1A11_ARATH
ID 1A11_ARATH Reviewed; 488 AA.
AC Q06429; Q43368; Q9S9C6;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase-like protein 1;
GN Name=ACS1; Synonyms=ACC2; OrderedLocusNames=At3g61510; ORFNames=F2A19.110;
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], LACK OF ENZYME ACTIVITY, AND
RP MUTAGENESIS OF SER-205.
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
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 [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 NUCLEOTIDE SEQUENCE OF 57-88.
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 100-152.
RC STRAIN=cv. C24; TISSUE=Flower;
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 [7]
RP TISSUE SPECIFICITY.
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).
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in young leaves and flowers. Not
CC expressed in roots. {ECO:0000269|PubMed:12968022}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
CC -!- CAUTION: Lacks the conserved tripeptide Ser/Thr-Asn-Pro in position 205
CC necessary for the ACS activity. {ECO:0000305}.
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DR EMBL; U26542; AAA96006.1; -; Genomic_DNA.
DR EMBL; U26543; AAB60312.1; -; mRNA.
DR EMBL; AL132962; CAB71081.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE80216.1; -; Genomic_DNA.
DR EMBL; AY133715; AAM91649.1; -; mRNA.
DR EMBL; Z12615; CAA78261.1; -; mRNA.
DR PIR; B47199; B47199.
DR PIR; T47943; T47943.
DR RefSeq; NP_191710.1; NM_116016.2.
DR AlphaFoldDB; Q06429; -.
DR SMR; Q06429; -.
DR IntAct; Q06429; 1.
DR STRING; 3702.AT3G61510.1; -.
DR PaxDb; Q06429; -.
DR PRIDE; Q06429; -.
DR ProteomicsDB; 244490; -.
DR EnsemblPlants; AT3G61510.1; AT3G61510.1; AT3G61510.
DR GeneID; 825324; -.
DR Gramene; AT3G61510.1; AT3G61510.1; AT3G61510.
DR KEGG; ath:AT3G61510; -.
DR Araport; AT3G61510; -.
DR TAIR; locus:2082817; AT3G61510.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q06429; -.
DR OMA; CDPEDGV; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q06429; -.
DR BioCyc; ARA:AT3G61510-MON; -.
DR PRO; PR:Q06429; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q06429; baseline and differential.
DR Genevisible; Q06429; AT.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
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 Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..488
FT /note="1-aminocyclopropane-1-carboxylate synthase-like
FT protein 1"
FT /id="PRO_0000123896"
FT MOD_RES 273
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT MUTAGEN 205
FT /note="S->TNPS: Restores ACS activity; when expressed in
FT E.coli."
FT /evidence="ECO:0000269|PubMed:8566772"
SQ SEQUENCE 488 AA; 55003 MW; 411E049B993DEEE1 CRC64;
MSQGACENQL LSKLALSDKH GEASPYFHGW KAYDNNPFHP THNPQGVIQM GLAENQLCSD
LIKEWIKENP QASICTAEGI DSFSDIAVFQ DYHGLKQFRQ AIATFMERAR GGRVRFEAER
VVMSGGATGA NETIMFCLAD PGDAFLVPTP YYAAFDRDLR WRTGVRIIPV ECSSSNNFQI
TKQALESAYL KAQETGIKIK GLIISNPLGT SLDRETLESL VSFINDKQIH LVCDEIYAAT
VFAEPGFISV AEIIQEMYYV NRDLIHIVYS LSKDMGLPGF RVGVVYSYND VVVSCARRMS
SFGLVSSQTQ SFLAAMLSDQ SFVDNFLVEV SKRVAKRHHM FTEGLEEMGI SCLRSNAGLF
VLMDLRHMLK DQTFDSEMAL WRVIINKVKI NVSPGSSFHC SEPGWFRVCF ANMDEDTLQI
ALERIKDFVV GDRANKNKNC NCICNNKREN KKRKSFQKNL KLSLSSMRYE EHVRSPKLMS
PHSPLLRA
