ID A0A0S3RK66_PHAAN Unreviewed; 310 AA.
AC A0A0S3RK66;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=aminocyclopropanecarboxylate oxidase {ECO:0000256|ARBA:ARBA00039090};
DE EC=1.14.17.4 {ECO:0000256|ARBA:ARBA00039090};
DE AltName: Full=Ethylene-forming enzyme {ECO:0000256|ARBA:ARBA00041616};
GN Name=Vigan.03G063600 {ECO:0000313|EMBL:BAT81000.1};
GN ORFNames=VIGAN_03063600 {ECO:0000313|EMBL:BAT81000.1};
OS Vigna angularis var. angularis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=157739 {ECO:0000313|EMBL:BAT81000.1, ECO:0000313|Proteomes:UP000291084};
RN [1] {ECO:0000313|EMBL:BAT81000.1, ECO:0000313|Proteomes:UP000291084}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Shumari {ECO:0000313|Proteomes:UP000291084};
RX PubMed=26616024; DOI=10.1038/srep16780;
RA Sakai H., Naito K., Ogiso-Tanaka E., Takahashi Y., Iseki K., Muto C.,
RA Satou K., Teruya K., Shiroma A., Shimoji M., Hirano T., Itoh T., Kaga A.,
RA Tomooka N.;
RT "The power of single molecule real-time sequencing technology in the de
RT novo assembly of a eukaryotic genome.";
RL Sci. Rep. 5:16780-16780(2015).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-aminocyclopropane-1-carboxylate + L-ascorbate + O2 = CO2 +
CC ethene + 2 H2O + hydrogen cyanide + L-dehydroascorbate;
CC Xref=Rhea:RHEA:23640, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:18153, ChEBI:CHEBI:18407,
CC ChEBI:CHEBI:38290, ChEBI:CHEBI:58360, ChEBI:CHEBI:58539;
CC EC=1.14.17.4; Evidence={ECO:0000256|ARBA:ARBA00036392};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000256|ARBA:ARBA00001962};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC {ECO:0000256|ARBA:ARBA00037892}.
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; AP015036; BAT81000.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S3RK66; -.
DR Proteomes; UP000291084; Chromosome 3.
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; PTHR47991:SF42; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Ethylene biosynthesis {ECO:0000256|ARBA:ARBA00022666};
KW Fruit ripening {ECO:0000256|ARBA:ARBA00033478};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003682};
KW Metal-binding {ECO:0000256|RuleBase:RU003682};
KW Oxidoreductase {ECO:0000256|RuleBase:RU003682};
KW Reference proteome {ECO:0000313|Proteomes:UP000291084}.
FT DOMAIN 153..253
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000259|PROSITE:PS51471"
FT COILED 107..134
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 310 AA; 35421 MW; 0CEDE088A36EA36C CRC64;
MEKFPVINLA NINGEEKKAT LEQIEDACQN WGFFELVNHG IPHELLDRVE RLTKEHYRKC
MEKRFNEAVG SKGLERVQDE LKDMDWESTF FLRHLPTSNI SEIPDLTEEY RDAMKEFAEK
LEKLAEELLD MLCENLGLEK GYLKRAFYGS RGPNFGTKVA NYPACPKPEL VKGLRAHTDA
GGIILLLQDD KVSGLQLLKD GKWVDVPPMR HSIVVNLGDQ IEVISNGKYK SVEHRVIARS
DGTRMSVASF YNPGSDAVIY PAPPLLEKEA KETEVVYPKF VFEDYMKLYA TLKFQPKEPR
FQAFNALNSS
//
