1A111_ARATH
ID 1A111_ARATH Reviewed; 460 AA.
AC Q9S9U6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 11;
DE Short=ACC synthase 11;
DE EC=4.4.1.14;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 11;
GN Name=ACS11; OrderedLocusNames=At4g08040; ORFNames=T17A2.2;
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=25 uM for AdoMet;
CC Vmax=25.20 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 with GRF3. {ECO:0000250,
CC ECO:0000269|PubMed:25122152}.
CC -!- TISSUE SPECIFICITY: Expressed in roots. {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; AF160183; AAD48074.1; -; Genomic_DNA.
DR EMBL; AL161509; CAB81141.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE82593.1; -; Genomic_DNA.
DR EMBL; AF332405; AAG48768.1; -; mRNA.
DR PIR; B85079; B85079.
DR RefSeq; NP_567330.1; NM_116873.2.
DR AlphaFoldDB; Q9S9U6; -.
DR SMR; Q9S9U6; -.
DR BioGRID; 11617; 1.
DR IntAct; Q9S9U6; 1.
DR STRING; 3702.AT4G08040.1; -.
DR PaxDb; Q9S9U6; -.
DR PRIDE; Q9S9U6; -.
DR EnsemblPlants; AT4G08040.1; AT4G08040.1; AT4G08040.
DR GeneID; 826317; -.
DR Gramene; AT4G08040.1; AT4G08040.1; AT4G08040.
DR KEGG; ath:AT4G08040; -.
DR Araport; AT4G08040; -.
DR TAIR; locus:2134485; AT4G08040.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9S9U6; -.
DR OMA; VWSRIHI; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q9S9U6; -.
DR SABIO-RK; Q9S9U6; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q9S9U6; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9S9U6; baseline and differential.
DR Genevisible; Q9S9U6; 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; IEA:UniProtKB-UniPathway.
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..460
FT /note="1-aminocyclopropane-1-carboxylate synthase 11"
FT /id="PRO_0000123905"
FT BINDING 45
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 267
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 460 AA; 51799 MW; 1A056347680E7E2F CRC64;
MLSSKVVGDS HGQDSSYFLG WQEYEKNPFH ESFNTSGIVQ MGLAENQLSF DLIEKWLEEH
PEVLGLKKND ESVFRQLALF QDYHGLPAFK DAMAKFMGKI RENKVKFDTN KMVLTAGSTS
ANETLMFCLA NPGDAFLIPA PYYPGFDRDL KWRTGVEIVP IHCVSSNGYK ITEDALEDAY
ERALKHNLNV KGVLITNPSN PLGTSTTREE LDLLLTFTST KKIHMVSDEI YSGTVFDSPE
FTSVLEVAKD KNMGLDGKIH VVYSLSKDLG LPGFRVGLIY SNNEKVVSAA TKMSSFGLIS
SQTQHLLANL LSDERFTTNY LEENKKRLRE RKDRLVSGLK EAGISCLKSN AGLFCWVDLR
HLLKSNTFEA EHSLWTKIVC EVGLNISPGS SCHCDEPGWF RVCFANMSDQ TMEVAMDRVK
GFVDNNNGGK QKRTMWDTRR RSLINKWVSK LSSVTCESER
