1A15_ARATH
ID 1A15_ARATH Reviewed; 470 AA.
AC Q37001; O49537; Q0WPI2; Q9S9C3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 5;
DE Short=ACC synthase 5;
DE EC=4.4.1.14;
DE AltName: Full=Ethylene-overproduction protein 2;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 5;
GN Name=ACS5; Synonyms=ACC5, ETO2; OrderedLocusNames=At5g65800;
GN ORFNames=F6H11.90, MPA24.15;
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 [GENOMIC DNA / MRNA].
RC STRAIN=cv. Columbia; TISSUE=Seedling;
RX PubMed=9011084; DOI=10.1046/j.1365-313x.1996.10061027.x;
RA Liang X.-W., Shen N.F., Theologis A.;
RT "Li(+)-regulated 1-aminocyclopropane-1-carboxylate synthase gene expression
RT in Arabidopsis thaliana.";
RL Plant J. 10:1027-1036(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9628582; DOI=10.1093/dnares/5.1.41;
RA Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence
RT features of the regions of 1,456,315 bp covered by nineteen physically
RT assigned P1 and TAC clones.";
RL DNA Res. 5:41-54(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [5]
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 [6]
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 [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-81.
RC STRAIN=cv. Columbia;
RX PubMed=1438312; DOI=10.1073/pnas.89.22.11046;
RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.;
RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992).
RN [9]
RP MUTANT ETO2.
RX PubMed=12566591; DOI=10.1105/tpc.006882;
RA Chae H.S., Faure F., Kieber J.J.;
RT "The eto1, eto2, and eto3 mutations and cytokinin treatment increase
RT ethylene biosynthesis in Arabidopsis by increasing the stability of ACS
RT protein.";
RL Plant Cell 15:545-559(2003).
RN [10]
RP ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE PROTEOLYTIC
RP PROCESSING.
RX PubMed=12968022; DOI=10.1074/jbc.m308297200;
RA Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A.,
RA Theologis A.;
RT "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate
RT synthase isozymes encoded by the Arabidopsis gene family.";
RL J. Biol. Chem. 278:49102-49112(2003).
RN [11]
RP DEGRADATION, AND INTERACTION WITH ETO1; EOL1 AND EOL2.
RX PubMed=15118728; DOI=10.1038/nature02516;
RA Wang K.L.-C., Yoshida H., Lurin C., Ecker J.R.;
RT "Regulation of ethylene gas biosynthesis by the Arabidopsis ETO1 protein.";
RL Nature 428:945-950(2004).
RN [12]
RP INTERACTION WITH FEI1 AND FEI2.
RX PubMed=19017745; DOI=10.1105/tpc.108.063354;
RA Xu S.-L., Rahman A., Baskin T.I., Kieber J.J.;
RT "Two leucine-rich repeat receptor kinases mediate signaling, linking cell
RT wall biosynthesis and ACC synthase in Arabidopsis.";
RL Plant Cell 20:3065-3079(2008).
RN [13]
RP INTERACTION WITH ETO1 AND EOL1.
RX PubMed=18808454; DOI=10.1111/j.1365-313x.2008.03693.x;
RA Christians M.J., Gingerich D.J., Hansen M., Binder B.M., Kieber J.J.,
RA Vierstra R.D.;
RT "The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate
RT ethylene biosynthesis in Arabidopsis by controlling type-2 ACC synthase
RT levels.";
RL Plant J. 57:332-345(2009).
RN [14]
RP INTERACTION WITH GRF3.
RX PubMed=25122152; DOI=10.1105/tpc.114.127605;
RA Catala R., Lopez-Cobollo R., Mar Castellano M., Angosto T., Alonso J.M.,
RA Ecker J.R., Salinas J.;
RT "The Arabidopsis 14-3-3 protein RARE COLD INDUCIBLE 1A links low-
RT temperature response and ethylene biosynthesis to regulate freezing
RT tolerance and cold acclimation.";
RL Plant Cell 26:3326-3342(2014).
CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes
CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-
CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate +
CC H(+) + S-methyl-5'-thioadenosine; Xref=Rhea:RHEA:21744,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17509, ChEBI:CHEBI:58360,
CC ChEBI:CHEBI:59789; EC=4.4.1.14;
CC Evidence={ECO:0000269|PubMed:12968022};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for S-adenosyl-L-methionine;
CC Vmax=81.70 uM/h/mg enzyme;
CC pH dependence:
CC Optimum pH is 7.8.;
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of
CC heterodimerization with other ACS enzymes is however unsure (By
CC similarity). Interacts (via its C-terminal region) with FEI1, FEI2,
CC ETO1, EOL1 and EOL2 (PubMed:15118728, PubMed:19017745,
CC PubMed:18808454). Interacts with GRF3 (PubMed:25122152). {ECO:0000250,
CC ECO:0000269|PubMed:15118728, ECO:0000269|PubMed:18808454,
CC ECO:0000269|PubMed:19017745, ECO:0000269|PubMed:25122152}.
CC -!- INTERACTION:
CC Q37001; O65020: ETO1; NbExp=3; IntAct=EBI-593450, EBI-593440;
CC -!- TISSUE SPECIFICITY: Expressed in roots and siliques.
CC {ECO:0000269|PubMed:12968022}.
CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). In
CC response to low dose of cytokinin. {ECO:0000269|PubMed:12968022}.
CC -!- PTM: May be processed at its C-terminus.
CC -!- PTM: Ubiquitinated (Probable). The interaction with ETO1 (and possibly
CC EOL1 and EOL2) mediate its proteasome-dependent degradation. Its
CC stability and degradation plays a central role in ethylene
CC biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L29261; AAA87292.1; -; mRNA.
DR EMBL; L29260; AAA87291.1; -; Genomic_DNA.
DR EMBL; AB010075; BAB10687.1; -; Genomic_DNA.
DR EMBL; AB020743; BAB10687.1; JOINED; Genomic_DNA.
DR EMBL; AL021684; CAA16680.1; -; Genomic_DNA.
DR EMBL; CP002688; AED98109.1; -; Genomic_DNA.
DR EMBL; AF334720; AAG50098.1; -; mRNA.
DR EMBL; AK229087; BAF00967.1; -; mRNA.
DR PIR; S71174; S71174.
DR RefSeq; NP_201381.1; NM_125977.2.
DR AlphaFoldDB; Q37001; -.
DR SMR; Q37001; -.
DR BioGRID; 21951; 8.
DR IntAct; Q37001; 3.
DR STRING; 3702.AT5G65800.1; -.
DR BindingDB; Q37001; -.
DR ChEMBL; CHEMBL2242742; -.
DR iPTMnet; Q37001; -.
DR PaxDb; Q37001; -.
DR PRIDE; Q37001; -.
DR EnsemblPlants; AT5G65800.1; AT5G65800.1; AT5G65800.
DR GeneID; 836709; -.
DR Gramene; AT5G65800.1; AT5G65800.1; AT5G65800.
DR KEGG; ath:AT5G65800; -.
DR Araport; AT5G65800; -.
DR TAIR; locus:2169980; AT5G65800.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q37001; -.
DR OMA; INEISHQ; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q37001; -.
DR BRENDA; 4.4.1.14; 399.
DR SABIO-RK; Q37001; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q37001; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q37001; baseline and differential.
DR Genevisible; Q37001; AT.
DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IDA:TAIR.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IMP:TAIR.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009693; P:ethylene biosynthetic process; IMP:TAIR.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IMP:TAIR.
DR GO; GO:0009735; P:response to cytokinin; IMP:TAIR.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Ethylene biosynthesis; Fruit ripening; Lyase; Phosphoprotein;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW Ubl conjugation.
FT CHAIN 1..470
FT /note="1-aminocyclopropane-1-carboxylate synthase 5"
FT /id="PRO_0000123899"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 461
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9SAR0"
FT MUTAGEN 201
FT /note="S->F: In cin5-3; defective in cytokinin induced
FT ethylene."
FT MUTAGEN 269
FT /note="S->N: In cin5-2; defective in cytokinin induced
FT ethylene."
FT MUTAGEN 459..470
FT /note="RVSWTDRVPDER->PGFMDRSCT: In eto2; increases its
FT stability leading to ethylene overproduction."
SQ SEQUENCE 470 AA; 53313 MW; 8B2527C9B52AE19A CRC64;
MKQLSTKVTS NGHGQDSSYF LGWEEYEKNP YDEIKNPNGM IQMGLAENQL CFDLIESWLT
KNPDAASLKR NGQSIFRELA LFQDYHGMPE FKKAMAEFME EIRGNRVTFD PKKIVLAAGS
TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ
AYQQAQKLDL KVKGVLVTNP SNPLGTALTR RELNLLVDFI TSKNIHLISD EIYSGTMFGF
EQFISVMDVL KDKKLEDTEV SKRVHVVYSL SKDLGLPGFR VGAIYSNDEM IVSAATKMSS
FGLVSSQTQY LLSALLSDKK FTSQYLEENQ KRLKSRQRRL VSGLESAGIT CLRSNAGLFC
WVDMRHLLDT NTFEAELDLW KKIVYNVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA
LKRLKTFVES TDCGRMISRS SHERLKSLRK KTVSNWVFRV SWTDRVPDER
