ID   1A13_SOLLC              Reviewed;         469 AA.
AC   Q42881; Q96571;
DT   28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 55.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 3;
DE            Short=ACC synthase 3;
DE            EC=4.4.1.14;
DE   AltName: Full=Le-ACS3;
DE            Short=ACS-3;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 3;
GN   Name=ACS3;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae;
OC   Solanum; Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. VFN8; TISSUE=Leaf, and Root;
RX   MEDLINE=95294010; PubMed=7775465; DOI=10.1074/jbc.270.23.14056;
RA   Olson D.C., Oetiker J.H., Yang S.F.;
RT   "Analysis of LE-ACS3, a 1-aminocyclopropane-1-carboxylic acid synthase
RT   gene expressed during flooding in the roots of tomato plants.";
RL   J. Biol. Chem. 270:14056-14061(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Rutgers;
RA   Kawakita K., Hennig L., Rottmann W.R., Yu G.X., Zarembinski T.I.,
RA   Taylor L.D., Theologis A.;
RT   "The tomato 1-aminocyclopropane-1-carboxylate (ACC) synthase multigene
RT   family is encoded by at least eight members.";
RL   Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   PARTIAL PROTEIN SEQUENCE.
RX   MEDLINE=91045911; PubMed=2122449; DOI=10.1073/pnas.87.20.7930;
RA   Yip W.K., Dong J.G., Kenny J.W., Thompson G.A., Yang S.F.;
RT   "Characterization and sequencing of the active site of 1-
RT   aminocyclopropane-1-carboxylate synthase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:7930-7934(1990).
CC   -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-
CC       carboxylate, a direct precursor of ethylene in higher plants.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane-
CC       1-carboxylate + methylthioadenosine.
CC   -!- COFACTOR: Pyridoxal phosphate.
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 (By similarity).
CC   -!- INDUCTION: By flooding.
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; L34171; AAA78789.1; -; Genomic_DNA.
DR   EMBL; U18055; AAB48946.1; -; Genomic_DNA.
DR   EMBL; U17972; AAB48945.1; -; mRNA.
DR   PIR; A57540; A57540.
DR   UniGene; Les.3642; -.
DR   HSSP; P37821; 1M7Y.
DR   SMR; Q42881; 12-428.
DR   BRENDA; 4.4.1.14; 281054.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase ...; IEA:EC.
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; IEA:UniProtKB-KW.
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   Direct protein sequencing; Ethylene biosynthesis; Fruit ripening;
KW   Lyase; Pyridoxal phosphate; S-adenosyl-L-methionine.
FT   CHAIN         1    469       1-aminocyclopropane-1-carboxylate
FT                                synthase 3.
FT                                /FTId=PRO_0000123913.
FT   MOD_RES     272    272       N6-(pyridoxal phosphate)lysine.
FT   CONFLICT    243    243       F -> L (in Ref. 2; AAB48945).
FT   CONFLICT    335    335       K -> R (in Ref. 2; AAB48945).
SQ   SEQUENCE   469 AA;  53094 MW;  FA5ADCCE3F54F5BC CRC64;
     MKLLSEKATC NSHGQDSSYF LGWQEYEKNP YDEIQNPKGI IQMGLAENQL SFDLLESWLA
     QNPDAAGFKR NGESIFRELA LFQDYHGLPA FKNAMTKFMS EIRGNRVSFD SNNLVLTAGA
     TSANETLMFC LANQGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FRITESALEE
     AYLDAKKRNL KVKGVLVTNP SNPLGTTLNR NELELLLTFI DEKGIHLISD EIYSGTVFNS
     PGFVSVMEVL IEKNYMKTRV WERVHIVYSL SKDLGLPGFR IGAIYSNDEM VVSAATKMSS
     FGLVSSQTQY LLSCMLSDKK FTKKYISENQ KRLKKRHAML VKGLKSAGIN CLESNAGLFC
     WVDMRHLLSS NNFDAEMDLW KKIVYDVGLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA
     MRRIKDFVES TAPNATNHQN QQQSNANSKK KSFSKWVFRL SFNDRQRER
//