ID   1A12_CUCMA              Reviewed;         475 AA.
AC   Q00257;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 100.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase CMA101;
DE            Short=ACC synthase;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
GN   Name=ACS2; Synonyms=PCVV4A;
OS   Cucurbita maxima (Pumpkin) (Winter squash).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Cucurbiteae; Cucurbita.
OX   NCBI_TaxID=3661;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RA   Nakagawa N., Mori H., Yamazaki K., Imaseki H.;
RT   "Cloning of a complementary DNA for auxin-induced 1-aminocyclopropane-1-
RT   carboxylate synthase and differential expression of the gene by auxin and
RT   wounding.";
RL   Plant Cell Physiol. 32:1153-1163(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RA   Nakagawa N., Kamiya Y., Imaseki H.;
RT   "Nucleotide sequence of an auxin-regulated 1-aminocyclopropane-1-carboxylic
RT   acid synthase gene from Cucurbita maxima Duch.";
RL   (er) Plant Gene Register PGR95-110(1995).
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 tissue wounding and auxin.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; U37774; AAA91152.1; -; Genomic_DNA.
DR   EMBL; D01033; BAA00839.1; -; mRNA.
DR   PIR; JQ2214; JQ2214.
DR   AlphaFoldDB; Q00257; -.
DR   SMR; Q00257; -.
DR   OrthoDB; 1156861at2759; -.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000504608; Unplaced.
DR   GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; ISS:UniProtKB.
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   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN           1..475
FT                   /note="1-aminocyclopropane-1-carboxylate synthase CMA101"
FT                   /id="PRO_0000123908"
FT   MOD_RES         272
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   475 AA;  53481 MW;  D02A666E137F44A0 CRC64;
     MKMLSTKATC NSHGQDSSYF LGWEAYENNP FHHTSNPNGI IQMGLAENQL SFDLLESWLS
     KNPDAASFKR DGKSIFRELA LFQDYHGLPA FKKALVEFMA EIRGNKVSFE ANNIVLTAGA
     TSANETLMFC LAEAGDAFLL PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITQSALEQ
     AYKDAQTRNL RVKGVLVTNP SNPLGTTMNR DELNLVFDFI TSKGIHLISD EIYSGTVFGS
     PGFVSAMEVL KERSSEDEEV WKRVHIVYSL SKDLGLPGFR VGAIYSNDDM VVAAATKMSS
     FGLVSSQTQY LLSAMLSDKK FTISYISENQ KRLKQRQKML VSGLQKAGIN CLDSNAGLFC
     WVDMRHLLES DKFESELELW KKIVYEVGLN ISPGSSCHCT EPGWFRVCFA NMSESTLKLA
     VRRLKSFVTE LRSTTTSNHR NHDNKICKNI KKNIFTKWVF RQSAQEANRK MQAER