000269|PubMed:12370189}. |
| Binding Site | BINDING 109; /note=Substrate; /evidence=ECO:0000305; BINDING 120; /note=Substrate; /evidence=ECO:0000250 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=(S)-4-amino-5-oxopentanoate + NADP(+) + tRNA(Glu) = H(+) + L-glutamyl-tRNA(Glu) + NADPH; Xref=Rhea:RHEA:12344, Rhea:RHEA-COMP:9663, Rhea:RHEA-COMP:9680, ChEBI:CHEBI:15378, ChEBI:CHEBI:57501, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:78442, ChEBI:CHEBI:78520; EC=1.2.1.70; Evidence={ECO:0000269|PubMed:12370189}; |
| DNA Binding | |
| EC Number | 1.2.1.70 |
| Enzyme Function | FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA). In the absence of NADPH, exhibits substrate esterase activity, leading to the release of glutamate from tRNA. {ECO:0000269|PubMed:12370189, ECO:0000269|PubMed:1569081}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. |
| nucleotide Binding | NP_BIND 189..194; /note=NADP; /evidence=ECO:0000305 |
| Features | Active site (1); Binding site (2); Chain (1); Mutagenesis (16); Nucleotide binding (1); Region (2); Sequence conflict (6); Site (1) |
| Keywords | Direct protein sequencing;NADP;Oxidoreductase;Porphyrin biosynthesis;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | 16606699; 24627523; |
| Motif | |
| Gene Encoded By | |
| Mass | 46,307 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24 uM for L-glutamyl-tRNA(Glu) {ECO:0000269|PubMed:12370189}; KM=39 uM for NADPH {ECO:0000269|PubMed:12370189}; |
| Metal Binding | |
| Rhea ID | RHEA:12344 |
| Cross Reference Brenda | 1.2.1.70; |