1A12_ARATH
ID 1A12_ARATH Reviewed; 496 AA.
AC Q06402; Q941E7;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 2;
DE Short=ACC synthase 2;
DE EC=4.4.1.14;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 2;
GN Name=ACS2; Synonyms=ACC1; OrderedLocusNames=At1g01480; ORFNames=F22L4.4;
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], ALTERNATIVE SPLICING (ISOFORM 1), AND
RP VARIANT ILE-136.
RC STRAIN=cv. Columbia;
RX PubMed=1357670; DOI=10.1073/pnas.89.20.9969;
RA van der Straeten D., Rodrigues-Pousada R.A., Villarroel R., Hanley S.,
RA Goodman H.M., Van Montagu M.;
RT "Cloning, genetic mapping, and expression analysis of an Arabidopsis
RT thaliana gene that encodes 1-aminocyclopropane-1-carboxylate synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:9969-9973(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RC STRAIN=cv. Columbia;
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RC STRAIN=cv. Columbia;
RX PubMed=9666060; DOI=10.1016/s0378-1119(98)00286-8;
RA Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P.,
RA De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P.,
RA van Montagu M.;
RT "Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located
RT at the top of chromosome 1.";
RL Gene 215:11-17(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
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 [7]
RP MUTAGENESIS OF 206-THR--PRO-208.
RC STRAIN=cv. Columbia;
RX PubMed=8566772; DOI=10.1016/0378-1119(95)00694-x;
RA Liang X.-W., Oono Y., Shen N.F., Koehler C., Li K., Scolnik P.A.,
RA Theologis A.;
RT "Characterization of two members (ACS1 and ACS3) of the 1-
RT aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis
RT thaliana.";
RL Gene 167:17-24(1995).
RN [8]
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 [9]
RP PHOSPHORYLATION AT SER-483; SER-488 AND SER-491.
RX PubMed=15539472; DOI=10.1105/tpc.104.026609;
RA Liu Y., Zhang S.;
RT "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by MPK6,
RT a stress-responsive mitogen-activated protein kinase, induces ethylene
RT biosynthesis in Arabidopsis.";
RL Plant Cell 16:3386-3399(2004).
RN [10]
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=45 uM for AdoMet;
CC Vmax=32 uM/h/mg enzyme;
CC pH dependence:
CC Optimum pH is 8.2.;
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q06402-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q06402-2; Sequence=VSP_009111;
CC -!- TISSUE SPECIFICITY: High in developing leaves and in flowers. Expressed
CC in roots and siliques. {ECO:0000269|PubMed:12968022}.
CC -!- INDUCTION: By ethylene. By indole-3-acetic acid (IAA) and cycloheximide
CC (CHX). {ECO:0000269|PubMed:12968022}.
CC -!- PTM: Phosphorylated on serine residue by MAP kinase (MPK6).
CC {ECO:0000269|PubMed:15539472}.
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; Z12614; CAA78260.1; -; Genomic_DNA.
DR EMBL; M95594; AAA97516.1; -; Genomic_DNA.
DR EMBL; M95595; AAB59298.1; -; mRNA.
DR EMBL; Y12776; CAA73310.1; -; Genomic_DNA.
DR EMBL; AC061957; AAF81308.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27293.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27294.1; -; Genomic_DNA.
DR EMBL; AF334719; AAG50097.1; -; mRNA.
DR EMBL; AY052207; AAK97678.1; -; mRNA.
DR EMBL; AY143877; AAN28816.1; -; mRNA.
DR PIR; A47199; A47199.
DR RefSeq; NP_171655.1; NM_100030.4. [Q06402-1]
DR RefSeq; NP_849572.1; NM_179241.1. [Q06402-2]
DR AlphaFoldDB; Q06402; -.
DR SMR; Q06402; -.
DR BioGRID; 22324; 1.
DR IntAct; Q06402; 1.
DR STRING; 3702.AT1G01480.1; -.
DR iPTMnet; Q06402; -.
DR PaxDb; Q06402; -.
DR PRIDE; Q06402; -.
DR ProteomicsDB; 245135; -. [Q06402-1]
DR EnsemblPlants; AT1G01480.1; AT1G01480.1; AT1G01480. [Q06402-1]
DR EnsemblPlants; AT1G01480.2; AT1G01480.2; AT1G01480. [Q06402-2]
DR GeneID; 837082; -.
DR Gramene; AT1G01480.1; AT1G01480.1; AT1G01480. [Q06402-1]
DR Gramene; AT1G01480.2; AT1G01480.2; AT1G01480. [Q06402-2]
DR KEGG; ath:AT1G01480; -.
DR Araport; AT1G01480; -.
DR TAIR; locus:2025361; AT1G01480.
DR eggNOG; KOG0256; Eukaryota.
DR InParanoid; Q06402; -.
DR OMA; HFMGKAR; -.
DR PhylomeDB; Q06402; -.
DR BioCyc; ARA:AT1G01480-MON; -.
DR BioCyc; MetaCyc:AT1G01480-MON; -.
DR BRENDA; 4.4.1.14; 399.
DR SABIO-RK; Q06402; -.
DR UniPathway; UPA00384; UER00562.
DR PRO; PR:Q06402; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q06402; baseline and differential.
DR Genevisible; Q06402; 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; 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 Alternative splicing; Ethylene biosynthesis; Fruit ripening; Lyase;
KW Phosphoprotein; Pyridoxal phosphate; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..496
FT /note="1-aminocyclopropane-1-carboxylate synthase 2"
FT /id="PRO_0000123897"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15539472"
FT MOD_RES 488
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15539472"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:15539472"
FT VAR_SEQ 1..106
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14593172"
FT /id="VSP_009111"
FT VARIANT 136
FT /note="M -> I"
FT /evidence="ECO:0000269|PubMed:1357670"
FT MUTAGEN 206..208
FT /note="Missing: Abolishes 1-aminocyclopropane-1-carboxylate
FT synthase function."
FT /evidence="ECO:0000269|PubMed:8566772"
SQ SEQUENCE 496 AA; 55532 MW; 766318AE9B5F1566 CRC64;
MGLPGKNKGA VLSKIATNNQ HGENSEYFDG WKAYDKDPFH LSRNPHGIIQ MGLAENQLCL
DLIKDWVKEN PEASICTLEG IHQFSDIANF QDYHGLKKFR QAIAHFMGKA RGGRVTFDPE
RVVMSGGATG ANETIMFCLA DPGDVFLIPS PYYAAFDRDL RWRTGVEIIP VPCSSSDNFK
LTVDAAEWAY KKAQESNKKV KGLILTNPSN PLGTMLDKDT LTNLVRFVTR KNIHLVVDEI
YAATVFAGGD FVSVAEVVND VDISEVNVDL IHIVYSLSKD MGLPGFRVGI VYSFNDSVVS
CARKMSSFGL VSSQTQLMLA SMLSDDQFVD NFLMESSRRL GIRHKVFTTG IKKADIACLT
SNAGLFAWMD LRHLLRDRNS FESEIELWHI IIDRVKLNVS PGSSFRCTEP GWFRICFANM
DDDTLHVALG RIQDFVSKNK NKIVEKASEN DQVIQNKSAK KLKWTQTNLR LSFRRLYEDG
LSSPGIMSPH SPLLRA
