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ACCO_PEA
ID   ACCO_PEA                Reviewed;         317 AA.
AC   P31239;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 84.
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   Pisum sativum (Garden pea).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Fabeae; Pisum.
OX   NCBI_TaxID=3888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Alaska; TISSUE=Shoot;
RX   PubMed=8278511; DOI=10.1104/pp.101.2.689;
RA   Peck S.C., Olson D.C., Kende H.;
RT   "A cDNA sequence encoding 1-aminocyclopropane-1-carboxylate oxidase from
RT   pea.";
RL   Plant Physiol. 101:689-690(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   -!- 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; M98357; AAA33644.1; -; mRNA.
DR   PIR; T06544; T06544.
DR   AlphaFoldDB; P31239; -.
DR   SMR; P31239; -.
DR   PRIDE; P31239; -.
DR   EnsemblPlants; Psat1g177520.1; Psat1g177520.1.cds; Psat1g177520.
DR   Gramene; Psat1g177520.1; Psat1g177520.1.cds; Psat1g177520.
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   2: Evidence at transcript level;
KW   Ethylene biosynthesis; Fruit ripening; Iron; Metal-binding; Oxidoreductase;
KW   Vitamin C.
FT   CHAIN           1..317
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase"
FT                   /id="PRO_0000067269"
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   317 AA;  36054 MW;  7F71D09ECF2C2A6F CRC64;
     MENFPIVDMG KLNTEDRKST MELIKDACEN WGFFECVNHG ISIEMMDTVE KLTKEHYKKC
     MEQRFKEMVA TKGLECVQSE IDDLDWESTF FLRHLPVSSI SEIPDLDDDY RKVMKEFALK
     LEELAEELLD LLCENLGLEK GYLKKAFYGS KGPNFGTKVS NYPPCPKPEL IKGLRAHTDA
     GGIILLFQDD KVSGLQLLKD DQWIDVPPMR HSIVINLGDQ LEVITNGKYK SVMHRVIAQT
     DGARMSIASF YNPGDDAVIS PASTLLKENE TSEVYPKFVF DDYMKLYMGL KFQAKEPRFE
     AMMKAMSSVK VGPVVSI
 
 
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