ID   ACCO_DIACA              Reviewed;         321 AA.
AC   P31528;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Probable 1-aminocyclopropane-1-carboxylate oxidase;
DE            Short=ACC oxidase;
DE            EC=1.14.17.4;
DE   AltName: Full=Ethylene-forming enzyme;
DE            Short=EFE;
DE   AltName: Full=Senescence-related protein;
GN   Name=ACO; Synonyms=CARSR120;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16668239; DOI=10.1104/pp.96.3.1000;
RA   Wang H., Woodson W.R.;
RT   "A flower senescence-related mRNA from carnation shares sequence similarity
RT   with fruit ripening-related mRNAs involved in ethylene biosynthesis.";
RL   Plant Physiol. 96:1000-1001(1991).
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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; M62380; AAA33276.1; -; mRNA.
DR   PIR; S30606; S30606.
DR   AlphaFoldDB; P31528; -.
DR   SMR; P31528; -.
DR   BRENDA; 1.14.17.4; 1925.
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..321
FT                   /note="Probable 1-aminocyclopropane-1-carboxylate oxidase"
FT                   /id="PRO_0000067257"
FT   DOMAIN          159..259
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         185
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         240
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   321 AA;  36819 MW;  424ADD80BD4DAD5B CRC64;
     MANIVNFPII DMEKLNNYNG VERSLVLDQI KDACHNWGFF QVVNHSLSHE LMDKVERMTK
     EHYKKFREQK FKDMVQTKGL VSAESQVNDI DWESTFYLRH RPTSNISEVP DLDDQYRKLM
     KEFAAQIERL SEQLLDLLCE NLGLEKAYLK NAFYGANGPT FGTKVSNYPP CPKPDLIKGL
     RAHTDAGGII LLFQDDKVSG LQLLKDGHWV DVPPMKHSIV VNLGDQLEVI TNGKYKSVMH
     RVIAQTDGNR MSIASFYNPG SDAVIYPAPT LVEKEEEKCR AYPKFVFEDY MNLYLKLKFQ
     EKEPRFEAMK AMETTGPIPT A