ID ACCO2_SOLLC Reviewed; 316 AA.
AC P07920;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 2;
DE Short=ACC oxidase 2;
DE EC=1.14.17.4;
DE AltName: Full=Ethylene-forming enzyme;
DE Short=EFE;
DE AltName: Full=Protein GTOMA;
GN Name=ACO2;
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=3697103; DOI=10.1093/nar/15.24.10600;
RA Holdsworth M.J., Schuch W., Grierson D.;
RT "Nucleotide sequence of an ethylene-related gene from tomato.";
RL Nucleic Acids Res. 15:10600-10600(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: Leaves.
CC -!- INDUCTION: By wounding.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; Y00478; CAA68538.1; -; Genomic_DNA.
DR PIR; S00519; S00519.
DR AlphaFoldDB; P07920; -.
DR SMR; P07920; -.
DR STRING; 4081.P07920; -.
DR PaxDb; 4081-Solyc12g005940-1-1; -.
DR eggNOG; KOG0143; Eukaryota.
DR InParanoid; P07920; -.
DR BRENDA; 1.14.17.4; 3101.
DR UniPathway; UPA00384; UER00563.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P07920; 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; 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 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 PANTHER; PTHR47991:SF215; FE2OG DIOXYGENASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR47991; OXOGLUTARATE/IRON-DEPENDENT DIOXYGENASE; 1.
DR Pfam; PF03171; 2OG-FeII_Oxy; 1.
DR Pfam; PF14226; DIOX_N; 1.
DR SUPFAM; SSF51197; Clavaminate synthase-like; 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..316
FT /note="1-aminocyclopropane-1-carboxylate oxidase 2"
FT /id="PRO_0000067262"
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 316 AA; 36168 MW; 7701CFF1955AABC9 CRC64;
MENFPIINLE KLNGAERVAT MEKINDACEN WGFFELVNHG IPHEVMDTVE KLTKGHYKKC
MEQRFKELVA KKGLEGVEVE VTDMDWESTF FLRHLPSSNI SQLPDLDDVY REVMRDFRKR
LEKLAEELLD LLCENLGLEK SYLKNTFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVSGLQLLKD GRWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVMHRVIAQK
DGTRMSLASF YNPGNDALIY PAPALVDKEA EEHNKQVYPK FMFDDYMKLY ANLKFQAKEP
RFEAMKAMES DPIAIA
//
