ID   1A1C_DIACA              Reviewed;         517 AA.
AC   P27486;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   25-MAY-2022, entry version 95.
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=ACS2; Synonyms=CARACC;
OS   Dianthus caryophyllus (Carnation) (Clove pink).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Caryophyllaceae; Caryophylleae; Dianthus.
OX   NCBI_TaxID=3570;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Petal;
RX   PubMed=1731995; DOI=10.1007/bf00034964;
RA   Park K.Y., Drory A., Woodson W.R.;
RT   "Molecular cloning of an 1-aminocyclopropane-1-carboxylate synthase from
RT   senescing carnation flower petals.";
RL   Plant Mol. Biol. 18:377-386(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; M66619; AAA33275.1; -; mRNA.
DR   PIR; S19252; S19252.
DR   AlphaFoldDB; P27486; -.
DR   SMR; P27486; -.
DR   PRIDE; P27486; -.
DR   UniPathway; UPA00384; UER00562.
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: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   S-adenosyl-L-methionine.
FT   CHAIN           1..517
FT                   /note="1-aminocyclopropane-1-carboxylate synthase"
FT                   /id="PRO_0000123911"
FT   REGION          443..467
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          497..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   517 AA;  58057 MW;  C31BA10732E940AE CRC64;
     MGSYKGVYDR EILSKIATND GHGENLEYFD GWKAYDRDPY HSTKNSNGVI QMGLAENQLC
     FDLVTEWLLK NPQASICTNE GVNKFMDIAI FQDYHGLPEF RSAVAKFMGK ARDEKVIFNP
     DRIVMSGGAS ASETLLFCLA NPGDAFLIPS PYYPAFNRDL RWRTGVNLIP FTCSSSNNFK
     ITKEALQSAY EDALKKNIKV KGIIVTNPSN PLGTVLDKDT LKMLLTFVNA KNIHLVCDEI
     YATTVFNSPS FISVAEVIKD MPHVNQDLVH ILYSLSKDMG MPGFRVGIIY SYNDRVVSTA
     RRMSSFGLVS SQTQFMIAAL LSDDDFVRRF LVESRDRLFR RHQHFTSELA KIGIGCLQGN
     AALFVWMDLR HLLDEATVER ELKLWRVIIN EVKINVSPGS SFLCSEPGWF RVCFANMDNA
     TLDVALNRIR SFVTRGRVDN STMTTTSARA AATTTTTTTT TTTTTTTTTT IKKKRGQMEL
     RLSFNNRRFE DGLMSPHSIL LSPHSPMPQS PLVKART