ID   1A1C_VIGRR              Reviewed;         368 AA.
AC   Q01912;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase;
DE            Short=ACC synthase;
DE            EC=4.4.1.14;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase;
DE   Flags: Fragment;
GN   Name=ACS5;
OS   Vigna radiata var. radiata (Mung bean) (Phaseolus aureus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX   NCBI_TaxID=3916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Berken / Rwilcz; TISSUE=Hypocotyl;
RX   PubMed=1421146; DOI=10.1007/bf00040602;
RA   Botella J.R., Arteca J.M., Schlagnhaufer C.D., Arteca R.N., Phillips A.T.;
RT   "Identification and characterization of a full-length cDNA encoding for an
RT   auxin-induced 1-aminocyclopropane-1-carboxylate synthase from etiolated
RT   mung bean hypocotyl segments and expression of its mRNA in response to
RT   indole-3-acetic acid.";
RL   Plant Mol. Biol. 20:425-436(1992).
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}.
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DR   EMBL; Z11562; CAA77655.1; -; mRNA.
DR   AlphaFoldDB; Q01912; -.
DR   SMR; Q01912; -.
DR   STRING; 3916.Q01912; -.
DR   SABIO-RK; Q01912; -.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000087766; Genome assembly.
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..>368
FT                   /note="1-aminocyclopropane-1-carboxylate synthase"
FT                   /id="PRO_0000123917"
FT   MOD_RES         230
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         368
SQ   SEQUENCE   368 AA;  41477 MW;  31BA61D5FC2D4CB8 CRC64;
     QMGLAENQLT SDLVEDWILN NPEASICTPE GINDFRAIAN FQDYHGLAEF RNAVAKFMAR
     TRGNRITFDP DRIVMSGGAT GAHEVTAFCL ADPGEAFLVP IPYYPGFDRD LRWRTGVKLV
     PVMCDSSNNF VLTKEALEDA YEKAREDNIR VKGLLITNPS NPLGTIMDRK TLRTVVSFIN
     EKRIHLVCDE IYAATVFSQP GFISIAEILE DETDIECDRN LVHIVYSLSK DMGFPGFRVG
     IIYSYNDAVV NCARKMSSFG LVSTQTQYLL ASMLNDDEFV ERFLAESAKR LAQRFRVFTG
     GLAKVGIKCL QSNAGLFVWM DLRQLLKKPT FDSETELWKV IIHEVKINVS PGYSFHCTEP
     GWFRVCFA