ID A0A0U4NDI1_9GAMM Unreviewed; 317 AA.
AC A0A0U4NDI1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=ATY27_10155 {ECO:0000313|EMBL:ALZ76094.1}, ATY27_19500
GN {ECO:0000313|EMBL:ALZ77725.1};
OS Rheinheimera sp. F8.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=1763998 {ECO:0000313|EMBL:ALZ76094.1, ECO:0000313|Proteomes:UP000059499};
RN [1] {ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|Proteomes:UP000059499};
RA Schuster A.K., Szewzyk U.;
RT "Draft genome sequence of Rheinheimera sp. F8, a biofilm-forming strain
RT which produces large amounts of extracellular DNA.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ALZ76094.1, ECO:0000313|Proteomes:UP000059499}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F8 {ECO:0000313|EMBL:ALZ76094.1,
RC ECO:0000313|Proteomes:UP000059499};
RX PubMed=26966195;
RA Schuster A.K., Szewzyk U.;
RT "Draft Genome Sequence of Rheinheimera sp. F8, a Biofilm-Forming Strain
RT Which Produces Large Amounts of Extracellular DNA.";
RL Genome Announc. 4:0-0(2016).
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; CP013656; ALZ76094.1; -; Genomic_DNA.
DR EMBL; CP013656; ALZ77725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U4NDI1; -.
DR Proteomes; UP000059499; 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:UP000059499}.
FT DOMAIN 165..271
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 317 AA; 35344 MW; 3CF2DCDAD13CB479 CRC64;
MTQQQVPTLD IRRFATDKDA FVAEIGKAYT EFGFCGISGH GIADEVVGET YKAIKQFFAL
PTEVKQQYHV PGQGGARGYT GFGVEKAKDS KHPDLKEFFH VGRELNGPAQ HECLYPNVWP
SEVPEFKAAT YTLYQALENL GCQVLEALAL FLKQEQQYFA DKVNYGNSIL RPIHYPPIQD
TSTQSIRAGQ HEDINLITLL VGSHESGLEI LRRDGSWLPV TTIPGTIVVN IGDMLQRLTN
HVLPSTTHRV VNPAGAAAGQ PRYSIPFFMH PNPDFVIETL SSCVSAENPD RYPQPINSND
YLLQRLEEIG LLKKAKY
//
