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ACCO4_PETHY
ID   ACCO4_PETHY             Reviewed;         319 AA.
AC   Q08508;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   03-AUG-2022, entry version 85.
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;
GN   Name=ACO4;
OS   Petunia hybrida (Petunia).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Petunioideae; Petunia.
OX   NCBI_TaxID=4102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8292780; DOI=10.1007/bf00042349;
RA   Tang X., Wang H., Brandt A.S., Woodson W.R.;
RT   "Organization and structure of the 1-aminocyclopropane-1-carboxylate
RT   oxidase gene family from Petunia hybrida.";
RL   Plant Mol. Biol. 23:1151-1164(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   -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC       family. {ECO:0000305}.
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DR   EMBL; L21979; AAA33698.1; -; Genomic_DNA.
DR   PIR; S42562; S42562.
DR   AlphaFoldDB; Q08508; -.
DR   SMR; Q08508; -.
DR   UniPathway; UPA00384; UER00563.
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: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: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   3: Inferred from homology;
KW   Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase; Vitamin C.
FT   CHAIN           1..319
FT                   /note="1-aminocyclopropane-1-carboxylate oxidase 4"
FT                   /id="PRO_0000067273"
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   319 AA;  36346 MW;  99E18DA297EE7EE2 CRC64;
     MENFPIINLE NLCGAERDAT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KFTKGHYKKC
     MEQRFKELVA SKGLEAVQAE VTDLDWESTF FLRHLPVSNI SEVPDLDDEY REVMRDFAKR
     LEKLAEELLD LLCENLGLEK GYLKKAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
     GGIILLFQDD KVSGLQLLKD DQWIDVPPMR HSIVINLGDQ LEVITNGKYK SVPHRVIAQT
     DGTRMSLASF YNPASDAVIY PAPALVERDA EENKQIYPKF VFDDYMKLYA RLKFQAKEPR
     FEAMKAMEAD VKIDPVATV
 
 
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