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ACCO2_DORSP
ID   ACCO2_DORSP             Reviewed;         325 AA.
AC   Q39705;
DT   25-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 88.
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;
GN   Name=ACO2;
OS   Doritaenopsis sp. (Moth orchid).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Asparagales; Orchidaceae;
OC   Epidendroideae; Vandeae; Aeridinae; x Doritaenopsis;
OC   unclassified x Doritaenopsis.
OX   NCBI_TaxID=4749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RC   STRAIN=cv. Hausermann's red bird 'Cardinal'; TISSUE=Perianth;
RX   PubMed=7610175; DOI=10.1104/pp.108.2.833;
RA   Nadeau J.A., O'Neill S.D.;
RT   "Nucleotide sequence of a cDNA encoding 1-aminocyclopropane-1-carboxylate
RT   oxidase from senescing orchid petals.";
RL   Plant Physiol. 108:833-834(1995).
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 pollination. {ECO:0000269|PubMed:7610175}.
CC   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; L37103; AAA97488.1; -; mRNA.
DR   AlphaFoldDB; Q39705; -.
DR   SMR; Q39705; -.
DR   PRIDE; Q39705; -.
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..325
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 2"
FT                   /id="PRO_0000067260"
FT   DOMAIN          157..257
FT                   /note="Fe2OG dioxygenase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         181
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         183
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT   BINDING         238
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ   SEQUENCE   325 AA;  37131 MW;  9215F6B2B9963D6C CRC64;
     MESGSFPVIN MELLQGSQRP AAMALLRDAC ENWGFFELLN HGISHELMNR VEAVNKEHYR
     RFREQRFKEF ASKTLDSVEN VDPDNLDWES TFFLRHLPTS NISQIPDLDD DCRATMKEFA
     RELEKLAERL LDLLCEDLGL EKGYLKRVFC GGSDGLPTFG TKVSNYPPCP KPDLIKGLRA
     HTDAGGIILL FQDDKVSGLQ LLKDREWIEV PPLRYSIVVN IGDQLEVITN GKYKSVLHRV
     VAQTDGNRMS IASFYNPGSD AVIFPAPALV EKEAEEEEKK EIYPKFVFQD YMNLYIRKKF
     EAKEPRFEAM KSMEIVMSSQ PIPTA
 
 
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