| IED ID | IndEnz0018000505 |
| Enzyme Type ID | peroxidase000505 |
| Protein Name |
Glutathione amide reductase GAR EC 1.8.1.16 |
| Gene Name | garB |
| Organism | Marichromatium gracile (Chromatium gracile) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Chromatiales Chromatiaceae Marichromatium Marichromatium gracile (Chromatium gracile) |
| Enzyme Sequence | MTQHFDLIAIGGGSGGLAVAEKAAAFGKRVALIESKALGGTCVNVGCVPKKVMWYASHLAEAVRDAPGFGVQASGGTLDWPRLVAGRDRYIGAINSFWDGYVERLGITRVDGHARFVDAHTIEVEGQRLSADHIVIATGGRPIVPRLPGAELGITSDGFFALQQQPKRVAIIGAGYIGIELAGLLRSFGSEVTVVALEDRLLFQFDPLLSATLAENMHAQGIETHLEFAVAALERDAQGTTLVAQDGTRLEGFDSVIWAVGRAPNTRDLGLEAAGIEVQSNGMVPTDAYQNTNVPGVYALGDITGRDQLTPVAIAAGRRLAERLFDGQSERKLDYDNIPTVVFAHPPLSKVGLSEPEARERLGDVLTVYETSFTPMRYALNEHGPKTAMKLVCAGPEQRVVGVHVIGDGADEMLQGFAVAVKMGATKADFDNTVAIHPGSAEELVTLKEPVRRPGDPLPEGAA |
| Enzyme Length | 463 |
| Uniprot Accession Number | D0VWY5 |
| Absorption | |
| Active Site | ACT_SITE 437; /note=Proton acceptor; /evidence=ECO:0000269|PubMed:17977556 |
| Activity Regulation | |
| Binding Site | BINDING 34; /note=FAD; /evidence=ECO:0000269|PubMed:17977556; BINDING 41; /note=FAD; /evidence=ECO:0000269|PubMed:17977556; BINDING 50; /note=FAD; /evidence=ECO:0000269|PubMed:17977556; BINDING 50; /note=NAD; /evidence=ECO:0000269|PubMed:17977556; BINDING 230; /note=NAD; via amide nitrogen; /evidence=ECO:0000269|PubMed:17977556; BINDING 261; /note=NAD; via amide nitrogen; /evidence=ECO:0000269|PubMed:17977556; BINDING 302; /note=FAD; /evidence=ECO:0000269|PubMed:17977556; BINDING 308; /note=NAD; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:17977556; BINDING 341; /note=NAD; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:17977556; BINDING 437; /note=FAD; via carbonyl oxygen; /evidence=ECO:0000269|PubMed:17977556 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2 glutathione amide + NAD(+) = glutathione amide disulfide + H(+) + NADH; Xref=Rhea:RHEA:27433, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:59895, ChEBI:CHEBI:59896; EC=1.8.1.16; Evidence={ECO:0000269|PubMed:11399772}; |
| DNA Binding | |
| EC Number | 1.8.1.16 |
| Enzyme Function | FUNCTION: Catalyzes the reduction of glutathione amide disulfide (GASSAG) to restore glutathione amide (GASH) in the presence of NADH. May play a role in GASH metabolism under anaerobic conditions as a sulfide carrier necessary for cytoplasmic sulfide oxidation. {ECO:0000269|PubMed:11399772}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 14..15; /note=FAD; /evidence=ECO:0000269|PubMed:17977556; NP_BIND 113..114; /note=FAD; /evidence=ECO:0000269|PubMed:17977556; NP_BIND 174..180; /note=NAD; /evidence=ECO:0000269|PubMed:17977556; NP_BIND 197..198; /note=NAD; /evidence=ECO:0000269|PubMed:17977556; NP_BIND 308..310; /note=FAD; /evidence=ECO:0000269|PubMed:17977556 |
| Features | Active site (1); Beta strand (23); Binding site (10); Chain (1); Disulfide bond (1); Helix (18); Initiator methionine (1); Metal binding (3); Nucleotide binding (5); Turn (1) |
| Keywords | 3D-structure;Direct protein sequencing;Disulfide bond;FAD;Flavoprotein;Metal-binding;NAD;Nickel;Nucleotide-binding;Oxidoreductase;Redox-active center |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (2) |
| Cross Reference PDB | 2R9Z; 2RAB; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 49,159 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=97 uM for glutathione amide disulfide (GASSAG) for the reverse reaction (in the presence of 100 uM NADH) {ECO:0000269|PubMed:11399772}; KM=6.9 mM for glutathione disulfide (GSH) for the reverse reaction {ECO:0000269|PubMed:11399772}; KM=13.2 uM for NADH for the reverse reaction (in the presence of 500 uM GASSAG) {ECO:0000269|PubMed:11399772}; KM=1.98 mM for NADPH for the reverse reaction {ECO:0000269|PubMed:11399772}; |
| Metal Binding | METAL 2; /note=Nickel; /evidence=ECO:0000269|PubMed:17977556; METAL 3; /note=Nickel; /evidence=ECO:0000269|PubMed:17977556; METAL 4; /note=Nickel; via pros nitrogen; /evidence=ECO:0000269|PubMed:17977556 |
| Rhea ID | RHEA:27433 |
| Cross Reference Brenda |