ID   ACCO1_DORSP             Reviewed;         327 AA.
AC   P31238;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 86.
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;
GN   Name=ACO1; Synonyms=ACO;
OS   Doritaenopsis sp. (Moth orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Vandeae; Aeridinae; x Doritaenopsis;
OC   unclassified x Doritaenopsis.
OX   NCBI_TaxID=4749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hausermann's red bird 'Cardinal'; TISSUE=Gynoecium;
RX   PubMed=7516081; DOI=10.1104/pp.103.1.31;
RA   Nadeau J.A., Zhang X., Nair H., O'Neill S.D.;
RT   "Temporal and spatial regulation of 1-aminocyclopropane-1-carboxylate
RT   oxidase in the pollination-induced senescence of orchid flowers.";
RL   Plant Physiol. 103:31-39(1993).
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   -!- INDUCTION: By pollination.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA21611.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L07912; AAA21611.1; ALT_INIT; mRNA.
DR   PIR; JQ2274; JQ2274.
DR   AlphaFoldDB; P31238; -.
DR   SMR; P31238; -.
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..327
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 1"
FT                   /id="PRO_0000067259"
FT   DOMAIN          157..257
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
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         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   327 AA;  37234 MW;  D4EC83D9971059EE CRC64;
     MESGSFPVIN MELLQGSQRP AAMALLRDAC ENWGLYELLN HGISHELMNR VETVNKEHYR
     RFREQRFKEF ASKTLDTVEN VEPENLDWES TFFLRHLPTS NISQIPDLDD DCRSTMKEFA
     LELENLAERL LDLLCEDLGL EKGYLKKVFC GGSDGLPTFG TKVSNYPPCP KPELIKGLRA
     HTDAGGIILL FQDDKVSGLQ LLKDGEWIDV PPVRHSIVVN IGDQLEVITN GKYKSVLHRV
     VAQTDGNRMS IASFYNPGSD AVIFPAPALV EKEAEEKEEK KKEIYPKFVF QDYMNLYIRK
     KFEAKEPRFE AMKSMEIVMS SQPIPTA