(data stored in SCRATCH zone)

SWISSPROT: 1A17_ARATH

ID   1A17_ARATH              Reviewed;         447 AA.
AC   Q9STR4;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 127.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 7;
DE            Short=ACC synthase 7;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 7;
GN   Name=ACS7; OrderedLocusNames=At4g26200; ORFNames=T25K17.10;
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, AND INDUCTION.
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 XBAT32, AND UBIQUITINATION.
RX   PubMed=20511490; DOI=10.1104/pp.110.156976;
RA   Prasad M.E., Schofield A., Lyzenga W., Liu H., Stone S.L.;
RT   "Arabidopsis RING E3 ligase XBAT32 regulates lateral root production
RT   through its role in ethylene biosynthesis.";
RL   Plant Physiol. 153:1587-1596(2010).
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=8.3 uM for AdoMet;
CC         Vmax=13.5 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 with XBAT32. {ECO:0000250,
CC       ECO:0000269|PubMed:20511490}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-2356842, EBI-2356842;
CC       Q43309:ACS4; NbExp=4; IntAct=EBI-2356842, EBI-2436015;
CC   -!- TISSUE SPECIFICITY: Expressed in roots. {ECO:0000269|PubMed:12968022}.
CC   -!- INDUCTION: By cycloheximide (CHX). {ECO:0000269|PubMed:12968022}.
CC   -!- PTM: Ubiquitinated by XBAT32. Ubiquitination probably leads to its
CC       subsequent degradation, thus controlling ethylene production.
CC       {ECO:0000269|PubMed:20511490}.
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}.
DR   EMBL; AL049171; CAB38949.1; -; Genomic_DNA.
DR   EMBL; AL161564; CAB79475.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85169.1; -; Genomic_DNA.
DR   EMBL; AF332390; AAG48754.1; -; mRNA.
DR   PIR; T06004; T06004.
DR   RefSeq; NP_194350.1; NM_118753.3.
DR   SMR; Q9STR4; -.
DR   BioGrid; 14013; 4.
DR   IntAct; Q9STR4; 2.
DR   STRING; 3702.AT4G26200.1; -.
DR   iPTMnet; Q9STR4; -.
DR   PaxDb; Q9STR4; -.
DR   PRIDE; Q9STR4; -.
DR   EnsemblPlants; AT4G26200.1; AT4G26200.1; AT4G26200.
DR   GeneID; 828726; -.
DR   Gramene; AT4G26200.1; AT4G26200.1; AT4G26200.
DR   KEGG; ath:AT4G26200; -.
DR   Araport; AT4G26200; -.
DR   TAIR; locus:2136779; AT4G26200.
DR   eggNOG; KOG0256; Eukaryota.
DR   eggNOG; COG0436; LUCA.
DR   HOGENOM; HOG000011234; -.
DR   InParanoid; Q9STR4; -.
DR   KO; K01762; -.
DR   OMA; CDVLQEQ; -.
DR   OrthoDB; 1156861at2759; -.
DR   PhylomeDB; Q9STR4; -.
DR   SABIO-RK; Q9STR4; -.
DR   UniPathway; UPA00384; UER00562.
DR   PRO; PR:Q9STR4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9STR4; baseline and differential.
DR   Genevisible; Q9STR4; 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: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; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
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;
DR   PRODOM; Q9STR4.
DR   SWISS-2DPAGE; Q9STR4.
KW   Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate;
KW   Reference proteome; S-adenosyl-L-methionine; Ubl conjugation.
FT   CHAIN           1..447
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 7"
FT                   /id="PRO_0000123901"
FT   BINDING         61
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   447 AA;  50666 MW;  E78CC1FC834FD4A9 CRC64;
     MGLPLMMERS SNNNNVELSR VAVSDTHGED SPYFAGWKAY DENPYDESHN PSGVIQMGLA
     ENQVSFDLLE TYLEKKNPEG SMWGSKGAPG FRENALFQDY HGLKTFRQAM ASFMEQIRGG
     KARFDPDRIV LTAGATAANE LLTFILADPN DALLVPTPYY PGFDRDLRWR TGVKIVPIHC
     DSSNHFQITP EALESAYQTA RDANIRVRGV LITNPSNPLG ATVQKKVLED LLDFCVRKNI
     HLVSDEIYSG SVFHASEFTS VAEIVENIDD VSVKERVHIV YSLSKDLGLP GFRVGTIYSY
     NDNVVRTARR MSSFTLVSSQ TQHMLASMLS DEEFTEKYIR INRERLRRRY DTIVEGLKKA
     GIECLKGNAG LFCWMNLGFL LEKKTKDGEL QLWDVILKEL NLNISPGSSC HCSEVGWFRV
     CFANMSENTL EIALKRIHEF MDRRRRF
//

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