ID   1A14_SOLLC              Reviewed;         476 AA.
AC   P29535; Q42894;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   02-SEP-2026, entry version 144.
DE   RecName: Full=1-aminocyclopropane-1-carboxylate synthase 4;
DE            Short=ACC synthase 4;
DE            EC=4.4.1.14;
DE   AltName: Full=Le-ACS4;
DE            Short=ACS-4;
DE   AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 4;
GN   Name=ACS4; Synonyms=ACC4, BTAS4, PCVV4B;
OS   Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum;
OC   Solanum subgen. Lycopersicon.
OX   NCBI_TaxID=4081;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. Caruso; TISSUE=Etiolated hypocotyl;
RX   PubMed=8366090; DOI=10.1016/s0021-9258(19)36532-9;
RA   Lincoln J.E., Campbell A.D., Oetiker J., Rottmann W.H., Oeller P.W.,
RA   Shen N.F., Theologis A.;
RT   "LE-ACS4, a fruit ripening and wound-induced 1-aminocyclopropane-1-
RT   carboxylate synthase gene of tomato (Lycopersicon esculentum). Expression
RT   in Escherichia coli, structural characterization, expression
RT   characteristics, and phylogenetic analysis.";
RL   J. Biol. Chem. 268:19422-19430(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Etiolated hypocotyl;
RX   PubMed=1762159; DOI=10.1016/0022-2836(91)90587-v;
RA   Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F., Nagy B.P.,
RA   Taylor L.P., Campbell A.D., Theologis A.;
RT   "1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a
RT   multigene family whose transcription is induced during fruit and floral
RT   senescence.";
RL   J. Mol. Biol. 222:937-961(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1711229; DOI=10.1073/pnas.88.12.5340;
RA   Olson D.C., White J.A., Edelman L., Harkins R.N., Kende H.;
RT   "Differential expression of two genes for 1-aminocyclopropane-1-carboxylate
RT   synthase in tomato fruits.";
RL   Proc. Natl. Acad. Sci. U.S.A. 88:5340-5344(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 20-159.
RC   STRAIN=cv. Orlando; TISSUE=Fruit;
RX   PubMed=2191304; DOI=10.1073/pnas.87.12.4859;
RA   van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.;
RT   "Cloning and sequence of two different cDNAs encoding 1-aminocyclopropane-
RT   1-carboxylate synthase in tomato.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 235-307, AND INDUCTION.
RC   TISSUE=Pericarp;
RX   PubMed=1549612; DOI=10.1073/pnas.89.6.2475;
RA   Yip W.K., Moore T., Yang S.F.;
RT   "Differential accumulation of transcripts for four tomato 1-
RT   aminocyclopropane-1-carboxylate synthase homologs under various
RT   conditions.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2475-2479(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         S-methyl-5'-thioadenosine + H(+); 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: Associated with fruit ripening, but unresponsive to auxin
CC       treatment in vegetative tissue. {ECO:0000269|PubMed:1549612}.
CC   -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000305}.
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DR   EMBL; M88487; AAA03164.1; -; Unassigned_DNA.
DR   EMBL; X59146; CAA41857.1; -; mRNA.
DR   EMBL; M63490; AAA34131.1; -; mRNA.
DR   EMBL; M38705; AAA81581.1; -; mRNA.
DR   EMBL; M83329; AAA68623.1; -; mRNA.
DR   PIR; S19679; S19679.
DR   RefSeq; NP_001233875.1; NM_001246946.1.
DR   AlphaFoldDB; P29535; -.
DR   SMR; P29535; -.
DR   FunCoup; P29535; 314.
DR   STRING; 4081.P29535; -.
DR   PaxDb; 4081-P29535; -.
DR   GeneID; 778356; -.
DR   KEGG; sly:778356; -.
DR   eggNOG; KOG0256; Eukaryota.
DR   InParanoid; P29535; -.
DR   OrthoDB; 691673at2759; -.
DR   UniPathway; UPA00384; UER00562.
DR   Proteomes; UP000004994; 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   CDD; cd00609; AAT_like; 1.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR004839; Aminotransferase_I/II_large.
DR   InterPro; IPR050478; Ethylene_sulfur-biosynth.
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   PANTHER; PTHR43795:SF42; 1-AMINOCYCLOPROPANE-1-CARBOXYLATE SYNTHASE 4; 1.
DR   PANTHER; PTHR43795; BIFUNCTIONAL ASPARTATE AMINOTRANSFERASE AND GLUTAMATE/ASPARTATE-PREPHENATE AMINOTRANSFERASE-RELATED; 1.
DR   Pfam; PF00155; Aminotran_1_2; 1.
DR   PRINTS; PR00753; ACCSYNTHASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 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..476
FT                   /note="1-aminocyclopropane-1-carboxylate synthase 4"
FT                   /id="PRO_0000123914"
FT   MOD_RES         282
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        15
FT                   /note="V -> A (in Ref. 2; CAA41857)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        82
FT                   /note="T -> A (in Ref. 4; AAA81581)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        253
FT                   /note="S -> P (in Ref. 2; CAA41857 and 5; AAA68623)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   476 AA;  53537 MW;  9BC7D97BD64CB044 CRC64;
     MDLETSEISN YKSSVVLSKL ASNEQHGENS PYFDGWKAYD NDPFHLVNNL NGVIQMGLAE
     NQLSVDLIEE WIKRNPKASI CTNDGIESFR RIANFQDYHG LPEFTNAIAK FMEKTRGGKV
     KFDAKRVVMA GGATGANETL ILCLADPGDA FLVPTPYYPG FNRDLRWRSG VQLLPISCKS
     CNNFKITIEA IEEAYEKGQQ ANVKIKGLIL TNPCNPLGTI LDRDTLKKIS TFTNEHNIHL
     VCDEIYAATV FNSPKFVSIA EIINEDNCIN KDLVHIVSSL SKDLGFPGFR VGIVYSFNDD
     VVNCARKMSS FGLVSTQTQH LLAFMLSDDE FVEEFLIESA KRLRERYEKF TRGLEEIGIK
     CLESNAGVYC WMDLRSLLKE ATLDAEMSLW KLIINEVKLN VSPGSSFNCS EVGWFRVCFA
     NIDDQTMEIA LARIRMFMDA YNNVNKNGVM KNKHNGRGTT YDLTPQMGST MKMLLA
//