ID   EFE_PSESG               Reviewed;         350 AA.
AC   Q7BS32;
DT   30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 64.
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. glycinea (Pseudomonas syringae pv. glycinea).
OG   Plasmid.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=318;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=7a/90;
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).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-30.
RC   STRAIN=KN130;
RX   PubMed=7952184; DOI=10.1099/13500872-140-9-2309;
RA   Nagahama K., Yoshino K., Matsuoka M., Sato M., Tanase S., Ogawa T.,
RA   Fukuda H.;
RT   "Ethylene production by strains of the plant-pathogenic bacterium
RT   Pseudomonas syringae depends upon the presence of indigenous plasmids
RT   carrying homologous genes for the ethylene-forming enzyme.";
RL   Microbiology 140:2309-2313(1994).
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.
CC       {ECO:0000305|PubMed:18944747, ECO:0000305|PubMed:7952184}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AF101057; AAD16439.1; -; Genomic_DNA.
DR   RefSeq; WP_004661945.1; NZ_RBVH01000146.1.
DR   AlphaFoldDB; Q7BS32; -.
DR   SMR; Q7BS32; -.
DR   BRENDA; 1.13.12.19; 14461.
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   Dioxygenase; Direct protein sequencing; Ethylene biosynthesis; Iron;
KW   Metal-binding; Oxidoreductase; Plasmid.
FT   CHAIN           1..350
FT                   /note="2-oxoglutarate-dependent ethylene/succinate-forming
FT                   enzyme"
FT                   /id="PRO_0000067276"
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"
SQ   SEQUENCE   350 AA;  39376 MW;  5EC87E07EFCD392B 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 RITTQSINKE NRLAHLEDLK KYSDTRATGS