1A14_SOLLC
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 03-AUG-2022, entry version 130.
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 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: 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 RefSeq; NP_001234280.1; NM_001247351.1.
DR AlphaFoldDB; P29535; -.
DR SMR; P29535; -.
DR STRING; 4081.Solyc05g050010.2.1; -.
DR PaxDb; P29535; -.
DR PRIDE; P29535; -.
DR GeneID; 778356; -.
DR KEGG; sly:778356; -.
DR eggNOG; KOG0256; Eukaryota.
DR InParanoid; P29535; -.
DR OrthoDB; 1156861at2759; -.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000004994; Unplaced.
DR ExpressionAtlas; P29535; baseline.
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:0008483; F:transaminase activity; IBA:GO_Central.
DR GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
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..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
