1A18_ARATH
ID 1A18_ARATH Reviewed; 469 AA.
AC Q9T065;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 8;
DE Short=ACC synthase 8;
DE EC=4.4.1.14;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 8;
GN Name=ACS8; OrderedLocusNames=At4g37770; ORFNames=T28I19.50;
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=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 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 [5]
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=15 uM for AdoMet;
CC Vmax=143 uM/h/mg enzyme;
CC pH dependence:
CC Optimum pH is 8.2.;
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 Q9T065; Q43309: ACS4; NbExp=2; IntAct=EBI-2357693, EBI-2436015;
CC Q9T065; Q9T065: ACS8; NbExp=2; IntAct=EBI-2357693, EBI-2357693;
CC -!- TISSUE SPECIFICITY: Expressed in roots. Expressed at low level in
CC flowers and siliques. {ECO:0000269|PubMed:12968022}.
CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX).
CC {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; AL035709; CAB38925.1; -; Genomic_DNA.
DR EMBL; AL161592; CAB80442.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86836.1; -; Genomic_DNA.
DR EMBL; AF334712; AAG50090.1; -; mRNA.
DR PIR; T06024; T06024.
DR RefSeq; NP_195491.1; NM_119939.3.
DR AlphaFoldDB; Q9T065; -.
DR SMR; Q9T065; -.
DR BioGRID; 15214; 2.
DR IntAct; Q9T065; 2.
DR STRING; 3702.AT4G37770.1; -.
DR PaxDb; Q9T065; -.
DR PRIDE; Q9T065; -.
DR EnsemblPlants; AT4G37770.1; AT4G37770.1; AT4G37770.
DR GeneID; 829933; -.
DR Gramene; AT4G37770.1; AT4G37770.1; AT4G37770.
DR KEGG; ath:AT4G37770; -.
DR Araport; AT4G37770; -.
DR TAIR; locus:2137579; AT4G37770.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9T065; -.
DR OMA; RRHTQAI; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q9T065; -.
DR SABIO-RK; Q9T065; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q9T065; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T065; baseline and differential.
DR Genevisible; Q9T065; 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:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR GO; GO:0009693; P:ethylene biosynthetic process; TAS:TAIR.
DR GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
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..469
FT /note="1-aminocyclopropane-1-carboxylate synthase 8"
FT /id="PRO_0000123902"
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"
SQ SEQUENCE 469 AA; 53371 MW; 7BB3CE13E87BDDCE CRC64;
MGLLSKKASC NTHGQDSSYF WGWEEYEKNP YDEIKNPDGI IQMGLAENQL SFDLIESWLA
KNPDAANFQR EGQSIFRELA LFQDYHGLPS FKNAMADFMS ENRGNRVSFN PNKLVLTAGA
TPANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIQCKSANG FRITKVALEE
AYEQAQKLNL KVKGVLITNP SNPLGTTTTR TELNHLLDFI SRKKIHLISD EIYSGTVFTN
PGFISVMEVL KDRKLENTDV FDRVHIVYSL SKDLGLPGFR VGVIYSNDDF VVSAATKMSS
FGLISSQTQY LLSALLSDKT FTKNYLEENQ IRLKNRHKKL VSGLEAAGIE CLKSNAGLFC
WVDMRHLLKS NTFEAEIELW KKIVYEVKLN ISPGSSCHCN EPGWFRVCFA NLSEETLKVA
LDRLKRFVDG PSPTRRSQSE HQRLKNLRKM KVSNWVFRLS FHDREPEER
