ACCO4_SOLLC
ID ACCO4_SOLLC Reviewed; 316 AA.
AC P24157;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 4;
DE Short=ACC oxidase 4;
DE EC=1.14.17.4;
DE AltName: Full=Ethylene-forming enzyme;
DE Short=EFE;
DE AltName: Full=Protein pHTOM5;
GN Name=ACO4; Synonyms=ACO3;
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.
RX PubMed=2065651; DOI=10.1002/j.1460-2075.1991.tb07730.x;
RA Spanu P., Reinhardt D., Boller T.;
RT "Analysis and cloning of the ethylene-forming enzyme from tomato by
RT functional expression of its mRNA in Xenopus laevis oocytes.";
RL EMBO J. 10:2007-2013(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Ailsa Craig;
RX PubMed=8624515; DOI=10.1046/j.1365-313x.1996.09040525.x;
RA Barry C.S., Blume B., Bouzayen M., Cooper W., Hamilton A.J., Grierson D.;
RT "Differential expression of the 1-aminocyclopropane-1-carboxylate oxidase
RT gene family of tomato.";
RL Plant J. 9:525-535(1996).
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: Expressed in all of the floral organs examined
CC apart from the sepals.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; X58885; CAA41689.1; -; mRNA.
DR EMBL; Z54199; CAA90904.1; -; Genomic_DNA.
DR PIR; S16327; S16327.
DR RefSeq; NP_001233928.1; NM_001246999.1.
DR AlphaFoldDB; P24157; -.
DR SMR; P24157; -.
DR STRING; 4081.Solyc07g049550.2.1; -.
DR PaxDb; P24157; -.
DR PRIDE; P24157; -.
DR EnsemblPlants; Solyc07g049550.3.1; Solyc07g049550.3.1; Solyc07g049550.3.
DR GeneID; 544285; -.
DR Gramene; Solyc07g049550.3.1; Solyc07g049550.3.1; Solyc07g049550.3.
DR KEGG; sly:544285; -.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR InParanoid; P24157; -.
DR OMA; AKTMEMI; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; P24157; -.
DR BioCyc; MetaCyc:MON-15536; -.
DR BRENDA; 1.14.17.4; 3101.
DR UniPathway; UPA00384; UER00563.
DR Proteomes; UP000004994; Chromosome 7.
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..316
FT /note="1-aminocyclopropane-1-carboxylate oxidase 4"
FT /id="PRO_0000067263"
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; 35974 MW; DE1C708950339AE7 CRC64;
MENFPIINLE NLNGDERAKT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KLTKGHYKKC
MEQRFKELVA SKGLEAVQAE VTDLDWESTF FLRHLPTSNI SQVPDLDEEY REVMRDFAKR
LEKLAEELLD LLCENLGLEK GYLKNAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVSGLQLLKD EQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVMHRVIAQT
DGTRMSLASF YNPGNDAVIY PAPSLIEESK QVYPKFVFDD YMKLYAGLKF QPKEPRFEAM
KAMEANVELV DQIASA
