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   02-SEP-2026, entry version 152.
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   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [4]
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   [5]
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   [6]
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         S-methyl-5'-thioadenosine + H(+); 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       Q9STR4; Q43309: ACS4; NbExp=4; IntAct=EBI-2356842, EBI-2436015;
CC       Q9STR4; Q9STR4: ACS7; NbExp=2; IntAct=EBI-2356842, EBI-2356842;
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}.
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DR   EMBL; AL049171; CAB38949.1; -; Genomic_DNA.
DR   EMBL; AL161564; CAB79475.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE85169.1; -; Genomic_DNA.
DR   EMBL; OZ408686; CAO7048784.1; -; Genomic_DNA.
DR   EMBL; AF332390; AAG48754.1; -; mRNA.
DR   PIR; T06004; T06004.
DR   RefSeq; NP_194350.1; NM_118753.3.
DR   PDB; 7DLW; X-ray; 2.19 A; A/B/C/D=1-447.
DR   PDB; 7DLY; X-ray; 2.94 A; A/B=1-447.
DR   AlphaFoldDB; Q9STR4; -.
DR   SMR; Q9STR4; -.
DR   BioGRID; 14013; 4.
DR   FunCoup; Q9STR4; 288.
DR   IntAct; Q9STR4; 2.
DR   STRING; 3702.Q9STR4; -.
DR   iPTMnet; Q9STR4; -.
DR   PaxDb; 3702-Q9STR4; -.
DR   ProteomicsDB; 244543; -.
DR   GeneID; 828726; -.
DR   KEGG; ath:AT4G26200; -.
DR   Araport; AT4G26200; -.
DR   TAIR; AT4G26200; ACS7.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_0_1; -.
DR   InParanoid; Q9STR4; -.
DR   OMA; PYYGTFV; -.
DR   PhylomeDB; Q9STR4; -.
DR   BRENDA; 4.4.1.14; 399.
DR   SABIO-RK; Q9STR4; -.
DR   UniPathway; UPA00384; UER00562.
DR   PRO; PR:Q9STR4; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q9STR4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISM:TAIR.
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   CDD; cd00609; AAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000051; 1-aminocyclopropane-1-carboxylate synthase 3; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050478; Ethylene_sulfur-biosynth.
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   PANTHER; PTHR43795:SF39; AMINOTRANSFERASE CLASS I_CLASSII DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
DR   PDBsum; 7DLW; -.
DR   PDBsum; 7DLY; -.
PE   1: Evidence at protein level;
KW   3D-structure; Ethylene biosynthesis; Fruit ripening; Lyase;
KW   Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW   Ubl conjugation.
FT   CHAIN           1..447
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 7"
FT                   /id="PRO_0000123901"
FT   BINDING         61
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         100
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         285
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   HELIX           20..23
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           32..42
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   TURN            47..49
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           66..70
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           92..95
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           104..117
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   TURN            118..120
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           126..128
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          129..133
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           134..146
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          152..158
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           163..166
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   TURN            167..171
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          174..178
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           182..184
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:7DLY"
FT   HELIX           190..202
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          207..215
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   TURN            217..219
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           222..224
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           225..238
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          241..245
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           249..251
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          252..254
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           255..257
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           261..266
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           271..274
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          277..283
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   TURN            284..286
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           290..292
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          295..300
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           302..311
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           312..314
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           316..318
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           319..330
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           332..359
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          369..376
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           378..380
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          382..385
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           386..398
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          402..406
FT                   /evidence="ECO:0007829|PDB:7DLY"
FT   HELIX           407..410
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          417..421
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   STRAND          423..425
FT                   /evidence="ECO:0007829|PDB:7DLW"
FT   HELIX           427..440
FT                   /evidence="ECO:0007829|PDB:7DLW"
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
//