ID   ACCO1_DICMU             Reviewed;         368 AA.
AC   A6BM06;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 49.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase;
DE            Short=ACC oxidase;
DE            Short=Dmaco;
DE            EC=1.14.17.4;
DE   AltName: Full=Ethylene-forming enzyme;
DE            Short=EFE;
GN   Name=aco;
OS   Dictyostelium mucoroides (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=31287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=17499244; DOI=10.1016/j.yexcr.2007.04.012;
RA   Amagai A., Soramoto S., Saito S., Maeda Y.;
RT   "Ethylene induces zygote formation through an enhanced expression of zyg1
RT   in Dictyostelium mucoroides.";
RL   Exp. Cell Res. 313:2493-2503(2007).
CC   -!- FUNCTION: Involved in ethylene biosynthesis and macrocyst formation.
CC       Overexpression induces overproduction of ethylene and augmented zyg1
CC       expression and zygote formation. {ECO:0000269|PubMed:17499244}.
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(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC       Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC       ProRule:PRU00805};
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC   -!- DISRUPTION PHENOTYPE: Show reduced level of ethylene production,
CC       suppressed zyg1 expression thus resulting in inhibition of zygote
CC       formation and impaired macrocyst formation.
CC       {ECO:0000269|PubMed:17499244}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB291210; BAF64840.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6BM06; -.
DR   SMR; A6BM06; -.
DR   PRIDE; A6BM06; -.
DR   UniPathway; UPA00384; UER00563.
DR   GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051213; F:dioxygenase activity; 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   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   3: Inferred from homology;
KW   Dioxygenase; Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..368
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase"
FT                   /id="PRO_0000392076"
FT   DOMAIN          177..307
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   REGION          191..226
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        202..225
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         229
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         231
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         287
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         298
FT                   /ligand="2-oxoglutarate"
FT                   /ligand_id="ChEBI:CHEBI:16810"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   368 AA;  42885 MW;  E103467A6B8A4DD4 CRC64;
     MEIDIEKLPI IDISSFQNNE NDKNQVAKEI NKACKEYGFF YIKNHGVDQE LIENLQNVIK
     KFFSLPLEIK MKWKMGLTNR EWLGFFKVGQ EITYGQVDWK EGCYYSSEMD GDINTIHNVP
     LYPTAEQEEQ YEIQGFKSTI HTYIEKLTHL SQQIIEAISL SLNLPQDYFF KNYTYDPFIL
     MGLLHYPSFH HQEQEEEQED DESNNGGKKS PNPDESKKPE VEKFGTGQHT DWGLLTVLYQ
     DDVGGLQVKS KNSEEYIDAP PIPGTFICNI GDMLDKMTGG YYLSNLHRVK YNKSGRDRFS
     IPFFLDPSLN SIPKLIPNYD QLSQFADKPE RWDKQNIHEF DGTYGQYFIK KIGRVFPDYV
     YKKSGELV