EFE_PSESH
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 03-AUG-2022, entry version 99.
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; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC 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 + 2 H(+) + O2 = 3 CO2 + ethene + 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=2-oxoglutarate + L-arginine + O2 = (S)-1-pyrroline-5-
CC carboxylate + CO2 + guanidine + H(+) + H2O + succinate;
CC Xref=Rhea:RHEA:31535, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:17388, ChEBI:CHEBI:30031, ChEBI:CHEBI:30087,
CC ChEBI:CHEBI:32682; 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}.
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DR EMBL; D13182; BAA02477.1; -; Genomic_DNA.
DR PIR; JQ1656; JQ1656.
DR RefSeq; WP_054082735.1; NZ_RBUR01000014.1.
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 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 AlphaFoldDB; P32021; -.
DR SMR; P32021; -.
DR KEGG; ag:BAA02477; -.
DR BioCyc; MetaCyc:MON-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:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.60.120.330; -; 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.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
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 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 178..180
FT /evidence="ECO:0007829|PDB:6CF3"
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 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 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
