ACCO4_ARATH
ID ACCO4_ARATH Reviewed; 323 AA.
AC Q06588; Q94K94; Q9S9K8;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 27-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=1-aminocyclopropane-1-carboxylate oxidase 4;
DE Short=ACC oxidase;
DE EC=1.14.17.4;
DE AltName: Full=Ethylene-forming enzyme;
DE Short=EFE;
GN Name=ACO4; Synonyms=ACO1, EAT1; OrderedLocusNames=At1g05010;
GN ORFNames=T7A14.12;
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 [MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=8262380; DOI=10.1016/0378-1119(93)90096-l;
RA Gomez-Lim M.A., Valdez-Lopez V.M., Cruz-Hernandez A., Saucedo-Arias L.J.;
RT "Isolation and characterization of a gene involved in ethylene biosynthesis
RT from Arabidopsis thaliana.";
RL Gene 134:217-221(1993).
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 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 [6]
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 [7]
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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
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 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 -!- TISSUE SPECIFICITY: Expressed in vegetative tissues. Expressed
CC constitutively at a low level in leaves and blades.
CC {ECO:0000269|PubMed:12972669, ECO:0000269|PubMed:17993622}.
CC -!- INDUCTION: Strongly induced by wounding, ethrel, iron, ethylene and 1-
CC amino-cyclopropane-carboxylic acid (ACC). Accumulates in response to
CC very-long-chain fatty acids (VLCFAs C20:0 to C30:0).
CC {ECO:0000269|PubMed:15272873, ECO:0000269|PubMed:17993622}.
CC -!- SIMILARITY: Belongs to the iron/ascorbate-dependent oxidoreductase
CC family. {ECO:0000305}.
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DR EMBL; X66719; CAA47251.1; -; mRNA.
DR EMBL; AC005322; AAC97998.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27779.1; -; Genomic_DNA.
DR EMBL; AF370155; AAK43970.1; -; mRNA.
DR EMBL; AY150384; AAN12929.1; -; mRNA.
DR PIR; A86184; A86184.
DR PIR; JT0755; JT0755.
DR RefSeq; NP_171994.1; NM_100380.4.
DR AlphaFoldDB; Q06588; -.
DR SMR; Q06588; -.
DR BioGRID; 24580; 1.
DR STRING; 3702.AT1G05010.1; -.
DR iPTMnet; Q06588; -.
DR MetOSite; Q06588; -.
DR PaxDb; Q06588; -.
DR PRIDE; Q06588; -.
DR ProteomicsDB; 244642; -.
DR EnsemblPlants; AT1G05010.1; AT1G05010.1; AT1G05010.
DR GeneID; 839345; -.
DR Gramene; AT1G05010.1; AT1G05010.1; AT1G05010.
DR KEGG; ath:AT1G05010; -.
DR Araport; AT1G05010; -.
DR TAIR; locus:2205568; AT1G05010.
DR eggNOG; KOG0143; Eukaryota.
DR HOGENOM; CLU_010119_16_1_1; -.
DR InParanoid; Q06588; -.
DR OMA; QLHDACE; -.
DR OrthoDB; 755371at2759; -.
DR PhylomeDB; Q06588; -.
DR UniPathway; UPA00384; UER00563.
DR PRO; PR:Q06588; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q06588; baseline and differential.
DR Genevisible; Q06588; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005576; C:extracellular region; HDA:TAIR.
DR GO; GO:0009815; F:1-aminocyclopropane-1-carboxylate oxidase activity; ISS: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; ISS:TAIR.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR GO; GO:0009620; P:response to fungus; IEP: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 Acetylation; Ethylene biosynthesis; Fruit ripening; Iron; Metal-binding;
KW Oxidoreductase; Plant defense; Reference proteome; Vitamin C.
FT CHAIN 1..323
FT /note="1-aminocyclopropane-1-carboxylate oxidase 4"
FT /id="PRO_0000067252"
FT DOMAIN 153..254
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"
FT BINDING 245
FT /ligand="2-oxoglutarate"
FT /ligand_id="ChEBI:CHEBI:16810"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00805"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CONFLICT 263
FT /note="A -> V (in Ref. 1; CAA47251)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="Y -> C (in Ref. 4; AAK43970)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 323 AA; 36677 MW; FC4B8DA190FA285C CRC64;
MESFPIINLE KLNGEERAIT MEKIKDACEN WGFFECVNHG ISLELLDKVE KMTKEHYKKC
MEERFKESIK NRGLDSLRSE VNDVDWESTF YLKHLPVSNI SDVPDLDDDY RTLMKDFAGK
IEKLSEELLD LLCENLGLEK GYLKKVFYGS KRPTFGTKVS NYPPCPNPDL VKGLRAHTDA
GGIILLFQDD KVSGLQLLKD GEWVDVPPVK HSIVVNLGDQ LEVITNGKYK SVEHRVLSQT
DGEGRMSIAS FYNPGSDSVI FPAPELIGKE AEKEKKENYP RFVFEDYMKL YSAVKFQAKE
PRFEAMKAME TTVANNVGPL ATA
