ID   ACCO1_CUCME             Reviewed;         318 AA.
AC   Q04644;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 1;
DE            Short=ACC oxidase 1;
DE            EC=1.14.17.4;
DE   AltName: Full=Ethylene-forming enzyme;
DE            Short=EFE;
DE   AltName: Full=PMEL1;
GN   Name=ACO1;
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 [MRNA].
RC   STRAIN=cv. Cantaloup Charentais; TISSUE=Fruit;
RX   PubMed=8444161; DOI=10.1111/j.1432-1033.1993.tb17628.x;
RA   Balague C., Watson C.F., Turner A.J., Rouge P., Picton S., Pech J.-C.,
RA   Grierson D.;
RT   "Isolation of a ripening and wound-induced cDNA from Cucumis melo L.
RT   encoding a protein with homology to the ethylene-forming enzyme.";
RL   Eur. J. Biochem. 212:27-34(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Andes; TISSUE=Fruit;
RA   Yamamoto M., Miki T., Ishiki Y., Nakagawa H., Ogura N., Sato T.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [3]
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: Fruit.
CC   -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; X69935; CAA49553.1; -; mRNA.
DR   EMBL; D31727; BAA06526.1; -; mRNA.
DR   EMBL; X95551; CAA64797.1; -; Genomic_DNA.
DR   PIR; JC6059; JC6059.
DR   RefSeq; NP_001284392.1; NM_001297463.1.
DR   AlphaFoldDB; Q04644; -.
DR   SMR; Q04644; -.
DR   GeneID; 103491357; -.
DR   KEGG; cmo:103491357; -.
DR   eggNOG; KOG0143; Eukaryota.
DR   OrthoDB; 755371at2759; -.
DR   BioCyc; MetaCyc:MON-15544; -.
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..318
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 1"
FT                   /id="PRO_0000067254"
FT   DOMAIN          153..254
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   318 AA;  36127 MW;  6B8E8A7B80C75D5C CRC64;
     MAVFPIINLE NINDDGRAKI LEQIEDACQN WGFFELVNHG IPHEFLDMVE KMTRDHYKKC
     MEERFKETVL SKGLEAAQAE VNDMDWESTF FLRHLPESNI SQMSDLDEEY KKIMKEFAKK
     LENLAEELLD LLCENLGLEK GYLKKAFYGS KGPTFGTKVS NYPPCPKPDL IKGLRAHTDA
     GGIILLFQDD KVSGLQLLKD GNWIDVPPMR HAIVVNLGDQ LEVITNGRYK SVMHRVLTQT
     SGTGRMSIAS FYNPGSDAVI YPAPALVEKD QDEEKKEVYP KFVFEDYMKL YLGVKFQAKE
     PRFEAMKANA NLGPMATA