1A16_ARATH
ID 1A16_ARATH Reviewed; 495 AA.
AC Q9SAR0; O82719; Q9SUT3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 6;
DE Short=ACC synthase 6;
DE EC=4.4.1.14;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 6;
GN Name=ACS6; Synonyms=ACC6; OrderedLocusNames=At4g11280; ORFNames=F8L21.70;
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=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(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 NUCLEOTIDE SEQUENCE [MRNA] OF 30-495, AND INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=10080689; DOI=10.1023/a:1006177902093;
RA Arteca J.M., Arteca R.N.;
RT "A multi-responsive gene encoding 1-aminocyclopropane-1-carboxylate
RT synthase (ACS6) in mature Arabidopsis leaves.";
RL Plant Mol. Biol. 39:209-219(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 53-418, AND INDUCTION.
RA Vahala J., Schlagnhaufer C.D., Pell E.J.;
RT "Induction of an ACC synthase cDNA by ozone in light-grown Arabidopsis
RT thaliana leaves.";
RL Physiol. Plantarum 103:45-50(1998).
RN [6]
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 [7]
RP FUNCTION, PHOSPHORYLATION AT SER-480; SER-483 AND SER-488, AND MUTAGENESIS
RP OF SER-480; SER-483 AND SER-488.
RX PubMed=15539472; DOI=10.1105/tpc.104.026609;
RA Liu Y., Zhang S.;
RT "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by MPK6,
RT a stress-responsive mitogen-activated protein kinase, induces ethylene
RT biosynthesis in Arabidopsis.";
RL Plant Cell 16:3386-3399(2004).
RN [8]
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 Involved in bacterial flagellin-induced ethylene production.
CC {ECO:0000269|PubMed:15539472}.
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=23 uM for AdoMet;
CC Vmax=120.60 uM/h/mg enzyme;
CC pH dependence:
CC Optimum pH is 7.3.;
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 with GRF3. {ECO:0000250,
CC ECO:0000269|PubMed:25122152}.
CC -!- INTERACTION:
CC Q9SAR0; Q43309: ACS4; NbExp=2; IntAct=EBI-2356658, EBI-2436015;
CC Q9SAR0; Q9SAR0: ACS6; NbExp=3; IntAct=EBI-2356658, EBI-2356658;
CC -!- TISSUE SPECIFICITY: Expressed in roots and flowers.
CC {ECO:0000269|PubMed:12968022}.
CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). By
CC auxin. By treatment with ozone. {ECO:0000269|PubMed:10080689,
CC ECO:0000269|PubMed:12968022, ECO:0000269|Ref.5}.
CC -!- PTM: Phosphorylated on serine residue by MAP kinase (MPK6).
CC {ECO:0000269|PubMed:15539472}.
CC -!- PTM: May be processed at its C-terminus.
CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation of
CC such stability, play a central role in ethylene biosynthesis. The
CC phosphorylation of serine residues on the C-terminus increases protein
CC stability.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL096882; CAB51412.1; -; Genomic_DNA.
DR EMBL; AL161531; CAB81229.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82992.1; -; Genomic_DNA.
DR EMBL; AF361097; AAK27237.1; -; mRNA.
DR EMBL; AF428292; AAL16124.1; -; mRNA.
DR EMBL; BT000487; AAN18056.1; -; mRNA.
DR EMBL; U73786; AAC63850.1; -; mRNA.
DR EMBL; U79524; AAC32251.1; -; mRNA.
DR PIR; T13019; T13019.
DR RefSeq; NP_192867.1; NM_117199.2.
DR AlphaFoldDB; Q9SAR0; -.
DR SMR; Q9SAR0; -.
DR BioGRID; 12029; 4.
DR IntAct; Q9SAR0; 4.
DR STRING; 3702.AT4G11280.1; -.
DR iPTMnet; Q9SAR0; -.
DR PaxDb; Q9SAR0; -.
DR PRIDE; Q9SAR0; -.
DR EnsemblPlants; AT4G11280.1; AT4G11280.1; AT4G11280.
DR GeneID; 826730; -.
DR Gramene; AT4G11280.1; AT4G11280.1; AT4G11280.
DR KEGG; ath:AT4G11280; -.
DR Araport; AT4G11280; -.
DR TAIR; locus:2128298; AT4G11280.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9SAR0; -.
DR OMA; VLIVNPH; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q9SAR0; -.
DR BRENDA; 4.4.1.14; 399.
DR SABIO-RK; Q9SAR0; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q9SAR0; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9SAR0; baseline and differential.
DR Genevisible; Q9SAR0; AT.
DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IDA:TAIR.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IEP:TAIR.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR GO; GO:0009693; P:ethylene biosynthetic process; TAS:TAIR.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IEP:TAIR.
DR GO; GO:0009733; P:response to auxin; IEP:TAIR.
DR GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR GO; GO:0009612; P:response to mechanical stimulus; IEP:TAIR.
DR GO; GO:0006979; P:response to oxidative stress; IEP:TAIR.
DR GO; GO:0009611; P:response to wounding; IEP: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 Plant defense; Pyridoxal phosphate; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..495
FT /note="1-aminocyclopropane-1-carboxylate synthase 6"
FT /id="PRO_0000123900"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 280
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15539472"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15539472"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15539472"
FT MUTAGEN 480
FT /note="S->D: 40-fold increase in ethylene production; when
FT associated with D-483 and D-488."
FT /evidence="ECO:0000269|PubMed:15539472"
FT MUTAGEN 483
FT /note="S->D: 40-fold increase in ethylene production; when
FT associated with D-480 and D-488."
FT /evidence="ECO:0000269|PubMed:15539472"
FT MUTAGEN 488
FT /note="S->D: 40-fold increase in ethylene production; when
FT associated with D-480 and D-483."
FT /evidence="ECO:0000269|PubMed:15539472"
FT CONFLICT 56
FT /note="L -> F (in Ref. 5; AAC32251)"
FT /evidence="ECO:0000305"
FT CONFLICT 433
FT /note="R -> K (in Ref. 4; AAC63850)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 495 AA; 55524 MW; 7FA94D3EABBCB4AB CRC64;
MVAFATEKKQ DLNLLSKIAS GDGHGENSSY FDGWKAYEEN PFHPIDRPDG VIQMGLAENQ
LCGDLMRKWV LKHPEASICT SEGVNQFSDI AIFQDYHGLP EFRQAVAKFM EKTRNNKVKF
DPDRIVMSGG ATGAHETVAF CLANPGDGFL VPTPYYPGFD RDLRWRTGVN LVPVTCHSSN
GFKITVEALE AAYENARKSN IPVKGLLVTN PSNPLGTTLD RECLKSLVNF TNDKGIHLIA
DEIYAATTFG QSEFISVAEV IEEIEDCNRD LIHIVYSLSK DMGLPGLRVG IVYSYNDRVV
QIARKMSSFG LVSSQTQHLI AKMLSDEEFV DEFIRESKLR LAARHAEITT GLDGLGIGWL
KAKAGLFLWM DLRNLLKTAT FDSETELWRV IVHQVKLNVS PGGSFHCHEP GWFRVCFANM
DHKTMETALE RIRVFTSQLE EETKPMAATT MMAKKKKKCW QSNLRLSFSD TRRFDDGFFS
PHSPVPPSPL VRAQT
