ID A0A172YT84_9GAMM Unreviewed; 336 AA.
AC A0A172YT84;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=A3K93_14045 {ECO:0000313|EMBL:ANF83350.1};
OS Acinetobacter sp. NCu2D-2.
OG Plasmid unnamed {ECO:0000313|EMBL:ANF83350.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1608473 {ECO:0000313|EMBL:ANF83350.1, ECO:0000313|Proteomes:UP000186584};
RN [1] {ECO:0000313|Proteomes:UP000186584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCu2D-2 {ECO:0000313|Proteomes:UP000186584};
RC PLASMID=Plasmid {ECO:0000313|Proteomes:UP000186584};
RA Wilharm G.;
RT "Acinetobacter strain NCu2D-2 is the representative of a novel species.";
RL Submitted (MAY-2016) 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; CP015595; ANF83350.1; -; Genomic_DNA.
DR RefSeq; WP_067731950.1; NZ_CP015595.1.
DR AlphaFoldDB; A0A172YT84; -.
DR KEGG; aciu:A3K93_14045; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000186584; Plasmid.
DR GO; GO:0102276; F:2-oxoglutarate oxygenase/decarboxylase (ethylene-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; 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 Plasmid {ECO:0000313|EMBL:ANF83350.1}.
FT DOMAIN 170..268
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 336 AA; 38280 MW; A9ABE90E87AE3386 CRC64;
MTDQYVLPLV DISKLQSPLL TDRLEVAAAL DRACQEVGFL YLTGSQFNFE YAKKLIDITK
AYFNQNLSDK MKHYIGLSQN HSGYVPIGEE QFASQSYDLK EAYDVNYDYQ GAISDYPLLG
RTQWPDFPEF KTVVSQYYEH LRQISRDIFS TFALALNVKE DYFADKITHA PSQLRLIHYP
FNPEIQDAEG IGAHTDYECF TLLLPTAPGL QVLNKKGQWI DIPLIENTLV MNIGDMMEIL
SNGKYLATKH RVKKVAEERY SFPLFCACNY DTVIEPIVKD ETPQYAALIG GEHLFNQTAQ
TFQYLKKRIA SGELVLKNAV PLSSFGLSEK SEETVQ
//
