ID   EFE_PSESJ               Reviewed;         337 AA.
AC   Q9Z3T0;
DT   30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 60.
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 syringae pv. pisi.
OG   Plasmid.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=59510;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=GSPB 1206;
RX   PubMed=18944747; AGRICOLA=IND22019584; DOI=10.1094/PHYTO.1999.89.5.360;
RA   Weingart H., Voelksch B., Ullrich M.S.;
RT   "Comparison of ethylene production by Pseudomonas syringae and Ralstonia
RT   solanacearum.";
RL   Phytopathology 89:360-365(1999).
CC   -!- FUNCTION: Simultaneously catalyzes two reactions, namely formation of
CC       ethylene and of succinate from 2-oxoglutarate. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- MISCELLANEOUS: A dual-circuit mechanism has been proposed in P.syringae
CC       pv phaseolicola 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   -!- MISCELLANEOUS: Encoded on an unnamed plasmid. {ECO:0000305,
CC       ECO:0000305|PubMed:18944747}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AF101061; AAD16443.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9Z3T0; -.
DR   SMR; Q9Z3T0; -.
DR   BRENDA; 1.13.12.19; 15409.
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   3: Inferred from homology;
KW   Dioxygenase; Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..337
FT                   /note="2-oxoglutarate-dependent ethylene/succinate-forming
FT                   enzyme"
FT                   /id="PRO_0000067278"
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"
SQ   SEQUENCE   337 AA;  38064 MW;  CCBA02DED1C3D6EC CRC64;
     MTNLQTFELP TEVIGSAADI SLGRALIQAW QKDGILQIKT DSEQNRKTQE AMAASKQFCK
     EPLTFKSSCV SDLTYSGYVA SGEEVTAGKP DFPEIFTVCK DLPVSDQRVK AGWPCHGPVP
     WPNNTYQKSM KAFMGELGLA GERLLKLTAL GFELPINTFT DLTRNGWHHM RVLRFPPQTS
     TMSSGIGAHT DYGLLVIAAQ DDVGGLYIRP PVEGEKRNRN WLPGESSAGM FEHDDPWTYV
     TPVQNVWTVF PGDILQFMTC GQLLSTPHKV RLNTRERFAC AYFHEPNFEA CAYQVFEPSG
     NERIHYGEHF TSMFMRCYPD RITTKRIHKD NRLAHFK