ID   ACCO3_CUCME             Reviewed;         320 AA.
AC   P54847;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 3;
DE            Short=ACC oxidase 3;
DE            EC=1.14.17.4;
DE   AltName: Full=Ethylene-forming enzyme;
DE            Short=EFE;
GN   Name=ACO3;
OS   Cucumis melo (Muskmelon).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3656;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Cantaloup Charentais; TISSUE=Leaf;
RX   PubMed=8628251; DOI=10.1007/bf02174348;
RA   Lasserre E., Bouquin T., Hernandez J.A., Bull J., Pech J.-C., Balague C.;
RT   "Structure and expression of three genes encoding ACC oxidase homologs from
RT   melon (Cucumis melo L.).";
RL   Mol. Gen. Genet. 251:81-90(1996).
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;
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC   -!- TISSUE SPECIFICITY: Flowers.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; X95553; CAA64799.1; -; Genomic_DNA.
DR   PIR; S66176; S66176.
DR   AlphaFoldDB; P54847; -.
DR   SMR; P54847; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   UniPathway; UPA00384; UER00563.
DR   Proteomes; UP000089565; Unplaced.
DR   GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.330; -; 1.
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   Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR   Pfam; PF14226; DIOX_N; 1.
DR   PROSITE; PS51471; FE2OG_OXY; 1.
PE   2: Evidence at transcript level;
KW   Ethylene biosynthesis; Fruit ripening; Iron; Metal-binding; Oxidoreductase;
KW   Reference proteome; Vitamin C.
FT   CHAIN           1..320
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 3"
FT                   /id="PRO_0000067255"
FT   DOMAIN          154..254
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         178
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         180
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         235
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   320 AA;  36397 MW;  60D95E5D5FAF34FF CRC64;
     MEMDFPVINM NNLNGESRVS VLNQINDACE NWGFFELVNH GISHELMDKV EKLTKEHYRK
     CMEQRFKEMV ASKGLDSVET EINDTDWEST FFLRHLPVSN MSEIGDLDEE YKKVMKEFAD
     ELEKLAEEVL DLLCENLGLE KGYLKKVFYG SKGPNFGTKV SNYPPCPKPE LIKGLRAHTD
     AGGLILLFQD DKVSGLHVLK DGKWVDVPPM HHSIVINLGD QLEVITNGKY KSVMHRVIAQ
     EDGNRMSIAS FYNPGNDAVI YPAPALVEGE QEKTKLYPKF VFDDYMKLYV GLKFQAKEPR
     FEAMKAMEST NLNMGPIATV