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1A1C_SOYBN
ID   1A1C_SOYBN              Reviewed;         484 AA.
AC   P31531;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 120.
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   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Century; TISSUE=Leaf;
RA   Liu D., Li N., Mattoo A.K.;
RL   Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases.
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; X67100; CAA47474.1; -; mRNA.
DR   PIR; S25002; S25002.
DR   RefSeq; NP_001236858.1; NM_001249929.1.
DR   AlphaFoldDB; P31531; -.
DR   SMR; P31531; -.
DR   STRING; 3847.GLYMA05G37410.2; -.
DR   PRIDE; P31531; -.
DR   EnsemblPlants; KRH59970; KRH59970; GLYMA_05G211700.
DR   GeneID; 547976; -.
DR   Gramene; KRH59970; KRH59970; GLYMA_05G211700.
DR   KEGG; gmx:547976; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   HOGENOM; CLU_017584_1_0_1; -.
DR   InParanoid; P31531; -.
DR   OMA; EQWSMEH; -.
DR   OrthoDB; 1156861at2759; -.
DR   BRENDA; 4.4.1.14; 2483.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000008827; Chromosome 5.
DR   Genevisible; P31531; GM.
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..484
FT                   /note="1-aminocyclopropane-1-carboxylate synthase"
FT                   /id="PRO_0000123919"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   484 AA;  54731 MW;  152F7AD12B992987 CRC64;
     MGLMDVDQTQ LLSKMVIGDG HGEASPYFDG WKAYDENPFH PKENPNGVIQ MGLAENQLTS
     DLVEDWILNN PEASICTPEG INDFRAIANF QDYHGLPEFR NAVAKFMGRT RGNRVTFDPD
     RIVMSGGATG AHEVTTFCLA DPGDAFLVPI PYYPGFDRDL RWRTGIKLVP VMCDSSNNFK
     LTKQALEDAY EKAKEDNIRV KGLLITNPSN PLGTVMDRNT LRTVMSFINE KRIHLVSDEI
     YSATVFSHPS FISIAEILEE DTDIECDRNL VHIVYSLSKD MGFPGFRVGI IYSYNDAVVH
     CARKMSSFGL VSTQTQYLLA SMLNDDEFVE SFLVESAKRL AQRHRVFTGG LAKVGIKCLQ
     SNAGLFVWMD LRQLLKKPTL DSEMELWRVI IDEVKINVSP GSSFHCTEPG WFRVCYANMD
     DMAVQIALQR IRNFVLQNKE IMVPNKKHCW HSNLRLSLKT RRFDDIMMSP HSPIPQSPLV
     KATI
 
 
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