1A14_ARATH
ID 1A14_ARATH Reviewed; 474 AA.
AC Q43309; Q9S9C4;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 4;
DE Short=ACC synthase 4;
DE EC=4.4.1.14;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 4;
GN Name=ACS4; Synonyms=ACC4; OrderedLocusNames=At2g22810; ORFNames=T20K9.2;
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 [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, AND
RP INDUCTION.
RC STRAIN=cv. Columbia;
RX PubMed=7642574; DOI=10.1074/jbc.270.32.19093;
RA Abel S., Nguyen M.D., Chow W., Theologis A.;
RT "ACS4, a primary indoleacetic acid-responsive gene encoding 1-
RT aminocyclopropane-1-carboxylate synthase in Arabidopsis thaliana.
RT Structural characterization, expression in Escherichia coli, and expression
RT characteristics in response to auxin.";
RL J. Biol. Chem. 270:19093-19099(1995).
RN [2]
RP ERRATUM OF PUBMED:7642574.
RA Abel S., Nguyen M.D., Chow W., Theologis A.;
RL J. Biol. Chem. 270:26020-26020(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
RN [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE OF 50-81.
RX PubMed=1438312; DOI=10.1073/pnas.89.22.11046;
RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.;
RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis
RT thaliana.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992).
RN [7]
RP ENZYME ACTIVITY, 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 [8]
RP INTERACTION WITH ETO1 AND EOL1.
RX PubMed=18808454; DOI=10.1111/j.1365-313x.2008.03693.x;
RA Christians M.J., Gingerich D.J., Hansen M., Binder B.M., Kieber J.J.,
RA Vierstra R.D.;
RT "The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate
RT ethylene biosynthesis in Arabidopsis by controlling type-2 ACC synthase
RT levels.";
RL Plant J. 57:332-345(2009).
RN [9]
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=15 uM for AdoMet;
CC Vmax=31.20 uM/h/mg enzyme;
CC pH dependence:
CC Optimum pH is 7.8.;
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. Interacts (via its C-terminal
CC region) with ETO1 and EOL1. {ECO:0000250, ECO:0000269|PubMed:18808454,
CC ECO:0000269|PubMed:20511490}.
CC -!- INTERACTION:
CC Q43309; Q43309: ACS4; NbExp=2; IntAct=EBI-2436015, EBI-2436015;
CC Q43309; Q9SAR0: ACS6; NbExp=2; IntAct=EBI-2436015, EBI-2356658;
CC Q43309; Q9STR4: ACS7; NbExp=4; IntAct=EBI-2436015, EBI-2356842;
CC Q43309; Q9T065: ACS8; NbExp=2; IntAct=EBI-2436015, EBI-2357693;
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves and flowers.
CC {ECO:0000269|PubMed:7642574}.
CC -!- INDUCTION: By indole-3-acetic acid (IAA) and cycloheximide (CHX). By
CC auxin. {ECO:0000269|PubMed:12968022, ECO:0000269|PubMed:7642574}.
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; U23481; AAC49037.1; -; mRNA.
DR EMBL; U23482; AAA85039.1; -; Genomic_DNA.
DR EMBL; AC004786; AAC32428.1; -; Genomic_DNA.
DR EMBL; AC005617; AAM15065.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC07360.1; -; Genomic_DNA.
DR EMBL; AF332404; AAG48767.1; -; mRNA.
DR PIR; B84617; B84617.
DR PIR; G46376; G46376.
DR RefSeq; NP_179866.1; NM_127846.2.
DR AlphaFoldDB; Q43309; -.
DR SMR; Q43309; -.
DR BioGRID; 2165; 2.
DR IntAct; Q43309; 5.
DR STRING; 3702.AT2G22810.1; -.
DR PaxDb; Q43309; -.
DR PRIDE; Q43309; -.
DR EnsemblPlants; AT2G22810.1; AT2G22810.1; AT2G22810.
DR GeneID; 816812; -.
DR Gramene; AT2G22810.1; AT2G22810.1; AT2G22810.
DR KEGG; ath:AT2G22810; -.
DR Araport; AT2G22810; -.
DR TAIR; locus:2059170; AT2G22810.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q43309; -.
DR OMA; AACFKRD; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q43309; -.
DR BioCyc; ARA:AT2G22810-MON; -.
DR BioCyc; MetaCyc:AT2G22810-MON; -.
DR SABIO-RK; Q43309; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q43309; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q43309; baseline and differential.
DR Genevisible; Q43309; 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; 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; Ubl conjugation.
FT CHAIN 1..474
FT /note="1-aminocyclopropane-1-carboxylate synthase 4"
FT /id="PRO_0000123898"
FT BINDING 47
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 474 AA; 53795 MW; 98FD27622EAF3C21 CRC64;
MVQLSRKATC NSHGQVSSYF LGWEEYEKNP YDVTKNPQGI IQMGLAENQL CFDLLESWLA
QNTDAACFKR DGQSVFRELA LFQDYHGLSS FKNAFADFMS ENRGNRVSFD SNNLVLTAGA
TSANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGVEI VPIQSSSTNG FRITKLALEE
AYEQAKKLDL NVKGILITNP SNPLGTTTTQ TELNILFDFI TKNKNIHLVS DEIYSGTVFN
SSEFISVMEI LKNNQLENTD VLNRVHIVCS LSKDLGLPGF RVGAIYSNDK DVISAATKMS
SFGLVSSQTQ YLLSSLLSDK KFTKNYLREN QKRLKNRQRK LVLGLEAIGI KCLKSNAGLF
CWVDMRPLLR SKTFEAEMDL WKKIVYEVKL NISPGSSCHC EEPGWFRVCF ANMIDETLKL
ALKRLKMLVD DENSSRRCQK SKSERLNGSR KKTMSNVSNW VFRLSFHDRE AEER
