ID   1A11_CUCPE              Reviewed;         493 AA.
AC   P23279;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 1;
DE            Short=ACC synthase 1;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
GN   Name=ACC1A;
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 [MRNA].
RX   PubMed=1995630; DOI=10.1016/s0021-9258(19)67859-2;
RA   Sato T., Oeller P.W., Theologis A.;
RT   "The 1-aminocyclopropane-1-carboxylate synthase of Cucurbita. Purification,
RT   properties, expression in Escherichia coli, and primary structure
RT   determination by DNA sequence analysis.";
RL   J. Biol. Chem. 266:3752-3759(1991).
RN   [2]
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: By wounding in fruit and etiolated hypocotyls. By
CC       indoleacetic acid (IAA)/benzyladenine/LiCl only in fruit tissue.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; M58323; AAA33113.1; -; mRNA.
DR   EMBL; M61195; AAA33111.1; -; Genomic_DNA.
DR   PIR; A41141; A41141.
DR   AlphaFoldDB; P23279; -.
DR   SMR; P23279; -.
DR   BRENDA; 4.4.1.14; 1740.
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   1: Evidence at protein level;
KW   Ethylene biosynthesis; Fruit ripening; Lyase; Pyridoxal phosphate;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..493
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 1"
FT                   /id="PRO_0000123909"
FT   MOD_RES         279
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT   CONFLICT        177
FT                   /note="G -> R (in Ref. 2; AAA33111)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   493 AA;  55780 MW;  921DC3DFB17A8769 CRC64;
     MGFHQIDERN QALLSKIALD DGHGENSPYF DGWKAYDNDP FHPENNPLGV IQMGLAENQL
     SFDMIVDWIR KHPEASICTP EGLERFKSIA NFQDYHGLPE FRNAIANFMG KVRGGRVKFD
     PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAGFDR DLKWRTRAQI IRVHCNGSNN
     FQVTKAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD
     EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR
     RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRV GERHARFTKE LDKMGITCLN
     SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD
     DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DEGNVLNSPH
     TMSPHSPLVI AKN