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Entry: A0A0F7KST0_9SPHN
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ID   A0A0F7KST0_9SPHN        Unreviewed;       308 AA.
AC   A0A0F7KST0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 20.
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   Name=efe {ECO:0000313|EMBL:AKH41815.1};
GN   ORFNames=WYH_00761 {ECO:0000313|EMBL:AKH41815.1};
OS   Croceibacterium atlanticum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Croceibacterium.
OX   NCBI_TaxID=1267766 {ECO:0000313|EMBL:AKH41815.1, ECO:0000313|Proteomes:UP000034392};
RN   [1] {ECO:0000313|EMBL:AKH41815.1, ECO:0000313|Proteomes:UP000034392}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=26DY36 {ECO:0000313|EMBL:AKH41815.1,
RC   ECO:0000313|Proteomes:UP000034392};
RA   Wu Y.-H., Cheng H., Wu X.-W.;
RT   "The complete genome of Altererythrobacter atlanticus strain 26DY36.";
RL   Submitted (MAY-2015) 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|RuleBase:RU003682}.
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DR   EMBL; CP011452; AKH41815.1; -; Genomic_DNA.
DR   RefSeq; WP_046902774.1; NZ_JACIJL010000004.1.
DR   AlphaFoldDB; A0A0F7KST0; -.
DR   STRING; 1267766.WYH_00761; -.
DR   KEGG; aay:WYH_00761; -.
DR   PATRIC; fig|1267766.3.peg.769; -.
DR   OrthoDB; 21825at2; -.
DR   Proteomes; UP000034392; Chromosome.
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:SF34; IRON/ASCORBATE OXIDOREDUCTASE DDB_G0283291-RELATED; 1.
DR   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   SUPFAM; SSF51197; Clavaminate synthase-like; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   3: Inferred from homology;
KW   Ethylene biosynthesis {ECO:0000256|ARBA:ARBA00022666};
KW   Iron {ECO:0000256|RuleBase:RU003682};
KW   Metal-binding {ECO:0000256|RuleBase:RU003682};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003682,
KW   ECO:0000313|EMBL:AKH41815.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034392}.
FT   DOMAIN          161..267
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   308 AA;  34653 MW;  D1972B315B7F34C5 CRC64;
     MTEVASVSLT RPLADFSDEL GRSFTEYGFA IVRDHPIAPD LIARAWDLSR QFFALPEDVK
     RQYHLAGMGG ARGYTPFGTE RAKDAQINDL KEFWHVGRSL PPGDPLEEFM PPNVWPQEIE
     GFQQTFEELF LAFETTGRRI LSAIALHLGL EEDFFDPTVE NGNSVMRLLH YPPVPESADG
     AIRAAAHEDI NTITLLLGAE ESGLQLLSRE GKWLSVAPPE GALAVNIGDM LQRLTNGVMR
     STTHRVVNPV GEAARRSRYS MPFFLHFRPD FEIRALSQCV EEGREHEVEA PITAHDYLMQ
     RLREINLV
//
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