1A19_ARATH
ID 1A19_ARATH Reviewed; 470 AA.
AC Q9M2Y8;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 9;
DE Short=ACC synthase 9;
DE EC=4.4.1.14;
DE AltName: Full=Ethylene-overproduction protein 3;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 9;
GN Name=ACS9; Synonyms=ETO3; OrderedLocusNames=At3g49700; ORFNames=T16K5.50;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(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 MUTANT ETO3.
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 [5]
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 [6]
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 [7]
RP INTERACTION WITH ETO1 AND EOL1, AND MUTAGENESIS OF VAL-457.
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).
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=40 uM for AdoMet;
CC Vmax=324.5 uM/h/mg enzyme;
CC pH dependence:
CC Optimum pH is 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 and EOL1. {ECO:0000250, ECO:0000269|PubMed:18808454,
CC ECO:0000269|PubMed:19017745}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and siliques.
CC {ECO:0000269|PubMed:12968022}.
CC -!- INDUCTION: By cycloheximide (CHX). {ECO:0000269|PubMed:12968022}.
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.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AL132965; CAB66908.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE78578.1; -; Genomic_DNA.
DR EMBL; AF332391; AAG48755.1; -; mRNA.
DR PIR; T46036; T46036.
DR RefSeq; NP_190539.1; NM_114830.2.
DR AlphaFoldDB; Q9M2Y8; -.
DR SMR; Q9M2Y8; -.
DR BioGRID; 9450; 2.
DR STRING; 3702.AT3G49700.1; -.
DR iPTMnet; Q9M2Y8; -.
DR PaxDb; Q9M2Y8; -.
DR PRIDE; Q9M2Y8; -.
DR EnsemblPlants; AT3G49700.1; AT3G49700.1; AT3G49700.
DR GeneID; 824132; -.
DR Gramene; AT3G49700.1; AT3G49700.1; AT3G49700.
DR KEGG; ath:AT3G49700; -.
DR Araport; AT3G49700; -.
DR TAIR; locus:2097350; AT3G49700.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9M2Y8; -.
DR OMA; CSITQAN; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q9M2Y8; -.
DR SABIO-RK; Q9M2Y8; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q9M2Y8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9M2Y8; baseline and differential.
DR Genevisible; Q9M2Y8; 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: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:0006417; P:regulation of translation; IDA: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; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..470
FT /note="1-aminocyclopropane-1-carboxylate synthase 9"
FT /id="PRO_0000123903"
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 MUTAGEN 457
FT /note="V->D: In eto3; increases its stability heading to
FT ethylene overproduction. Impairs the binding to ETO1 and
FT slightly affects the binding to EOL1."
FT /evidence="ECO:0000269|PubMed:18808454"
SQ SEQUENCE 470 AA; 53170 MW; 2110331C76ACED4E CRC64;
MKQLSRKVTS NAHGQDSSYF LGWEEYEKNP YDEIKNPNGI IQMGLAENQL CFDLIETWLA
KNPDAAGLKK DGQSIFKELA LFQDYHGLPE FKKALAEFME EIRGNRVTFD PSKIVLAAGS
TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ
AYQQAQKLDL KVKGVLVTNP SNPLGTMLTR RELNLLVDFI TSKNIHLISD EIYSGTVFGF
EQFVSVMDVL KDKNLENSEV SKRVHIVYSL SKDLGLPGFR VGAIYSNDEM VVSAATKMSS
FGLVSSQTQY LLSALLSDKK FTSTYLDENQ KRLKIRQKKL VSGLEAAGIT CLKSNAGLFC
WVDMRHLLDT NTFEAELELW KKIVYDVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA
MKRLKEYVES TDSRRVISKS SHDRIKSLRK RTVSNWVFRV SWTDRVPDER
