ID   1A11_PRUMU              Reviewed;         492 AA.
AC   Q9MB95;
DT   02-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 87.
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=ACS1;
OS   Prunus mume (Japanese apricot) (Armeniaca mume).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Amygdaleae; Prunus.
OX   NCBI_TaxID=102107;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Mita S., Kirita C., Kato M., Hyodo H.;
RT   "Expression of ACC synthase is enhanced earlier than that of ACC oxidase
RT   during fruit ripening of mume (Prunus mume).";
RL   Physiol. Plantarum 107:319-328(1999).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; AB031026; BAA90549.1; -; mRNA.
DR   AlphaFoldDB; Q9MB95; -.
DR   SMR; Q9MB95; -.
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..492
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 1"
FT                   /id="PRO_0000123918"
FT   MOD_RES         277
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   492 AA;  55066 MW;  2002047AF2B43D89 CRC64;
     MGSSSATANR FLLSKIATSE GHGENSPYFD GWKAYDRNPF HPTKNPEGVI QMGLAENQLS
     FDSIEDWIKK NPKASICTPE GVEEFKNVAI FQDYHGFPEF RKAVAMFMSK ARGGRVTFDP
     NRVVMSGGAT GANELVMFCL ADPGDAFLVP SPYYPAFFRD LGWRTGVQIV PVDCDSSNNF
     KITKEALEAA YEKAQKNNIN VKGLIITNPS NPLGTTLDRN TLESLVEFIN QKNIHLVCDE
     IYAATVFSSP TFTCISEVIQ NMNCNPNLIH IVYSLSKDMG LPGLRVGIVY SYNDDVVNIG
     RKMSSFGLVS SQTQHMLPSM LLDEEFVARF LETSPKRLAK RHGVFTKGLE EVGINCLKSN
     AGLFCWMDLR RLLEDQTFDG EMVLWRVIVN EVGPNVSPGS SFKCVEPGWF RVCFANMDDE
     TLEVALKRIR TFVRQGKKAQ DQVVQVKSPK RWKSNLRLSF SSSSTRRFDQ ESVNVLSPHM
     MSPHSPLVRA KT