ID E4TRN5_MARTH Unreviewed; 324 AA.
AC E4TRN5;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=Ftrac_1768 {ECO:0000313|EMBL:ADR21756.1};
OS Marivirga tractuosa (strain ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408
OS / VKM B-1430 / H-43) (Microscilla tractuosa) (Flexibacter tractuosus).
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Marivirgaceae; Marivirga.
OX NCBI_TaxID=643867 {ECO:0000313|EMBL:ADR21756.1, ECO:0000313|Proteomes:UP000008720};
RN [1] {ECO:0000313|EMBL:ADR21756.1, ECO:0000313|Proteomes:UP000008720}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23168 / DSM 4126 / NBRC 15989 / NCIMB 1408 / VKM B-1430 /
RC H-43 {ECO:0000313|Proteomes:UP000008720};
RX PubMed=21677852; DOI=10.4056/sigs.1623941;
RA Pagani I., Chertkov O., Lapidus A., Lucas S., Del Rio T.G., Tice H.,
RA Copeland A., Cheng J.F., Nolan M., Saunders E., Pitluck S., Held B.,
RA Goodwin L., Liolios K., Ovchinikova G., Ivanova N., Mavromatis K., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA Han C., Tapia R., Ngatchou-Djao O.D., Rohde M., Goker M., Spring S.,
RA Sikorski J., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Marivirga tractuosa type strain (H-43).";
RL Stand. Genomic Sci. 4:154-162(2011).
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 -!- 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; CP002349; ADR21756.1; -; Genomic_DNA.
DR RefSeq; WP_013453903.1; NC_014759.1.
DR AlphaFoldDB; E4TRN5; -.
DR STRING; 643867.Ftrac_1768; -.
DR KEGG; mtt:Ftrac_1768; -.
DR eggNOG; COG3491; Bacteria.
DR HOGENOM; CLU_010119_6_3_10; -.
DR OrthoDB; 21825at2; -.
DR Proteomes; UP000008720; 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 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:UP000008720}.
FT DOMAIN 173..282
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
SQ SEQUENCE 324 AA; 36665 MW; 334525134DF2A687 CRC64;
MSKKLYDEIP SLNLEDFTNG TEETKAQFVK ELGEAYNNIG FVAIKGHYLS NELSQKLYAA
VEKFFNLSTE QKKAYEKEEL AGQRGYTSKG KEQAKGHKVP DLKEFYQVGQ FVPDDHELKK
EYPDNLWPSE VPELAELAKD AYQKLEKTGF EMLRAIAIYL GLDENYFDSE VTYGNSILRA
IHYPPIENPE DLPEDAVRAA QHGDINLITL LMGASADGLQ VLRRDGEWIP ITALPNQLVV
NVGDMLARLT NDKLKSTIHR VVNPAKEQMK SSRYSIPFFM HPKSSMDLTC LDSCVDTDNP
KKYEDMSAGE FLAERLAEIG LLKK
//
