ID A0A1H0PI44_9ACTN Unreviewed; 342 AA.
AC A0A1H0PI44;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=SAMN04487981_11614 {ECO:0000313|EMBL:SDP04663.1};
OS Streptomyces sp. cf386.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1761904 {ECO:0000313|EMBL:SDP04663.1, ECO:0000313|Proteomes:UP000198720};
RN [1] {ECO:0000313|Proteomes:UP000198720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF386 {ECO:0000313|Proteomes:UP000198720};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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 -!- 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}.
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DR EMBL; FNHV01000016; SDP04663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0PI44; -.
DR STRING; 1761904.SAMN04487981_11614; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000198720; 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:UP000198720}.
FT DOMAIN 176..277
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 342 AA; 37826 MW; 4BE14D5BBB235C6D CRC64;
MAQPTALPVI DISRFSAPDA DRDSFLAELR AAAHEVGFFY VTGHGVPVSL QDEILGAART
FFALPEERRL EIENVNSPQF RGYTRTGTEH TGGNADWREQ IDIGPERAAL DTGPHDPAYL
RLIGPNQWPS AQPELREIVL RWQAEALRVS REVLRALAAA LGQDEGYFDT WFDDEAAVYV
KIVHYPPRVA QDADQGVGAH KDYGYLALLQ QDEVGGLQVQ REDGEWIDAP PVPGAFVLNI
GEMLEIATQG YLKATQHRVV SPQSGVERFS IPFFLGPRLD AVVEPLHLPT ELAARSRGVT
DDPNNPLLAA YGENAVVGWL RSHPRVAERW WADVLVEQGG AR
//
