ACCO2_ARATH
ID ACCO2_ARATH Reviewed; 320 AA.
AC Q41931; O81093; Q7DLM8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 2;
DE Short=ACC oxidase 2;
DE Short=AtACO2;
DE EC=1.14.17.4;
GN Name=ACO2; Synonyms=EI305; OrderedLocusNames=At1g62380; ORFNames=F24O1.10;
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 [MRNA], TISSUE SPECIFICITY, AND INDUCTION BY ETHYLENE.
RC STRAIN=cv. Columbia;
RX PubMed=10409511; DOI=10.1242/dev.126.16.3661;
RA Raz V., Ecker J.R.;
RT "Regulation of differential growth in the apical hook of Arabidopsis.";
RL Development 126:3661-3668(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 230-320.
RC STRAIN=cv. Columbia; TISSUE=Green siliques;
RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.;
RT "The Arabidopsis thaliana transcribed genome: the GDR cDNA program.";
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP TISSUE SPECIFICITY.
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 [8]
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 [9]
RP INDUCTION BY OZONE.
RC STRAIN=cv. Columbia;
RX PubMed=15728341; DOI=10.1104/pp.104.055681;
RA Overmyer K., Brosche M., Pellinen R., Kuittinen T., Tuominen H.,
RA Ahlfors R., Keinaenen M., Saarma M., Scheel D., Kangasjaervi J.;
RT "Ozone-induced programmed cell death in the Arabidopsis radical-induced
RT cell death1 mutant.";
RL Plant Physiol. 137:1092-1104(2005).
RN [10]
RP INDUCTION BY ETHYLENE.
RC STRAIN=cv. Columbia;
RX PubMed=16920797; DOI=10.1073/pnas.0605528103;
RA Olmedo G., Guo H., Gregory B.D., Nourizadeh S.D., Aguilar-Henonin L.,
RA Li H., An F., Guzman P., Ecker J.R.;
RT "ETHYLENE-INSENSITIVE5 encodes a 5'-->3' exoribonuclease required for
RT regulation of the EIN3-targeting F-box proteins EBF1/2.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:13286-13293(2006).
RN [11]
RP FUNCTION, INDUCTION BY VERY-LONG-CHAIN FATTY ACIDS, AND TISSUE SPECIFICITY.
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 [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20023197; DOI=10.1105/tpc.109.070201;
RA Linkies A., Mueller K., Morris K., Tureckova V., Wenk M., Cadman C.S.C.,
RA Corbineau F., Strnad M., Lynn J.R., Finch-Savage W.E., Leubner-Metzger G.;
RT "Ethylene interacts with abscisic acid to regulate endosperm rupture during
RT germination: a comparative approach using Lepidium sativum and Arabidopsis
RT thaliana.";
RL Plant Cell 21:3803-3822(2009).
RN [13]
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 [14]
RP COFACTOR.
RX PubMed=20018591; DOI=10.1104/pp.109.147942;
RA Tan Y.-F., O'Toole N., Taylor N.L., Millar A.H.;
RT "Divalent metal ions in plant mitochondria and their role in interactions
RT with proteins and oxidative stress-induced damage to respiratory
RT function.";
RL Plant Physiol. 152:747-761(2010).
RN [15]
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. Required to
CC mediate the 1-aminocyclopropane-1-carboxylic acid (ACC)-mediated
CC reversion of the ABA-induced inhibition of seed germination via
CC endosperm rupture. May promote stem elongation by maximizing the
CC extensibility cells, possibly by activating ethylene biosynthesis, in
CC response to very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
CC {ECO:0000269|PubMed:17993622, ECO:0000269|PubMed:20023197}.
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 ECO:0000269|PubMed:20018591};
CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00805,
CC ECO:0000269|PubMed:20018591};
CC Note=Binds 1 Fe(2+) ion per subunit. Can also bind Cu(2+) ions.
CC {ECO:0000255|PROSITE-ProRule:PRU00805, ECO:0000269|PubMed:20018591};
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 2/2.
CC -!- TISSUE SPECIFICITY: Expressed in vegetative tissues. Constitutively
CC expressed in leaves and blades. In ethylene exposed etiolated
CC seedlings, localized in cells at the outer side of the exaggerated hook
CC in an ethylene-dependent manner and following an ethylene sensitive
CC pattern. Also detected in the root tip when treated by ethylene.
CC {ECO:0000269|PubMed:10409511, ECO:0000269|PubMed:12972669,
CC ECO:0000269|PubMed:17993622}.
CC -!- INDUCTION: Upon iron deprivation. Induced by ethylene, particularly in
CC root tips and hooks of ethiolated seedlings. Promoted by ozone O(3).
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:10409511, ECO:0000269|PubMed:15272873,
CC ECO:0000269|PubMed:15728341, ECO:0000269|PubMed:16920797,
CC ECO:0000269|PubMed:17993622, ECO:0000269|PubMed:20627899,
CC ECO:0000269|PubMed:21316254}.
CC -!- DISRUPTION PHENOTYPE: Impaired in the 1-aminocyclopropane-1-carboxylic
CC acid (ACC)-mediated reversion of the ABA-induced inhibition of seed
CC germination. {ECO:0000269|PubMed:20023197}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AF016100; AAC27484.1; -; mRNA.
DR EMBL; AC003113; AAF70838.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE33960.1; -; Genomic_DNA.
DR EMBL; AY045876; AAK76550.1; -; mRNA.
DR EMBL; AY062685; AAL32763.1; -; mRNA.
DR EMBL; AY093381; AAM13380.1; -; mRNA.
DR EMBL; AY133851; AAM91785.1; -; mRNA.
DR EMBL; AK230351; BAF02150.1; -; mRNA.
DR EMBL; Z17775; CAA79062.1; -; mRNA.
DR PIR; T01448; T01448.
DR PIR; T52267; T52267.
DR RefSeq; NP_176428.1; NM_104918.5.
DR PDB; 5GJ9; X-ray; 2.10 A; A/B=1-303.
DR PDB; 5GJA; X-ray; 2.10 A; A/B/C/D/E/F/G/H=1-303.
DR PDBsum; 5GJ9; -.
DR PDBsum; 5GJA; -.
DR AlphaFoldDB; Q41931; -.
DR SMR; Q41931; -.
DR BioGRID; 27757; 2.
DR IntAct; Q41931; 1.
DR STRING; 3702.AT1G62380.1; -.
DR iPTMnet; Q41931; -.
DR MetOSite; Q41931; -.
DR SwissPalm; Q41931; -.
DR PaxDb; Q41931; -.
DR PRIDE; Q41931; -.
DR ProteomicsDB; 244377; -.
DR EnsemblPlants; AT1G62380.1; AT1G62380.1; AT1G62380.
DR GeneID; 842536; -.
DR Gramene; AT1G62380.1; AT1G62380.1; AT1G62380.
DR KEGG; ath:AT1G62380; -.
DR Araport; AT1G62380; -.
DR TAIR; locus:2027099; AT1G62380.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR OMA; CPGPEMI; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; Q41931; -.
DR UniPathway; UPA00384; UER00563.
DR PRO; PR:Q41931; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q41931; baseline and differential.
DR Genevisible; Q41931; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:TAIR.
DR GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS:TAIR.
DR GO; GO:0005507; F:copper ion binding; HDA:TAIR.
DR GO; GO:0051213; F:dioxygenase activity; IBA:GO_Central.
DR GO; GO:0031418; F:L-ascorbic acid 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:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009727; P:detection of ethylene stimulus; IDA:TAIR.
DR GO; GO:0009693; P:ethylene biosynthetic process; TAS:TAIR.
DR GO; GO:0010030; P:positive regulation of seed germination; IMP:UniProtKB.
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; Coiled coil; Copper; Ethylene biosynthesis; Iron;
KW Metal-binding; Oxidoreductase; Plant defense; Reference proteome;
KW Vitamin C.
FT CHAIN 1..320
FT /note="1-aminocyclopropane-1-carboxylate oxidase 2"
FT /id="PRO_0000408298"
FT DOMAIN 156..256
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 111..143
FT /evidence="ECO:0000255"
FT BINDING 180
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 182
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 237
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT BINDING 247
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT CONFLICT 261
FT /note="E -> D (in Ref. 1; AAC27484)"
FT /evidence="ECO:0000305"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 12..15
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 20..33
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 46..62
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 64..74
FT /evidence="ECO:0007829|PDB:5GJ9"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5GJA"
FT STRAND 91..100
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 111..139
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:5GJ9"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 157..165
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 205..208
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 216..220
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 222..227
FT /evidence="ECO:0007829|PDB:5GJ9"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 237..239
FT /evidence="ECO:0007829|PDB:5GJ9"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 280..290
FT /evidence="ECO:0007829|PDB:5GJ9"
FT HELIX 296..301
FT /evidence="ECO:0007829|PDB:5GJ9"
SQ SEQUENCE 320 AA; 36183 MW; E9B22DF21FDE35A4 CRC64;
MEKNMKFPVV DLSKLNGEER DQTMALINEA CENWGFFEIV NHGLPHDLMD KIEKMTKDHY
KTCQEQKFND MLKSKGLDNL ETEVEDVDWE STFYVRHLPQ SNLNDISDVS DEYRTAMKDF
GKRLENLAED LLDLLCENLG LEKGYLKKVF HGTKGPTFGT KVSNYPPCPK PEMIKGLRAH
TDAGGIILLF QDDKVSGLQL LKDGDWIDVP PLNHSIVINL GDQLEVITNG KYKSVLHRVV
TQQEGNRMSV ASFYNPGSDA EISPATSLVE KDSEYPSFVF DDYMKLYAGV KFQPKEPRFA
AMKNASAVTE LNPTAAVETF
