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ACCO3_PETHY
ID   ACCO3_PETHY             Reviewed;         320 AA.
AC   Q08507;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 3;
DE            Short=ACC oxidase 3;
DE            EC=1.14.17.4;
DE   AltName: Full=Ethylene-forming enzyme;
DE            Short=EFE;
GN   Name=ACO3;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8292780; DOI=10.1007/bf00042349;
RA   Tang X., Wang H., Brandt A.S., Woodson W.R.;
RT   "Organization and structure of the 1-aminocyclopropane-1-carboxylate
RT   oxidase gene family from Petunia hybrida.";
RL   Plant Mol. Biol. 23:1151-1164(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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; L21978; AAA33697.1; -; Genomic_DNA.
DR   PIR; S42561; S42561.
DR   AlphaFoldDB; Q08507; -.
DR   SMR; Q08507; -.
DR   UniPathway; UPA00384; UER00563.
DR   GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016706; F:2-oxoglutarate-dependent dioxygenase activity; IEA:UniProt.
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:0009805; P:coumarin biosynthetic process; IEA:UniProt.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0002238; P:response to molecule of fungal origin; IEA:UniProt.
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   Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..320
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 3"
FT                   /id="PRO_0000067272"
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   320 AA;  36274 MW;  7ED735D6D721EEE0 CRC64;
     MENFPIINLE KLNGSERDAT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KLTKGHYKKC
     MEQRFKELVA SKGLEAVQAE VTDLDWESTF FLRHLPVSNI SEVPDLDDEY REVMRDFAKR
     LEKLAEELLD LLCENLGLEK GYLKKAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
     GGIILLFQDD KVSGLQLLKD GQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVLHRVIAQT
     DGTRMSLASF YNPGSDAVIY PAPTLVEKEA DQECKQVYPK FVFDDYMKLY AGLKFQAKEP
     RFEAMKAREA DVKSDPIATA
 
 
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