ID   EFE_RALSO               Reviewed;         345 AA.
AC   Q8XPV7;
DT   30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 100.
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; OrderedLocusNames=RSp1529; ORFNames=RS04806;
OS   Ralstonia solanacearum (strain GMI1000) (Pseudomonas solanacearum).
OG   Plasmid megaplasmid Rsp.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AL646053; CAD18680.1; -; Genomic_DNA.
DR   RefSeq; WP_011004776.1; NC_003296.1.
DR   AlphaFoldDB; Q8XPV7; -.
DR   SMR; Q8XPV7; -.
DR   STRING; 267608.RSp1529; -.
DR   EnsemblBacteria; CAD18680; CAD18680; RSp1529.
DR   GeneID; 60504429; -.
DR   KEGG; rso:RSp1529; -.
DR   PATRIC; fig|267608.8.peg.5009; -.
DR   eggNOG; COG3491; Bacteria.
DR   HOGENOM; CLU_045863_0_0_4; -.
DR   OMA; YRISVPF; -.
DR   BRENDA; 1.13.12.19; 5176.
DR   UniPathway; UPA00385; -.
DR   Proteomes; UP000001436; Plasmid megaplasmid Rsp.
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; Reference proteome.
FT   CHAIN           1..345
FT                   /note="2-oxoglutarate-dependent ethylene/succinate-forming
FT                   enzyme"
FT                   /id="PRO_0000067280"
FT   DOMAIN          167..288
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         191
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         270
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   345 AA;  39206 MW;  EB011E7709A041AD CRC64;
     MTDLTTFHLP ERITNTEAHR ELGQAMVKAW RTDGIFQITL SKPQEQTTDE AFAESRQFFS
     QDFETKSRHV SALTYSGYIA SREEVTAGEA DYSEIFTICP DIGLEDARVR ENLPCHGPVP
     WPGAAYRDRM KAFMGMLGTF GERLLQLIAL GLDLDDMDTF TRLTQDGWHH MRVLRFPTVQ
     SSENARGIGA HTDYGMLVIA AQDDVGGLYV RPPIEGERRN RNWLPSESTA GVYEHDDGWN
     FIKPMPAVLT VFPGDFLQFL TGGHLLSTPH KVRLNTRERF AMAYFHEPNF DAWVEPLEAD
     AAVAPIHYGT HFTNMFMRCY PKRITTRRIM ENGLLDKLPT LSELA