EFE_PSECA
ID EFE_PSECA Reviewed; 350 AA.
AC Q7BS31;
DT 30-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 54.
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 cannabina.
OG Plasmid.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=86840;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GSPB 2553;
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.
CC {ECO:0000305|PubMed:18944747}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF101059; AAD16441.1; -; Genomic_DNA.
DR RefSeq; WP_004661945.1; NZ_VXJZ01000173.1.
DR AlphaFoldDB; Q7BS31; -.
DR SMR; Q7BS31; -.
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..350
FT /note="2-oxoglutarate-dependent ethylene/succinate-forming
FT enzyme"
FT /id="PRO_0000067275"
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 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