ACCO3_PETHY
ID ACCO3_PETHY Reviewed; 320 AA.
AC Q08507;
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 3;
DE Short=ACC oxidase 3;
DE EC=1.14.17.4;
DE AltName: Full=Ethylene-forming enzyme;
DE Short=EFE;
GN Name=ACO3;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L21978; AAA33697.1; -; Genomic_DNA.
DR PIR; S42561; S42561.
DR AlphaFoldDB; Q08507; -.
DR SMR; Q08507; -.
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..320
FT /note="1-aminocyclopropane-1-carboxylate oxidase 3"
FT /id="PRO_0000067272"
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 320 AA; 36274 MW; 7ED735D6D721EEE0 CRC64;
MENFPIINLE KLNGSERDAT MEMIKDACEN WGFFELVNHG IPHEVMDTVE KLTKGHYKKC
MEQRFKELVA SKGLEAVQAE VTDLDWESTF FLRHLPVSNI SEVPDLDDEY REVMRDFAKR
LEKLAEELLD LLCENLGLEK GYLKKAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVSGLQLLKD GQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVLHRVIAQT
DGTRMSLASF YNPGSDAVIY PAPTLVEKEA DQECKQVYPK FVFDDYMKLY AGLKFQAKEP
RFEAMKAREA DVKSDPIATA