| IED ID | IndEnz0010001487 |
| Enzyme Type ID | esterase001487 |
| Protein Name |
Glutamyl-tRNA reductase GluTR EC 1.2.1.70 |
| Gene Name | hemA MK0200 |
| Organism | Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Methanopyri Methanopyrales Methanopyraceae Methanopyrus Methanopyrus kandleri Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) |
| Enzyme Sequence | MEDLVCVGITHKEAEVEELEKARFESDEAVRDIVESFGLSGCVLLQTCNRVEVYASGARDRAEELGDLIHDDAWVKRGSEAVRHLFRVACGLESMMVGEQEILRQVKKAYDRAARLGTLDEALKIVFRRAINLGKRAREETRISEGAVSIGSAAVELAERELGSLHDKTVLVVGAGEMGKTVAKSLVDRGVRAVLVANRTYERAVELARDLGGEAVRFDELVDHLARSDVVVSATAAPHPVIHVDDVREALRKRDRRSPILIIDIANPRDVEEGVENIEDVEVRTIDDLRVIARENLERRRKEIPKVEKLIEEELSTVEEELEKLKERRLVADVAKSLHEIKDRELERALRRLKTGDPENVLQDFAEAYTKRLINVLTSAIMELPDEYRRAACRALRRASELNG |
| Enzyme Length | 404 |
| Uniprot Accession Number | Q9UXR8 |
| Absorption | |
| Active Site | ACT_SITE 48; /note=Nucleophile |
| Activity Regulation | ACTIVITY REGULATION: Inhibited by heavy metal compounds, Zn(2+), and heme. Also competitively inhibited by glutamycin. |
| Binding Site | BINDING 94; /note=Substrate; BINDING 105; /note=Substrate |
| 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; |
| 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:10521455}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 90 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1.; |
| Pathway | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2. |
| nucleotide Binding | NP_BIND 174..179; /note=NADP; /evidence=ECO:0000305 |
| Features | Active site (1); Beta strand (11); Binding site (2); Chain (1); Helix (17); Mutagenesis (3); Nucleotide binding (1); Region (2); Site (1); Turn (3) |
| Keywords | 3D-structure;Direct protein sequencing;NADP;Oxidoreductase;Porphyrin biosynthesis;Reference proteome |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 1GPJ; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,444 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:12344 |
| Cross Reference Brenda | 1.2.1.70; |