ACCO1_MALDO
ID ACCO1_MALDO Reviewed; 314 AA.
AC Q00985; O24063;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=PAE12;
DE AltName: Full=Protein AP4;
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Golden Delicious; TISSUE=Fruit;
RX PubMed=1377961; DOI=10.1007/bf00027344;
RA Ross G.S., Knighton M.L., Lay-Yee M.;
RT "An ethylene-related cDNA from ripening apples.";
RL Plant Mol. Biol. 19:231-238(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16668829; DOI=10.1104/pp.98.4.1530;
RA Dong J.G., Olsen D.B., Silverstone A., Yang S.F.;
RT "Sequence of a cDNA coding for a 1-aminocyclopropane-1-carboxylate oxidase
RT homolog from apple fruit.";
RL Plant Physiol. 98:1530-1531(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Golden Delicious;
RA Castiglione S., Malerba M., Pirola B., Bianchetti R., Sala F., Ventura M.,
RA Pancaldi M., Sansavini S.;
RT "Allelic forms of ripening-related ACC oxidase in apple.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Granny Smith;
RX PubMed=9747852; DOI=10.1023/a:1006065926397;
RA Atkinson R.G., Bolitho K.M., Wright M.A., Iturriagagoitia-Bueno T.,
RA Reid S.J., Ross G.S.;
RT "Apple ACC-oxidase and polygalacturonase: ripening-specific gene expression
RT and promoter analysis in transgenic tomato.";
RL Plant Mol. Biol. 38:449-460(1998).
RN [5]
RP CHARACTERIZATION, AND PROTEIN SEQUENCE OF 115-134.
RX PubMed=1409700; DOI=10.1073/pnas.89.20.9789;
RA Dong J.G., Fernandez-Maculet J.C., Yang S.F.;
RT "Purification and characterization of 1-aminocyclopropane-1-carboxylate
RT oxidase from apple fruit.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9789-9793(1992).
RN [6]
RP CHARACTERIZATION, AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=7763615; DOI=10.1007/bf00195676;
RA Dupille E., Rombaldi C., Lelievre J.-M., Cleyet-Marel J.-C., Pech J.-C.,
RA Latche A.;
RT "Purification, properties and partial amino-acid sequence of 1-
RT aminocyclopropane-1-carboxylic acid oxidase from apple fruits.";
RL Planta 190:65-70(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 -!- SUBUNIT: Monomer.
CC -!- DEVELOPMENTAL STAGE: Expressed during fruit ripening.
CC -!- INDUCTION: By ethylene and wounding.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; X61390; CAA43662.1; -; mRNA.
DR EMBL; M81794; AAA33412.1; -; mRNA.
DR EMBL; Y14005; CAA74328.1; -; Genomic_DNA.
DR EMBL; AF030859; AAC36461.1; -; Genomic_DNA.
DR PIR; S22513; S22513.
DR AlphaFoldDB; Q00985; -.
DR SMR; Q00985; -.
DR STRING; 3750.XP_008384117.1; -.
DR BindingDB; Q00985; -.
DR PRIDE; Q00985; -.
DR EnsemblPlants; mRNA:MD10G0280000; mRNA:MD10G0280000; MD10G0280000.
DR Gramene; mRNA:MD10G0280000; mRNA:MD10G0280000; MD10G0280000.
DR BioCyc; MetaCyc:MON-16249; -.
DR BRENDA; 1.14.17.4; 3164.
DR SABIO-RK; Q00985; -.
DR UniPathway; UPA00384; UER00563.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; IEA:UniProtKB-EC.
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:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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 1: Evidence at protein level;
KW Direct protein sequencing; Ethylene biosynthesis; Fruit ripening; Iron;
KW Metal-binding; Oxidoreductase; Vitamin C.
FT CHAIN 1..314
FT /note="1-aminocyclopropane-1-carboxylate oxidase 1"
FT /id="PRO_0000067265"
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 314 AA; 35410 MW; BEADA64C7AD10E1E CRC64;
MATFPVVDLS LVNGEERAAT LEKINDACEN WGFFELVNHG MSTELLDTVE KMTKDHYKKT
MEQRFKEMVA AKGLDDVQSE IHDLDWESTF FLRHLPSSNI SEIPDLEEEY RKTMKEFAVE
LEKLAEKLLD LLCENLGLEK GYLKKVFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHSDA
GGIILLFQDD KVSGLQLLKD GEWVDVPPMH HSIVINLGDQ IEVITNGKYK SVMHRVIAQS
DGTRMSIASF YNPGNDSFIS PAPAVLEKKT EDAPTYPKFV FDDYMKLYSG LKFQAKEPRF
EAMKAKESTP VATA
