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Database: UniProt
Entry: A0A0D0NR73_KITGR
LinkDB: A0A0D0NR73_KITGR
Original site: A0A0D0NR73_KITGR 
ID   A0A0D0NR73_KITGR        Unreviewed;       338 AA.
AC   A0A0D0NR73;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 29.
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=TR51_19990 {ECO:0000313|EMBL:KIQ61611.1};
OS   Kitasatospora griseola (Streptomyces griseolosporeus).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=2064 {ECO:0000313|EMBL:KIQ61611.1, ECO:0000313|Proteomes:UP000032066};
RN   [1] {ECO:0000313|EMBL:KIQ61611.1, ECO:0000313|Proteomes:UP000032066}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MF730-N6 {ECO:0000313|EMBL:KIQ61611.1,
RC   ECO:0000313|Proteomes:UP000032066};
RA   Arens J.C., Haltli B., Kerr R.G.;
RT   "Draft genome sequence of Kitasatospora griseola MF730-N6, a bafilomycin,
RT   terpentecin and satosporin producer.";
RL   Submitted (FEB-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   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via 2-oxoglutarate.
CC       {ECO:0000256|ARBA:ARBA00004767}.
CC   -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000256|ARBA:ARBA00004792}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000256|ARBA:ARBA00008056, ECO:0000256|RuleBase:RU003682}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIQ61611.1}.
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DR   EMBL; JXZB01000004; KIQ61611.1; -; Genomic_DNA.
DR   RefSeq; WP_043913159.1; NZ_JXZB01000004.1.
DR   AlphaFoldDB; A0A0D0NR73; -.
DR   STRING; 2064.TR51_19990; -.
DR   PATRIC; fig|2064.6.peg.4299; -.
DR   OrthoDB; 21825at2; -.
DR   Proteomes; UP000032066; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009693; P:ethylene biosynthetic process; 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   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
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:UP000032066}.
FT   DOMAIN          175..279
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   338 AA;  37163 MW;  802004E3BB5C7C7E CRC64;
     MTMQHPTALP VIDLSLADGT PAERDRLRRE LREAATGVGF FQLVGHGVTA AETVDLTSAM
     RAFFALPEAD RLSVSNLNSP HFRGYTRTGD ERTGGSRDWR DQLDIGPELP AHVPAPGEPA
     YWWLEGPNQW PAALPELRTA ALHWIARLDG VARRLLHELL ASIGARPDFY DDAFTPHPHL
     HLKLVRYPGT APDGAAQGVG THKDYGFITL LLQDTVGGLQ VERPDHTFLD VPPMEGAFVV
     NLGELLEVAT DGYLKATSHR VLSPAGARER FSVPFFYNPR LDAHIAPLDF PHAHHAPGAT
     QDPANPLHAD FGFNELKGFA RAHPEVTRRH HAELLPQA
//
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