ACCO3_ARATH
ID ACCO3_ARATH Reviewed; 320 AA.
AC O65378;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 3;
DE Short=ACC oxidase 3;
DE Short=AtACO3;
DE EC=1.14.17.4 {ECO:0000305|PubMed:19513806};
GN OrderedLocusNames=At1g12010; ORFNames=F12F1.12;
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=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 [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 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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=cv. Columbia, and cv. Landsberg erecta;
RX PubMed=19513806; DOI=10.1007/s11103-009-9509-7;
RA Cheng W.-H., Chiang M.-H., Hwang S.-G., Lin P.-C.;
RT "Antagonism between abscisic acid and ethylene in Arabidopsis acts in
RT parallel with the reciprocal regulation of their metabolism and signaling
RT pathways.";
RL Plant Mol. Biol. 71:61-80(2009).
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 ECO:0000269|PubMed:19513806}.
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; Evidence={ECO:0000305|PubMed:19513806};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23641;
CC Evidence={ECO:0000305|PubMed:19513806};
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: Accumulates in response to very-long-chain fatty acids
CC (VLCFAs C20:0 to C30:0). {ECO:0000269|PubMed:17993622}.
CC -!- DISRUPTION PHENOTYPE: Reduced ethylene levels.
CC {ECO:0000269|PubMed:19513806}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; AC002131; AAC17613.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE28826.1; -; Genomic_DNA.
DR EMBL; AY052694; AAK96598.1; -; mRNA.
DR EMBL; AF446874; AAL38607.1; -; mRNA.
DR PIR; B86255; B86255.
DR RefSeq; NP_172665.1; NM_101073.3.
DR AlphaFoldDB; O65378; -.
DR SMR; O65378; -.
DR STRING; 3702.AT1G12010.1; -.
DR PaxDb; O65378; -.
DR PRIDE; O65378; -.
DR ProteomicsDB; 244383; -.
DR EnsemblPlants; AT1G12010.1; AT1G12010.1; AT1G12010.
DR GeneID; 837753; -.
DR Gramene; AT1G12010.1; AT1G12010.1; AT1G12010.
DR KEGG; ath:AT1G12010; -.
DR Araport; AT1G12010; -.
DR TAIR; locus:2008905; AT1G12010.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR InParanoid; O65378; -.
DR OMA; HGISHEQ; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; O65378; -.
DR UniPathway; UPA00384; UER00563.
DR PRO; PR:O65378; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; O65378; baseline and differential.
DR Genevisible; O65378; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; IMP: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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0071398; P:cellular response to fatty acid; IEP:UniProtKB.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009693; P:ethylene biosynthetic process; IMP:TAIR.
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 Coiled coil; Ethylene biosynthesis; Iron; Metal-binding; Oxidoreductase;
KW Plant defense; Reference proteome; Vitamin C.
FT CHAIN 1..320
FT /note="1-aminocyclopropane-1-carboxylate oxidase 3"
FT /id="PRO_0000408299"
FT DOMAIN 155..256
FT /note="Fe2OG dioxygenase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT COILED 111..131
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"
SQ SEQUENCE 320 AA; 36532 MW; 97ECE9AB8D69C1C3 CRC64;
MEMNIKFPVI DLSKLNGEER DQTMALIDDA CQNWGFFELV NHGLPYDLMD NIERMTKEHY
KKHMEQKFKE MLRSKGLDTL ETEVEDVDWE STFYLHHLPQ SNLYDIPDMS NEYRLAMKDF
GKRLEILAEE LLDLLCENLG LEKGYLKKVF HGTTGPTFAT KLSNYPPCPK PEMIKGLRAH
TDAGGLILLF QDDKVSGLQL LKDGDWVDVP PLKHSIVINL GDQLEVITNG KYKSVMHRVM
TQKEGNRMSI ASFYNPGSDA EISPATSLVD KDSKYPSFVF DDYMKLYAGL KFQAKEPRFE
AMKNAEAAAD LNPVAVVETF
