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ACCO_DIOKA
ID   ACCO_DIOKA              Reviewed;         318 AA.
AC   Q8S932;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=DK-ACO1;
OS   Diospyros kaki (Kaki persimmon) (Diospyros chinensis).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; Ericales; Ebenaceae; Diospyros.
OX   NCBI_TaxID=35925;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Hiratanenashi;
RX   PubMed=12529535; DOI=10.1104/pp.010462;
RA   Nakano R., Ogura E., Kubo Y., Inaba A.;
RT   "Ethylene biosynthesis in detached young persimmon fruit is initiated in
RT   calyx and modulated by water loss from the fruit.";
RL   Plant Physiol. 131:276-286(2003).
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; Evidence={ECO:0000250};
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC       methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC   -!- INDUCTION: By water stress.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; AB073008; BAB89351.1; -; mRNA.
DR   AlphaFoldDB; Q8S932; -.
DR   SMR; Q8S932; -.
DR   PRIDE; Q8S932; -.
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:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
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   Stress response; Vitamin C.
FT   CHAIN           1..318
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase"
FT                   /id="PRO_0000067258"
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   318 AA;  36038 MW;  2821982E16529D75 CRC64;
     MESFPVINME KMNGEERAAT MGLINDACEN WGFFELVNHG IPPELMDTVE RVTKAHYKKC
     MEQRFKELVA SKALEGIQAE VTDMDWESTY FLRHLPQSNI SEVPDLDEEY RRVMKDFAER
     LEKLAEYLLD LLCENLGLEK GYLKKAFYGT KGPNFGTKVA NYPPCPKADL IKGLRAHTDA
     GGIILLFQDD KVSGLQLLKD DQWIDVPPMK HSIVINLGDQ LEVITNGKYK SVLHRVVAQT
     DGTRMSIASF YNPGNDAVIY PAPALVEKEV EEKEVYPKFV FDDYMKLYAA LKFQAKEPRF
     EAMKAVEANV NLGPIATV
 
 
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