1A1C_TOBAC
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 25-MAY-2022, entry version 96.
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; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
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; DOI=10.1104/pp.100.3.1615;
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 1-
RT aminocyclopropane-1-carboxylate synthase.";
RL Plant Physiol. 100:1615-1616(1992).
CC -!- FUNCTION: Catalyzes the formation of 1-aminocyclopropane-1-carboxylate,
CC a direct precursor of ethylene in higher plants.
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 -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC -!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-
CC methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
CC -!- SUBUNIT: Homodimer.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X65982; CAA46797.1; -; mRNA.
DR PIR; T03978; T03978.
DR RefSeq; NP_001313190.2; NM_001326261.2.
DR AlphaFoldDB; Q07262; -.
DR SMR; Q07262; -.
DR STRING; 4097.Q07262; -.
DR GeneID; 107831434; -.
DR KEGG; nta:107831434; -.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000084051; Unplaced.
DR GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:UniProtKB-EC.
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; IEA:UniProtKB-UniPathway.
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 2: Evidence at transcript level;
KW Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..491
FT /note="1-aminocyclopropane-1-carboxylate synthase"
FT /id="PRO_0000123920"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
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