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 18-JUN-2025, entry version 134.
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 S-methyl-5'-thioadenosine + H(+); 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X67100; CAA47474.1; -; mRNA.
DR PIR; S25002; S25002.
DR RefSeq; NP_001236858.1; NM_001249929.2.
DR AlphaFoldDB; P31531; -.
DR SMR; P31531; -.
DR FunCoup; P31531; 651.
DR STRING; 3847.P31531; -.
DR PaxDb; 3847-GLYMA05G37410.2; -.
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; TYAMSAG; -.
DR OrthoDB; 691673at2759; -.
DR BRENDA; 4.4.1.14; 2483.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000008827; Chromosome 5.
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: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 CDD; cd00609; AAT_like; 1.
DR FunFam; 3.40.640.10:FF:000051; 1-aminocyclopropane-1-carboxylate synthase 3; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004839; Aminotransferase_I/II_large.
DR InterPro; IPR050478; Ethylene_sulfur-biosynth.
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 PANTHER; PTHR43795:SF6; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 6; 1.
DR PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR PRINTS; PR00753; ACCSYNTHASE.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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
//
