ID   1A19_ARATH              Reviewed;         470 AA.
AC   Q9M2Y8;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 9;
DE            Short=ACC synthase 9;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 9;
DE   AltName: Full=Ethylene-overproduction protein 3;
GN   Name=ACS9; Synonyms=ETO3; OrderedLocusNames=At3g49700;
GN   ORFNames=T16K5.50;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   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.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   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
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [3]
RP   MUTANT ETO3.
RX   PubMed=12566591; DOI=10.1105/tpc.006882;
RA   Chae H.S., Faure F., Kieber J.J.;
RT   "The eto1, eto2, and eto3 mutations and cytokinin treatment increase
RT   ethylene biosynthesis in Arabidopsis by increasing the stability of
RT   ACS protein.";
RL   Plant Cell 15:545-559(2003).
RN   [4]
RP   ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, AND PUTATIVE
RP   PROTEOLYTIC 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).
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
CC       ethylene.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane-
CC       1-carboxylate + methylthioadenosine.
CC   -!- COFACTOR: Pyridoxal phosphate.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=40 uM for AdoMet;
CC         Vmax=324.5 uM/h/mg enzyme;
CC       pH dependence:
CC         Optimum pH is 8;
CC   -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-
CC       adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step
CC       1/2.
CC   -!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of
CC       heterodimerization with other ACS enzymes is however unsure (By
CC       similarity).
CC   -!- TISSUE SPECIFICITY: Expressed in roots and siliques.
CC   -!- INDUCTION: By cycloheximide (CHX).
CC   -!- PTM: May be processed at its C-terminus.
CC   -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation
CC       of such stability, play a central role in ethylene biosynthesis.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AL132965; CAB66908.1; -; Genomic_DNA.
DR   EMBL; AF332391; AAG48755.1; -; mRNA.
DR   IPI; IPI00537517; -.
DR   PIR; T46036; T46036.
DR   RefSeq; NP_190539.1; -.
DR   UniGene; At.743; -.
DR   HSSP; P37821; 1M7Y.
DR   SMR; Q9M2Y8; 10-428.
DR   GeneID; 824132; -.
DR   GenomeReviews; BA000014_GR; AT3G49700.
DR   KEGG; ath:AT3G49700; -.
DR   NMPDR; fig|3702.1.peg.16218; -.
DR   TAIR; At3g49700; -.
DR   OMA; Q9M2Y8; IANDESK.
DR   BRENDA; 4.4.1.14; 302.
DR   ArrayExpress; Q9M2Y8; -.
DR   GermOnline; AT3G49700; Arabidopsis thaliana.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase ...; IDA:TAIR.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0016769; F:transferase activity, transferring nitrogen...; IEA:InterPro.
DR   GO; GO:0009693; P:ethylene biosynthetic process; IMP:TAIR.
DR   GO; GO:0006417; P:regulation of translation; IDA:TAIR.
DR   GO; GO:0009835; P:ripening; IEA:UniProtKB-KW.
DR   InterPro; IPR001176; ACC_synthase.
DR   InterPro; IPR004839; Aminotrans_I/II.
DR   InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR   Gene3D; G3DSA:3.40.640.10; PyrdxlP-dep_Trfase_major_sub1; 1.
DR   Gene3D; G3DSA:3.90.1150.10; PyrdxlP-dep_Trfase_major_sub2; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Ethylene biosynthesis; Fruit ripening; Lyase;
KW   Pyridoxal phosphate; S-adenosyl-L-methionine.
FT   CHAIN         1    470       1-aminocyclopropane-1-carboxylate
FT                                synthase 9.
FT                                /FTId=PRO_0000123903.
FT   BINDING      47     47       Substrate (By similarity).
FT   BINDING      85     85       Substrate (By similarity).
FT   MOD_RES     272    272       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
FT   MUTAGEN     457    457       V->D: In eto3; increases its stability
FT                                heading to ethylene overproduction.
SQ   SEQUENCE   470 AA;  53170 MW;  2110331C76ACED4E CRC64;
     MKQLSRKVTS NAHGQDSSYF LGWEEYEKNP YDEIKNPNGI IQMGLAENQL CFDLIETWLA
     KNPDAAGLKK DGQSIFKELA LFQDYHGLPE FKKALAEFME EIRGNRVTFD PSKIVLAAGS
     TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ
     AYQQAQKLDL KVKGVLVTNP SNPLGTMLTR RELNLLVDFI TSKNIHLISD EIYSGTVFGF
     EQFVSVMDVL KDKNLENSEV SKRVHIVYSL SKDLGLPGFR VGAIYSNDEM VVSAATKMSS
     FGLVSSQTQY LLSALLSDKK FTSTYLDENQ KRLKIRQKKL VSGLEAAGIT CLKSNAGLFC
     WVDMRHLLDT NTFEAELELW KKIVYDVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA
     MKRLKEYVES TDSRRVISKS SHDRIKSLRK RTVSNWVFRV SWTDRVPDER
//