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 03-AUG-2022, entry version 136.
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 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; 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 PDBsum; 7DLW; -.
DR PDBsum; 7DLY; -.
DR AlphaFoldDB; Q9STR4; -.
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 ProteomicsDB; 244543; -.
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 HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q9STR4; -.
DR OMA; HGIEYAT; -.
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: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 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 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 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 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
