GenomeNet

Database: UniProt
Entry: I4ETV0_9ACTN
LinkDB: I4ETV0_9ACTN
Original site: I4ETV0_9ACTN 
ID   I4ETV0_9ACTN            Unreviewed;       209 AA.
AC   I4ETV0;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 38.
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   OrderedLocusNames=MODMU_1364 {ECO:0000313|EMBL:CCH86813.1};
OS   Modestobacter marinus.
OC   Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC   Geodermatophilaceae; Modestobacter.
OX   NCBI_TaxID=477641 {ECO:0000313|EMBL:CCH86813.1, ECO:0000313|Proteomes:UP000006461};
RN   [1] {ECO:0000313|EMBL:CCH86813.1, ECO:0000313|Proteomes:UP000006461}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BC501 {ECO:0000313|EMBL:CCH86813.1,
RC   ECO:0000313|Proteomes:UP000006461};
RX   PubMed=22887672; DOI=10.1128/JB.01029-12;
RA   Normand P., Gury J., Pujic P., Chouaia B., Crotti E., Brusetti L.,
RA   Daffonchio D., Vacherie B., Barbe V., Medigue C., Calteau A.,
RA   Ghodhbane-Gtari F., Essoussi I., Nouioui I., Abbassi-Ghozzi I., Gtari M.;
RT   "Genome Sequence of Radiation-Resistant Modestobacter marinus Strain BC501,
RT   a Representative Actinobacterium That Thrives on Calcareous Stone
RT   Surfaces.";
RL   J. Bacteriol. 194:4773-4774(2012).
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   ---------------------------------------------------------------------------
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; FO203431; CCH86813.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4ETV0; -.
DR   STRING; 477641.MODMU_1364; -.
DR   KEGG; mmar:MODMU_1364; -.
DR   PATRIC; fig|477641.3.peg.1291; -.
DR   eggNOG; COG3491; Bacteria.
DR   HOGENOM; CLU_010119_6_3_11; -.
DR   Proteomes; UP000006461; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   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:UP000006461}.
FT   DOMAIN          62..192
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000259|PROSITE:PS51471"
FT   REGION          181..209
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   209 AA;  22210 MW;  87209DFA53636115 CRC64;
     MTGTVEEEWY APNSWPAEVP GLRPAATAFS AACAGVAEDL LRVAALALDL ADDFFVSRCT
     GDTWTVELDR FPARQEVGTV LPGQLRAGPH TDAGTLALVD REPGSGGLQV RALDGCWVDA
     PFVPGALTVN AGDLLARWTG DRWRSTPHRV LPPPVELPGE ELLDLAFRAE ADPGTVVERL
     PTPAAGPTRY EPVTAGRFRR SRSGSVSVG
//
DBGET integrated database retrieval system