ID   1A1C_TOBAC              Reviewed;         491 AA.
AC   Q07262;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1994, sequence version 1.
DT   16-JUN-2009, entry version 54.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase;
DE            Short=ACC synthase;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
GN   Name=ACS1;
OS   Nicotiana tabacum (Common tobacco).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   asterids; lamiids; Solanales; Solanaceae; Nicotianoideae; Nicotianeae;
OC   Nicotiana.
OX   NCBI_TaxID=4097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Xanthi;
RX   PubMed=16653174;
RA   Bailey B.A., Avni A., Li N., Matoo A.K., Anderson J.D.;
RT   "Nucleotide sequence of the Nicotiana tabacum cv Xanthi gene encoding
RT   1-aminocyclopropane-1-carboxylate synthase.";
RL   Plant Physiol. 100:1615-1616(1992).
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.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family.
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DR   EMBL; X65982; CAA46797.1; -; mRNA.
DR   PIR; T03978; T03978.
DR   HSSP; P18485; 1IAX.
DR   SMR; Q07262; 16-438.
DR   BRENDA; 4.4.1.14; 298.
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   2: Evidence at transcript level;
KW   Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate;
KW   S-adenosyl-L-methionine.
FT   CHAIN         1    491       1-aminocyclopropane-1-carboxylate
FT                                synthase.
FT                                /FTId=PRO_0000123920.
FT   MOD_RES     278    278       N6-(pyridoxal phosphate)lysine (By
FT                                similarity).
SQ   SEQUENCE   491 AA;  55291 MW;  57B9FF4306686DFD CRC64;
     MGFENEKNSS ILSKLATNEE LGENSPYFDG WKAYDNDPFH PLKNPNGVIQ MGLAENQLCF
     DLIEEWIKRN PNASICTTEG IKSFRAIANF QDYHGLPEFR SAIAKFMEKT RGGRVTFDPE
     RVVMAGGATG ANETIIFCLA DTGDAFLVPS PYYPAFNRDL RWRTGVQLIP IPCDSSNNFQ
     ITTKAVREAY ENAQKSNIKV KGLILTNPSN PLGTTLDRDT LKNLLTFTNQ HNIHLVCDEI
     YAATVFNTPQ FVSIAEILDD ETSHCNKDLV HIVYSLSKDM GLPGFRVGIV YSFNDAVVNC
     ARKMSSFGLV STQTQYLLAE MLSDERFVSN FLTESSKRLA KRHKHFTNGL EEVGIKCLRS
     NAGLFCWMDL RPLLKESTFD SEMSLWRVII NDVKLNVSPG SSFDCQEPGF FRVCFANMDD
     ETVDIALARI RSFVGVKKSG DESTPILMEK KQQWKKNNLR LSFSKRMYDE SVNLSPLSSP
     IPHSPLVRAR T
//