ACCO1_SOLLC
ID ACCO1_SOLLC Reviewed; 315 AA.
AC P05116;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 2.
DT 03-AUG-2022, entry version 128.
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;
DE AltName: Full=Protein pTOM 13;
GN Name=ACO1; Synonyms=ETH1;
OS Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC Solanum subgen. Lycopersicon.
OX NCBI_TaxID=4081;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ailsa Craig;
RX PubMed=1868215; DOI=10.1007/bf00036816;
RA Koeck M., Hamilton A.J., Grierson D.;
RT "eth1, a gene involved in ethylene synthesis in tomato.";
RL Plant Mol. Biol. 17:141-142(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 21-315.
RC STRAIN=cv. Ailsa Craig;
RX PubMed=3029690; DOI=10.1093/nar/15.2.731;
RA Holdsworth M.J., Bird C.R., Ray J., Schuch W., Grierson D.;
RT "Structure and expression of an ethylene-related mRNA from tomato.";
RL Nucleic Acids Res. 15:731-739(1987).
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 -!- TISSUE SPECIFICITY: Predominantly expressed in the petals and the
CC stigma and style.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; X58273; CAA41212.1; -; Genomic_DNA.
DR EMBL; X04792; CAA28479.1; -; mRNA.
DR PIR; S16591; S16591.
DR RefSeq; NP_001234024.2; NM_001247095.2.
DR AlphaFoldDB; P05116; -.
DR SMR; P05116; -.
DR STRING; 4081.Solyc07g049530.2.1; -.
DR PaxDb; P05116; -.
DR PRIDE; P05116; -.
DR EnsemblPlants; Solyc07g049530.3.1; Solyc07g049530.3.1; Solyc07g049530.3.
DR GeneID; 544052; -.
DR Gramene; Solyc07g049530.3.1; Solyc07g049530.3.1; Solyc07g049530.3.
DR KEGG; sly:544052; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR InParanoid; P05116; -.
DR OMA; DLDDHYR; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; P05116; -.
DR BRENDA; 1.14.17.4; 3101.
DR UniPathway; UPA00384; UER00563.
DR Proteomes; UP000004994; Chromosome 7.
DR ExpressionAtlas; P05116; baseline and differential.
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:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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; Fruit ripening; Iron; Metal-binding; Oxidoreductase;
KW Reference proteome; Vitamin C.
FT CHAIN 1..315
FT /note="1-aminocyclopropane-1-carboxylate oxidase 1"
FT /id="PRO_0000067261"
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 315 AA; 35813 MW; 053E975EC8B5B2E9 CRC64;
MENFPIINLE KLNGDERANT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KMTKGHYKKC
MEQRFKELVA SKGLEAVQAE VTDLDWESTF FLRHLPTSNI SQVPDLDEEY REVMRDFAKR
LEKLAEELLD LLCENLGLEK GYLKNAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVSGLQLLKD EQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVLHRVIAQT
DGTRMSLASF YNPGSDAVIY PAKTLVEKEA EESTQVYPKF VFDDYMKLYA GLKFQAKEPR
FEAMKAMESD PIASA
