ACCO1_PETHY
ID ACCO1_PETHY Reviewed; 319 AA.
AC Q08506;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 1;
DE Short=ACC oxidase 1;
DE Short=ACCO;
DE EC=1.14.17.4;
DE AltName: Full=Ethylene-forming enzyme;
DE Short=EFE;
GN Name=ACO1;
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.
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).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND COFACTOR.
RX PubMed=15489165; DOI=10.1016/j.chembiol.2004.08.012;
RA Zhang Z., Ren J.-S., Clifton I.J., Schofield C.J.;
RT "Crystal structure and mechanistic implications of 1-aminocyclopropane-1-
RT carboxylic acid oxidase -- the ethylene-forming enzyme.";
RL Chem. Biol. 11:1383-1394(2004).
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 Evidence={ECO:0000269|PubMed:15489165};
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; L21976; AAC37381.1; -; Unassigned_DNA.
DR PIR; S42560; S42560.
DR PDB; 1W9Y; X-ray; 2.10 A; A=1-319.
DR PDB; 1WA6; X-ray; 2.55 A; X=1-319.
DR PDB; 5TCV; X-ray; 2.60 A; A=1-319.
DR PDB; 5TCW; X-ray; 2.70 A; A=1-319.
DR PDBsum; 1W9Y; -.
DR PDBsum; 1WA6; -.
DR PDBsum; 5TCV; -.
DR PDBsum; 5TCW; -.
DR AlphaFoldDB; Q08506; -.
DR SMR; Q08506; -.
DR UniPathway; UPA00384; UER00563.
DR EvolutionaryTrace; Q08506; -.
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 1: Evidence at protein level;
KW 3D-structure; Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Vitamin C.
FT CHAIN 1..319
FT /note="1-aminocyclopropane-1-carboxylate oxidase 1"
FT /id="PRO_0000067271"
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 BINDING 179
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT BINDING 234
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 9..13
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 43..74
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 88..96
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:5TCW"
FT HELIX 108..136
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 142..148
FT /evidence="ECO:0007829|PDB:1W9Y"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 168..171
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 180..191
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 195..199
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 219..224
FT /evidence="ECO:0007829|PDB:1W9Y"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 234..236
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 240..242
FT /evidence="ECO:0007829|PDB:1W9Y"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 282..287
FT /evidence="ECO:0007829|PDB:1W9Y"
FT TURN 288..293
FT /evidence="ECO:0007829|PDB:1W9Y"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:1W9Y"
SQ SEQUENCE 319 AA; 36187 MW; B17768B2B5E0CE82 CRC64;
MENFPIISLD KVNGVERAAT MEMIKDACEN WGFFELVNHG IPREVMDTVE KMTKGHYKKC
MEQRFKELVA SKALEGVQAE VTDMDWESTF FLKHLPISNI SEVPDLDEEY REVMRDFAKR
LEKLAEELLD LLCENLGLEK GYLKNAFYGS KGPNFGTKVS NYPPCPKPDL IKGLRAHTDA
GGIILLFQDD KVSGLQLLKD GQWIDVPPMR HSIVVNLGDQ LEVITNGKYK SVMHRVIAQK
DGARMSLASF YNPGSDAVIY PAPALVEKEA EENKQVYPKF VFDDYMKLYA GLKFQAKEPR
FEAMKAMETD VKMDPIATV
