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Database: UniProt
Entry: A0A0N0JHT7_9SPHN
LinkDB: A0A0N0JHT7_9SPHN
Original site: A0A0N0JHT7_9SPHN 
ID   A0A0N0JHT7_9SPHN        Unreviewed;       330 AA.
AC   A0A0N0JHT7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, 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=IP65_07480 {ECO:0000313|EMBL:KPF54565.1};
OS   Novosphingobium sp. AAP1.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF54565.1, ECO:0000313|Proteomes:UP000037880};
RN   [1] {ECO:0000313|EMBL:KPF54565.1, ECO:0000313|Proteomes:UP000037880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP1 {ECO:0000313|EMBL:KPF54565.1,
RC   ECO:0000313|Proteomes:UP000037880};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-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|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:KPF54565.1}.
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DR   EMBL; LJHO01000003; KPF54565.1; -; Genomic_DNA.
DR   RefSeq; WP_022678419.1; NZ_LJHO01000003.1.
DR   AlphaFoldDB; A0A0N0JHT7; -.
DR   STRING; 1523413.IP65_07480; -.
DR   PATRIC; fig|1523413.3.peg.2458; -.
DR   OrthoDB; 21825at2; -.
DR   Proteomes; UP000037880; 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   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:UP000037880}.
FT   DOMAIN          168..266
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
SQ   SEQUENCE   330 AA;  36628 MW;  C4AE2E5D335C0D4E CRC64;
     MPDHALPLVD ISRLQSPSRA DRLAVAQELD RACVEAGFLY VTGSQIDAGL RARLVARAQD
     YFSQDLATKM QGYIGLSHNH SGYVPVGEEQ FGSGPADLKE AYDINIDYHG SERRPLLGPN
     LWPAMPGFRA DVQAWYAHLT GISHQLFRAF ALALGLDETH FDAHLRHPPS QLRLIHYPHD
     PAAQDRPGIG AHTDYECFTL LHVTAPGLQV VDRHGAWFDV PLIDGALIMN VGDMMEIMSN
     GRYLATKHRV KTVAQERYSF PLFCSCDYDH VIAPVVRGEA PRYRPIKGGE HLFNQTAQTF
     AYLKQRIARG DLVLNDPVPL ASFGRPEAGA
//
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