IED ID | IndEnz0010000687 |
Enzyme Type ID | esterase000687 |
Protein Name |
Glutathione-dependent formaldehyde-activating enzyme EC 4.4.1.22 S- hydroxymethyl glutathione synthase |
Gene Name | gfa |
Organism | Paracoccus denitrificans |
Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Alphaproteobacteria Rhodobacterales Rhodobacteraceae Paracoccus Paracoccus denitrificans |
Enzyme Sequence | MVDTSGVKIHPAVDNGIKPAQPGFAGGTLHCKCSTNPVRVAVRAQTAHNHVCGCTKCWKPEGAIFSQVAVVGRDALEVLEGAEKLEIVNAEAPIQRHRCRDCGVHMYGRIENRDHPFYGLDFVHTELSDEDGWSAPEFAAFVSSIIESGVDPSRMEAIRARLRELGLEPYDALSPPLMDAIATHIAKRSGALAA |
Enzyme Length | 194 |
Uniprot Accession Number | Q51669 |
Absorption | |
Active Site | |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=S-(hydroxymethyl)glutathione = formaldehyde + glutathione; Xref=Rhea:RHEA:22488, ChEBI:CHEBI:16842, ChEBI:CHEBI:57925, ChEBI:CHEBI:58758; EC=4.4.1.22; |
DNA Binding | |
EC Number | 4.4.1.22 |
Enzyme Function | FUNCTION: Catalyzes the condensation of formaldehyde and glutathione to S-hydroxymethylglutathione. {ECO:0000269|PubMed:11741920}. |
Temperature Dependency | |
PH Dependency | |
Pathway | PATHWAY: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (glutathione route): step 1/3. |
nucleotide Binding | |
Features | Beta strand (14); Chain (1); Domain (1); Helix (8); Initiator methionine (1); Metal binding (7); Turn (2) |
Keywords | 3D-structure;Direct protein sequencing;Lyase;Metal-binding;Zinc |
Interact With | |
Induction | |
Subcellular Location | |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | |
Structure 3D | X-ray crystallography (2) |
Cross Reference PDB | 1X6M; 1XA8; |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 20,967 |
Kinetics | |
Metal Binding | METAL 31; /note=Zinc 1; structural; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239; METAL 33; /note=Zinc 1; structural; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239; METAL 52; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239; METAL 54; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239; METAL 57; /note=Zinc 2; catalytic; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239; METAL 99; /note=Zinc 1; structural; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239; METAL 102; /note=Zinc 1; structural; /evidence=ECO:0000255|PROSITE-ProRule:PRU01239 |
Rhea ID | RHEA:22488 |
Cross Reference Brenda | 4.4.1.22; |