ID A0A518N6Y1_9GAMM Unreviewed; 317 AA.
AC A0A518N6Y1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 27-MAR-2024, entry version 11.
DE RecName: Full=2-oxoglutarate-dependent ethylene/succinate-forming enzyme {ECO:0000256|ARBA:ARBA00019045};
DE EC=1.13.12.19 {ECO:0000256|ARBA:ARBA00012531};
DE EC=1.14.20.7 {ECO:0000256|ARBA:ARBA00012293};
DE AltName: Full=2-oxoglutarate dioxygenase (ethylene-forming) {ECO:0000256|ARBA:ARBA00031011};
DE AltName: Full=2-oxoglutarate/L-arginine monooxygenase/decarboxylase (succinate-forming) {ECO:0000256|ARBA:ARBA00031282};
GN ORFNames=FPZ22_12775 {ECO:0000313|EMBL:QDW67642.1};
OS Luteimonas granuli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=1176533 {ECO:0000313|EMBL:QDW67642.1, ECO:0000313|Proteomes:UP000316584};
RN [1] {ECO:0000313|EMBL:QDW67642.1, ECO:0000313|Proteomes:UP000316584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gr-4 {ECO:0000313|EMBL:QDW67642.1,
RC ECO:0000313|Proteomes:UP000316584};
RA Im W.-T.;
RT "Full genome sequence of Luteimonas sp. Gr-4.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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 Evidence={ECO:0000256|ARBA:ARBA00000134};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxoglutarate + L-arginine + O2 = CO2 + guanidine + L-
CC glutamate 5-semialdehyde + succinate; Xref=Rhea:RHEA:31535,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:30031, ChEBI:CHEBI:30087, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:58066; EC=1.14.20.7;
CC Evidence={ECO:0000256|ARBA:ARBA00036123};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000256|ARBA:ARBA00001954};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate.
CC {ECO:0000256|ARBA:ARBA00004767}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
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DR EMBL; CP042218; QDW67642.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A518N6Y1; -.
DR KEGG; lug:FPZ22_12775; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000316584; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 PANTHER; PTHR47990; 2-OXOGLUTARATE (2OG) AND FE(II)-DEPENDENT OXYGENASE SUPERFAMILY PROTEIN-RELATED; 1.
DR PANTHER; PTHR47990:SF62; IRON_ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR PRINTS; PR00682; IPNSYNTHASE.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR PROSITE; PS51471; FE2OG_OXY; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000316584}.
FT DOMAIN 170..276
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 317 AA; 35308 MW; 2F85766F270D8EB3 CRC64;
MAPRIPTLDI RRFTHPAGPA ERQAFVDELG AAYREWGFAG IRNHGIPQTL IDEAYAAFKA
FFALPEETKK KYHVPGGGGA RGYTPFGIET AKDSKHFDLK EFWHVGREIP DDSGYRDVMP
PNLWPDEVPE FRAKGYALYQ ALDHLGSQVL RALALHIGLP EDYFADKTDS GNSILRPIHY
PPITADDIPN VRAGAHGDIN LITLLVGASA AGLEVLSHDG EWVPFTSDED TIVVNIGDML
QRLTNHVYPS TIHRVVNPPG ELARQPRYSV PFFLHPNPDF LIDVLPSCVT ADNPSRYPEP
ITAQAYLEER LREIKLA
//
