ACCO_TOBAC
ID ACCO_TOBAC Reviewed; 319 AA.
AC Q43792; Q9SXL3;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase;
DE Short=ACC oxidase;
DE EC=1.14.17.4;
DE AltName: Full=Ethylene-forming enzyme;
DE Short=EFE;
GN Name=ACO;
OS Nicotiana tabacum (Common tobacco).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC Nicotiana.
OX NCBI_TaxID=4097;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Samsun NN; TISSUE=Leaf;
RA Knoester M., Bol J.F., Van Loon L.C., Linthorst H.J.M.;
RT "Sequence of a cDNA clone encoding tobacco ethylene-forming enzyme.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC STRAIN=cv. Samsun NN; TISSUE=Leaf;
RA Ohtsubo N., Mitsuhara I., Koga M., Seo S., Ohashi Y.;
RT "Ethylene promotes the necrotic lesion formation and basic PR gene
RT expression in TMV-infected tobacco.";
RL Plant Cell Physiol. 40:808-817(1999).
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; Evidence={ECO:0000250};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC -!- INDUCTION: Up-regulated during the early stage of hypersensitive
CC response. {ECO:0000269|Ref.2}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; Z46349; CAA86468.1; -; mRNA.
DR EMBL; AB012857; BAA83466.1; -; mRNA.
DR PIR; S48811; S48811.
DR RefSeq; NP_001312238.1; NM_001325309.1.
DR AlphaFoldDB; Q43792; -.
DR SMR; Q43792; -.
DR STRING; 4097.Q43792; -.
DR GeneID; 107781126; -.
DR KEGG; nta:107781126; -.
DR UniPathway; UPA00384; UER00563.
DR Proteomes; UP000084051; Unplaced.
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:0051213; F:dioxygenase activity; IBA:GO_Central.
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:0006952; P:defense response; IEA:UniProtKB-KW.
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 2: Evidence at transcript level;
KW Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase; Plant defense;
KW Reference proteome; Vitamin C.
FT CHAIN 1..319
FT /note="1-aminocyclopropane-1-carboxylate oxidase"
FT /id="PRO_0000386525"
FT DOMAIN 152..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"
FT CONFLICT 119
FT /note="K -> Q (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="K -> Q (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="S -> A (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
FT CONFLICT 167
FT /note="K -> Q (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="T -> S (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
FT CONFLICT 211
FT /note="L -> H (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="Y -> N (in Ref. 2; BAA83466)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 319 AA; 36187 MW; 94598EEF2F486636 CRC64;
MENFPIINLE KLNGSERADT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KMTKGHYKKC
MEQRFKELVA SKGLEAVQAE VTDLDWESTF FLRHLPVSNI CEVPDLDDQY REVMRDFAKR
LEKLAEELLD LLCENLGLEK GYLKKIFYGT KGPNFGSKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVTGLQLLKD GQWIDVPPMR LSIVVNLGDQ LEVITNGKYK SVMHRVITQT
DGTRMSLASF YNPGSDAVIF PAPTLVEKEA EESKAIYPKF VFDDYMKLYA GLKFQAKEPR
FEAMIKAMET VKSDPVATA
