| IED ID | IndEnz0007000383 |
| Enzyme Type ID | catalase000383 |
| Protein Name |
2-oxoglutarate-dependent ethylene/succinate-forming enzyme EFE Ethylene-forming enzyme EC 1.13.12.19 EC 1.14.20.7 2-oxoglutarate dioxygenase ethylene-forming 2-oxoglutarate/L-arginine monooxygenase/decarboxylase succinate-forming |
| Gene Name | efe |
| Organism | Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola) |
| Taxonomic Lineage | cellular organisms Bacteria Proteobacteria Gammaproteobacteria Pseudomonadales Pseudomonadaceae Pseudomonas Pseudomonas syringae group Pseudomonas syringae group genomosp. 2 Pseudomonas savastanoi (Pseudomonas syringae pv. savastanoi) Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. phaseolicola) |
| Enzyme Sequence | MTNLQTFELPTEVTGCAADISLGRALIQAWQKDGIFQIKTDSEQDRKTQEAMAASKQFCKEPLTFKSSCVSDLTYSGYVASGEEVTAGKPDFPEIFTVCKDLSVGDQRVKAGWPCHGPVPWPNNTYQKSMKTFMEELGLAGERLLKLTALGFELPINTFTDLTRDGWHHMRVLRFPPQTSTLSRGIGAHTDYGLLVIAAQDDVGGLYIRPPVEGEKRNRNWLPGESSAGMFEHDEPWTFVTPTPGVWTVFPGDILQFMTGGQLLSTPHKVKLNTRERFACAYFHEPNFEASAYPLFEPSANERIHYGEHFTNMFMRCYPDRITTQRINKENRLAHLEDLKKYSDTRATGS |
| Enzyme Length | 350 |
| Uniprot Accession Number | P32021 |
| Absorption | |
| Active Site | |
| Activity Regulation | ACTIVITY REGULATION: Activated by catalase. Inhibited by chelating reagents such as EDTA and Tiron (4,5-dihydroxy-1,3-benzene disulphonic acid), and by DTNB (5,5'-dithio-bis-2-nitrobenzoate) and hydrogen peroxide. |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + 2 H(+) + O2 = 3 CO2 + ethene + H2O; Xref=Rhea:RHEA:31523, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:18153; EC=1.13.12.19; CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-arginine + O2 = (S)-1-pyrroline-5-carboxylate + CO2 + guanidine + H(+) + H2O + succinate; Xref=Rhea:RHEA:31535, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:17388, ChEBI:CHEBI:30031, ChEBI:CHEBI:30087, ChEBI:CHEBI:32682; EC=1.14.20.7; |
| DNA Binding | |
| EC Number | 1.13.12.19; 1.14.20.7 |
| Enzyme Function | FUNCTION: Simultaneously catalyzes two reactions, namely formation of ethylene and of succinate from 2-oxoglutarate, with a molar ratio of 2:1. {ECO:0000269|PubMed:1445291}. |
| Temperature Dependency | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 20-25 degrees Celsius.; |
| PH Dependency | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-7.5.; |
| Pathway | PATHWAY: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate. |
| nucleotide Binding | |
| Features | Beta strand (14); Chain (1); Domain (1); Helix (12); Metal binding (2); Sequence conflict (1); Turn (5) |
| Keywords | 3D-structure;Dioxygenase;Direct protein sequencing;Ethylene biosynthesis;Iron;Metal-binding;Oxidoreductase;Plasmid |
| Interact With | |
| Induction | |
| Subcellular Location | |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (18) |
| Cross Reference PDB | 5LSQ; 5LUN; 5MOF; 5V2T; 5V2U; 5V2V; 5V2X; 5V2Y; 5V2Z; 5V31; 5V32; 5V34; 5VKA; 5VKB; 6CBA; 6CF3; 6VP4; 6VP5; |
| Mapped Pubmed ID | 28420789; 28780854; 33522811; |
| Motif | |
| Gene Encoded By | Plasmid pPSP1 |
| Mass | 39,445 |
| Kinetics | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=59 uM for Fe(2+); KM=19 uM for 2-oxoglutarate; KM=18 uM for L-arginine; |
| Metal Binding | METAL 189; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805; METAL 268; /note=Iron; /evidence=ECO:0000255|PROSITE-ProRule:PRU00805 |
| Rhea ID | RHEA:31523; RHEA:31535 |
| Cross Reference Brenda | 1.13.12.19;1.14.20.7; |