ID   ACCO2_MALDO             Reviewed;         330 AA.
AC   O48882;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 2;
DE            Short=ACC oxidase 2;
DE            EC=1.14.17.4;
DE   AltName: Full=Ethylene-forming enzyme;
DE            Short=EFE;
GN   Name=ACO2;
OS   Malus domestica (Apple) (Pyrus malus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX   NCBI_TaxID=3750;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Fuji; TISSUE=Fruit;
RA   Nam K.H., Kim W.T.;
RT   "ACC oxidase from apple fruit.";
RL   Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening.
CC   -!- INDUCTION: By ethylene and wounding.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AF015787; AAB94031.1; -; Genomic_DNA.
DR   PIR; T16988; T16988.
DR   AlphaFoldDB; O48882; -.
DR   SMR; O48882; -.
DR   STRING; 3750.XP_008371045.1; -.
DR   BRENDA; 1.14.17.4; 3164.
DR   UniPathway; UPA00384; UER00563.
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   Vitamin C.
FT   CHAIN           1..330
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 2"
FT                   /id="PRO_0000067266"
FT   DOMAIN          153..253
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         177
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         179
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         234
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   330 AA;  37522 MW;  B95C491D13C20C6E CRC64;
     MATFPVVDMD LINGEERAAT LEKINDACEN WGFFELVNHG ISTELLDTVE KMNKDHYKKT
     MEQRFKEMVA AKGLEAVQSE IHYLDWESTF FLRHLPSSNI SEIPDLEEDY RKTMKEFAVE
     LEKLAEKLLD LLCENLGLEK GYLKKAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
     GGIILLFQDD KVSGLQLLKD GEWMDVPPVH HSIVINLGDQ IEVITNGKYK SIMHRVIAQS
     DGTRMSIASF YNPGDDAFIS PAPALLEEKS EVSPTYPKFL FDDYMKLYSG LKFQAKEPRF
     EAMKARETTP VETARGLRAV RWNTTKRNQN