ACCO1_ARATH
ID ACCO1_ARATH Reviewed; 310 AA.
AC Q9ZUN4;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 1;
DE Short=ACC oxidase 1;
DE Short=AtACO1;
DE EC=1.14.17.4;
GN Name=ACO1; OrderedLocusNames=At2g19590; ORFNames=F3P11.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP INDUCTION BY LOW LIGHT.
RX PubMed=12972669; DOI=10.1104/pp.103.022665;
RA Vandenbussche F., Vriezen W.H., Smalle J., Laarhoven L.J.J., Harren F.J.M.,
RA Van Der Straeten D.;
RT "Ethylene and auxin control the Arabidopsis response to decreased light
RT intensity.";
RL Plant Physiol. 133:517-527(2003).
RN [5]
RP INDUCTION BY ETHYLENE.
RC STRAIN=cv. Columbia;
RX PubMed=15272873; DOI=10.1111/j.1365-313x.2004.02156.x;
RA De Paepe A., Vuylsteke M., Van Hummelen P., Zabeau M., Van Der Straeten D.;
RT "Transcriptional profiling by cDNA-AFLP and microarray analysis reveals
RT novel insights into the early response to ethylene in Arabidopsis.";
RL Plant J. 39:537-559(2004).
RN [6]
RP INDUCTION BY POTASSIUM DEPRIVATION.
RX PubMed=15173595; DOI=10.1073/pnas.0401707101;
RA Shin R., Schachtman D.P.;
RT "Hydrogen peroxide mediates plant root cell response to nutrient
RT deprivation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8827-8832(2004).
RN [7]
RP INDUCTION BY POTASSIUM DEPRIVATION.
RX PubMed=15734909; DOI=10.1104/pp.104.057216;
RA Gierth M., Maeser P., Schroeder J.I.;
RT "The potassium transporter AtHAK5 functions in K(+) deprivation-induced
RT high-affinity K(+) uptake and AKT1 K(+) channel contribution to K(+) uptake
RT kinetics in Arabidopsis roots.";
RL Plant Physiol. 137:1105-1114(2005).
RN [8]
RP FUNCTION, AND INDUCTION BY VERY-LONG-CHAIN FATTY ACIDS.
RC STRAIN=cv. Columbia;
RX PubMed=17993622; DOI=10.1105/tpc.107.054437;
RA Qin Y.-M., Hu C.-Y., Pang Y., Kastaniotis A.J., Hiltunen J.K., Zhu Y.-X.;
RT "Saturated very-long-chain fatty acids promote cotton fiber and Arabidopsis
RT cell elongation by activating ethylene biosynthesis.";
RL Plant Cell 19:3692-3704(2007).
RN [9]
RP INDUCTION BY IRON DEFICIENCY.
RX PubMed=20627899; DOI=10.1093/jxb/erq203;
RA Garcia M.J., Lucena C., Romera F.J., Alcantara E., Perez-Vicente R.;
RT "Ethylene and nitric oxide involvement in the up-regulation of key genes
RT related to iron acquisition and homeostasis in Arabidopsis.";
RL J. Exp. Bot. 61:3885-3899(2010).
RN [10]
RP INDUCTION BY NITRIC OXIDE.
RX PubMed=21316254; DOI=10.1016/j.plaphy.2011.01.019;
RA Garcia M.J., Suarez V., Romera F.J., Alcantara E., Perez-Vicente R.;
RT "A new model involving ethylene, nitric oxide and Fe to explain the
RT regulation of Fe-acquisition genes in Strategy I plants.";
RL Plant Physiol. Biochem. 49:537-544(2011).
CC -!- FUNCTION: Enzyme involved in the ethylene biosynthesis. May promote
CC stem elongation by maximizing the extensibility cells, possibly by
CC activating ethylene biosynthesis, in response to very-long-chain fatty
CC acids (VLCFAs C20:0 to C30:0). {ECO:0000269|PubMed:17993622}.
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(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU00805};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC -!- INDUCTION: Upon potassium K(+) and iron deprivation. Induced in leaf
CC blades in low light intensities. Seems repressed by ethylene.
CC Accumulates in response to very-long-chain fatty acids (VLCFAs C20:0 to
CC C30:0). Induced in roots by nitric oxide (NO).
CC {ECO:0000269|PubMed:12972669, ECO:0000269|PubMed:15173595,
CC ECO:0000269|PubMed:15272873, ECO:0000269|PubMed:15734909,
CC ECO:0000269|PubMed:17993622, ECO:0000269|PubMed:20627899,
CC ECO:0000269|PubMed:21316254}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC005917; AAD10157.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC06898.1; -; Genomic_DNA.
DR EMBL; AF370195; AAK44010.1; -; mRNA.
DR EMBL; AY062951; AAL33783.1; -; mRNA.
DR PIR; F84578; F84578.
DR RefSeq; NP_179549.1; NM_127517.5.
DR AlphaFoldDB; Q9ZUN4; -.
DR SMR; Q9ZUN4; -.
DR BioGRID; 1833; 1.
DR STRING; 3702.AT2G19590.1; -.
DR iPTMnet; Q9ZUN4; -.
DR PaxDb; Q9ZUN4; -.
DR PRIDE; Q9ZUN4; -.
DR ProteomicsDB; 243279; -.
DR EnsemblPlants; AT2G19590.1; AT2G19590.1; AT2G19590.
DR GeneID; 816478; -.
DR Gramene; AT2G19590.1; AT2G19590.1; AT2G19590.
DR KEGG; ath:AT2G19590; -.
DR Araport; AT2G19590; -.
DR TAIR; locus:2050364; AT2G19590.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR OMA; YRHQPKS; -.
DR OrthoDB; 622449at2759; -.
DR PhylomeDB; Q9ZUN4; -.
DR UniPathway; UPA00384; UER00563.
DR PRO; PR:Q9ZUN4; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q9ZUN4; baseline and differential.
DR Genevisible; Q9ZUN4; AT.
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:0071398; P:cellular response to fatty acid; IEP:UniProtKB.
DR GO; GO:0071732; P:cellular response to nitric oxide; IEP:UniProtKB.
DR GO; GO:0051365; P:cellular response to potassium ion starvation; IEP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
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 Coiled coil; Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Plant defense; Reference proteome; Vitamin C.
FT CHAIN 1..310
FT /note="1-aminocyclopropane-1-carboxylate oxidase 1"
FT /id="PRO_0000408297"
FT DOMAIN 158..259
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 113..133
FT /evidence="ECO:0000255"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 184
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 240
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 250
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
SQ SEQUENCE 310 AA; 35202 MW; 8CA84DFBEC4E1647 CRC64;
MVLIKEREME IPVIDFAELD GEKRSKTMSL LDHACDKWGF FMVDNHGIDK ELMEKVKKMI
NSHYEEHLKE KFYQSEMVKA LSEGKTSDAD WESSFFISHK PTSNICQIPN ISEELSKTMD
EYVCQLHKFA ERLSKLMCEN LGLDQEDIMN AFSGPKGPAF GTKVAKYPEC PRPELMRGLR
EHTDAGGIIL LLQDDQVPGL EFFKDGKWVP IPPSKNNTIF VNTGDQLEIL SNGRYKSVVH
RVMTVKHGSR LSIATFYNPA GDAIISPAPK LLYPSGYRFQ DYLKLYSTTK FGDKGPRLET
MKKMGNADSA
