ID EFE_PSESH Reviewed; 350 AA. AC P32021; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 113. DE RecName: Full=2-oxoglutarate-dependent ethylene/succinate-forming enzyme; DE Short=EFE; DE Short=Ethylene-forming enzyme; DE EC=1.13.12.19; DE EC=1.14.20.7; DE AltName: Full=2-oxoglutarate dioxygenase (ethylene-forming); DE AltName: Full=2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming); GN Name=efe; OS Pseudomonas savastanoi pv. phaseolicola (Pseudomonas syringae pv. OS phaseolicola). OG Plasmid pPSP1. OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=319; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=PK2; RX PubMed=1445325; DOI=10.1016/0006-291x(92)91131-9; RA Fukuda H., Ogawa T., Ishihara K., Fujii T., Nagahama K., Omata T., RA Inoue Y., Tanase S., Morino Y.; RT "Molecular cloning in Escherichia coli, expression, and nucleotide sequence RT of the gene for the ethylene-forming enzyme of Pseudomonas syringae pv. RT phaseolicola PK2."; RL Biochem. Biophys. Res. Commun. 188:826-832(1992). RN [2] RP PROTEIN SEQUENCE OF 1-30, AND CHARACTERIZATION. RC STRAIN=PK2; RX PubMed=1770346; DOI=10.1099/00221287-137-10-2281; RA Nagahama K., Ogawa T., Fujii T., Tazaki M., Tanase S., Morino Y., RA Fukuda H.; RT "Purification and properties of an ethylene-forming enzyme from Pseudomonas RT syringae pv. phaseolicola PK2."; RL J. Gen. Microbiol. 137:2281-2286(1991). RN [3] RP FUNCTION, AND MECHANISM. RC STRAIN=PK2; RX PubMed=1445291; DOI=10.1016/0006-291x(92)91081-z; RA Fukuda H., Ogawa T., Tazaki M., Nagahama K., Fujii T., Tanase S., RA Morino Y.; RT "Two reactions are simultaneously catalyzed by a single enzyme: the RT arginine-dependent simultaneous formation of two products, ethylene and RT succinate, from 2-oxoglutarate by an enzyme from Pseudomonas syringae."; RL Biochem. Biophys. Res. Commun. 188:483-489(1992). CC -!- FUNCTION: Simultaneously catalyzes two reactions, namely formation of CC ethylene and of succinate from 2-oxoglutarate, with a molar ratio of CC 2:1. {ECO:0000269|PubMed:1445291}. CC -!- CATALYTIC ACTIVITY: CC Reaction=2-oxoglutarate + O2 + 2 H(+) = ethene + 3 CO2 + H2O; CC Xref=Rhea:RHEA:31523, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:18153; EC=1.13.12.19; CC -!- CATALYTIC ACTIVITY: CC Reaction=L-arginine + 2-oxoglutarate + O2 = guanidine + L-glutamate 5- CC semialdehyde + succinate + CO2; Xref=Rhea:RHEA:31535, CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, CC ChEBI:CHEBI:30031, ChEBI:CHEBI:30087, ChEBI:CHEBI:32682, CC ChEBI:CHEBI:58066; EC=1.14.20.7; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC -!- ACTIVITY REGULATION: Activated by catalase. Inhibited by chelating CC reagents such as EDTA and Tiron (4,5-dihydroxy-1,3-benzene disulphonic CC acid), and by DTNB (5,5'-dithio-bis-2-nitrobenzoate) and hydrogen CC peroxide. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=59 uM for Fe(2+); CC KM=19 uM for 2-oxoglutarate; CC KM=18 uM for L-arginine; CC pH dependence: CC Optimum pH is 7.0-7.5.; CC Temperature dependence: CC Optimum temperature is 20-25 degrees Celsius.; CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate. CC -!- SUBUNIT: Monomer. CC -!- MISCELLANEOUS: A dual-circuit mechanism has been proposed in CC PubMed:1445291 for the complete reaction, in which the binding of L- CC arginine and 2-oxoglutarate in a Schiff-base structure generates a CC common intermediate for the two reactions. CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D13182; BAA02477.1; -; Genomic_DNA. DR PIR; JQ1656; JQ1656. DR RefSeq; WP_054082735.1; NZ_LGKV01000002.1. DR PDB; 5LSQ; X-ray; 1.55 A; A=3-350. DR PDB; 5LUN; X-ray; 1.08 A; A/B/C/D=2-350. DR PDB; 5MOF; X-ray; 1.45 A; A=3-350. DR PDB; 5V2T; X-ray; 1.23 A; A=1-350. DR PDB; 5V2U; X-ray; 2.06 A; A=1-350. DR PDB; 5V2V; X-ray; 3.04 A; A=1-350. DR PDB; 5V2X; X-ray; 1.85 A; A/B=1-350. DR PDB; 5V2Y; X-ray; 1.43 A; A=1-350. DR PDB; 5V2Z; X-ray; 1.23 A; A=1-350. DR PDB; 5V31; X-ray; 2.45 A; A=1-350. DR PDB; 5V32; X-ray; 1.49 A; A=1-350. DR PDB; 5V34; X-ray; 1.48 A; A=1-350. DR PDB; 5VKA; X-ray; 1.17 A; A=1-350. DR PDB; 5VKB; X-ray; 1.14 A; A=1-350. DR PDB; 6CBA; X-ray; 1.13 A; A=1-350. DR PDB; 6CF3; X-ray; 1.12 A; A=1-350. DR PDB; 6VP4; X-ray; 1.83 A; A/B/C/D=1-350. DR PDB; 6VP5; X-ray; 1.97 A; A/B/C/D=1-350. DR PDB; 8UC2; X-ray; 1.60 A; A=1-350. DR AlphaFoldDB; P32021; -. DR SMR; P32021; -. DR KEGG; ag:BAA02477; -. DR BioCyc; MetaCyc:MONOMER-16773; -. DR BRENDA; 1.13.12.19; 5194. DR BRENDA; 1.14.20.7; 5194. DR SABIO-RK; P32021; -. DR UniPathway; UPA00385; -. DR GO; GO:0102276; F:2-oxoglutarate oxygenase/decarboxylase (ethylene-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.60.120.330; B-lactam Antibiotic, Isopenicillin N Synthase, Chain; 1. DR InterPro; IPR026992; DIOX_N. DR InterPro; IPR044861; IPNS-like_FE2OG_OXY. DR InterPro; IPR027443; IPNS-like_sf. DR InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase_dom. DR PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1. DR Pfam; PF03171; 2OG-FeII_Oxy; 1. DR Pfam; PF14226; DIOX_N; 1. DR SUPFAM; SSF51197; Clavaminate synthase-like; 1. DR PROSITE; PS51471; FE2OG_OXY; 1. DR PDBsum; 5LSQ; -. DR PDBsum; 5LUN; -. DR PDBsum; 5MOF; -. DR PDBsum; 5V2T; -. DR PDBsum; 5V2U; -. DR PDBsum; 5V2V; -. DR PDBsum; 5V2X; -. DR PDBsum; 5V2Y; -. DR PDBsum; 5V2Z; -. DR PDBsum; 5V31; -. DR PDBsum; 5V32; -. DR PDBsum; 5V34; -. DR PDBsum; 5VKA; -. DR PDBsum; 5VKB; -. DR PDBsum; 6CBA; -. DR PDBsum; 6CF3; -. DR PDBsum; 6VP4; -. DR PDBsum; 6VP5; -. DR PDBsum; 8UC2; -. PE 1: Evidence at protein level; KW 3D-structure; Dioxygenase; Direct protein sequencing; KW Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase; Plasmid. FT CHAIN 1..350 FT /note="2-oxoglutarate-dependent ethylene/succinate-forming FT enzyme" FT /id="PRO_0000067277" FT DOMAIN 166..286 FT /note="Fe2OG dioxygenase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 189 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT BINDING 268 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805" FT CONFLICT 30 FT /note="W -> K (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT HELIX 3..5 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 8..10 FT /evidence="ECO:0007829|PDB:6CF3" FT HELIX 17..33 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 36..39 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 42..59 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 63..67 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 77..79 FT /evidence="ECO:0007829|PDB:5LUN" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 84..86 FT /evidence="ECO:0007829|PDB:5VKB" FT STRAND 94..98 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 107..110 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 124..151 FT /evidence="ECO:0007829|PDB:5LUN" FT TURN 156..159 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 160..162 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 169..175 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 176..178 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 184..189 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 193..200 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 206..208 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 209..211 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 216..218 FT /evidence="ECO:0007829|PDB:5V2U" FT HELIX 223..225 FT /evidence="ECO:0007829|PDB:5LUN" FT TURN 228..233 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 238..240 FT /evidence="ECO:0007829|PDB:5V2V" FT STRAND 246..251 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 253..258 FT /evidence="ECO:0007829|PDB:5LUN" FT TURN 259..261 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 265..267 FT /evidence="ECO:0007829|PDB:6CF3" FT STRAND 268..271 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 277..284 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 295..297 FT /evidence="ECO:0007829|PDB:6VP4" FT HELIX 306..317 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 322..329 FT /evidence="ECO:0007829|PDB:5LUN" FT TURN 330..333 FT /evidence="ECO:0007829|PDB:5LUN" FT HELIX 334..339 FT /evidence="ECO:0007829|PDB:5LUN" FT STRAND 341..343 FT /evidence="ECO:0007829|PDB:5V2T" SQ SEQUENCE 350 AA; 39445 MW; 5FD86F07EFCD392B CRC64; MTNLQTFELP TEVTGCAADI SLGRALIQAW QKDGIFQIKT DSEQDRKTQE AMAASKQFCK EPLTFKSSCV SDLTYSGYVA SGEEVTAGKP DFPEIFTVCK DLSVGDQRVK AGWPCHGPVP WPNNTYQKSM KTFMEELGLA GERLLKLTAL GFELPINTFT DLTRDGWHHM RVLRFPPQTS TLSRGIGAHT DYGLLVIAAQ DDVGGLYIRP PVEGEKRNRN WLPGESSAGM FEHDEPWTFV TPTPGVWTVF PGDILQFMTG GQLLSTPHKV KLNTRERFAC AYFHEPNFEA SAYPLFEPSA NERIHYGEHF TNMFMRCYPD RITTQRINKE NRLAHLEDLK KYSDTRATGS //