ID   1A12_CUCPE              Reviewed;         494 AA.
AC   Q00379;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 2;
DE            Short=ACC synthase 2;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
GN   Name=ACS2; Synonyms=ACC1B;
OS   Cucurbita pepo (Vegetable marrow) (Summer squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1871117; DOI=10.1073/pnas.88.16.7021;
RA   Huang P.-L., Parks J.E., Rottman W.H., Theologis A.;
RT   "Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in zucchini
RT   (Cucurbita pepo) are clustered and similar but differentially regulated.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:7021-7025(1991).
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   -!- INDUCTION: Hormones, such as auxin, environmental factors, such as
CC       mechanical wounding and a number of chemicals.
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; M61195; AAA33112.1; -; Genomic_DNA.
DR   PIR; B41141; B41141.
DR   AlphaFoldDB; Q00379; -.
DR   SMR; Q00379; -.
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..494
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 2"
FT                   /id="PRO_0000123910"
FT   REGION          474..494
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        345
FT                   /note="A -> AS (in Ref. 1; AAA33112)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   494 AA;  55923 MW;  02AE029AA4912C36 CRC64;
     MGFHQIDERN QALLSKIAID DGHGENSAYF DGWKAYDNNP FHPENNPLGV IQMGLAENQL
     SFGMIVDWIR KHPEASICTP EGLEKFKSIA NFQDYHGLQE FRKAMASFMG KVRGGRVKFD
     PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAAFDR DLKWRTRAQI IPVHCNSSNN
     FQVTEAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD
     EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR
     RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRL GERHARFTKE LDKMGITCLN
     SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD
     DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DKGNVLNSPH
     TMSPHSPLVR ARTY