ID A0A1H9VFR7_9RHOB Unreviewed; 302 AA.
AC A0A1H9VFR7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=SAMN04490244_10786 {ECO:0000313|EMBL:SES20535.1};
OS Tranquillimonas rosea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Tranquillimonas.
OX NCBI_TaxID=641238 {ECO:0000313|EMBL:SES20535.1, ECO:0000313|Proteomes:UP000198885};
RN [1] {ECO:0000313|EMBL:SES20535.1, ECO:0000313|Proteomes:UP000198885}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23042 {ECO:0000313|EMBL:SES20535.1,
RC ECO:0000313|Proteomes:UP000198885};
RA de Groot N.N.;
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 -!- 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FOGU01000007; SES20535.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9VFR7; -.
DR STRING; 641238.SAMN04490244_10786; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000198885; 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: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 Iron {ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000198885}.
FT DOMAIN 168..264
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 302 AA; 32247 MW; 25900510AE47EBC2 CRC64;
MIPVLDWQRF LSGDAAGFVA DLGRACRGPG FFLLTNHAIP TALTDGIFGA AERFFALPEA
QKAPLDIRRN PHNRGWVPGG SESLDAASGQ VDRKEAFNVG LDLAPDDPRI LAGEPFRGVN
LWPALDGFDA ACLAYYDAAW RQGTALMGAV ARDLGLSPAH FDGAFRAPLA TLRLLHYPPG
GGGIGAGAHT DYGALTLLAT DGEPGLQVLP RGGEWTDVPH LEGALVVNIG DCLMRWTNDI
YASTPHRVRP PRRQRRSVAF FLDPDPDAEI AALPGTGAPV YPPVTGAAYL RSRLEATYSE
DT
//
