1A11_CUCMA
ID 1A11_CUCMA Reviewed; 493 AA.
AC P23599;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 25-MAY-2022, entry version 95.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase CMW33;
DE Short=ACC synthase;
DE EC=4.4.1.14;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
GN Name=ACS1; Synonyms=ACCW;
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 [MRNA].
RA Nakajima N., Mori H., Yamazaki K., Imaseki H.;
RT "Molecular cloning and sequence of a complementary DNA encoding 1-
RT aminocyclopropane-1-carboxylate synthase induced by tissue wounding.";
RL Plant Cell Physiol. 31:1021-1029(1990).
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.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; D01032; BAA00838.1; -; mRNA.
DR PIR; JQ0926; JQ0926.
DR AlphaFoldDB; P23599; -.
DR SMR; P23599; -.
DR OrthoDB; 1156861at2759; -.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000504608; Unplaced.
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 Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..493
FT /note="1-aminocyclopropane-1-carboxylate synthase CMW33"
FT /id="PRO_0000123907"
FT MOD_RES 279
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 493 AA; 55896 MW; F39234AC99CBEF6B CRC64;
MEFHQIDERN QALLSKIAVD DGHGENSPYF DGWKAYDNDP FHPEDNPLGV IQMGLAENQL
SFDMIVDWIR KHPEASICTP KGLERFKSIA NFQDYHGLPE FRNGIASFMG KVRGGRVQFD
PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAAFDR DLKWRTRAQI IRVHCNSSNN
FQVTKAALEI AYKKAQEANI KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD
EIYSATVFKA PTFISIAQIV EEMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR
RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRL AERHARFTKE LDKMGITCLN
SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD
DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRRRENKLR LSFSFSGRRY DEGNVLNSPH
TMSPHSPLVI AKN
