1A13_SOLLC
ID 1A13_SOLLC Reviewed; 469 AA.
AC Q42881; Q96571;
DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 3;
DE Short=ACC synthase 3;
DE EC=4.4.1.14;
DE AltName: Full=Le-ACS3;
DE Short=ACS-3;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 3;
GN Name=ACS3;
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 [GENOMIC DNA].
RC STRAIN=cv. VFN8; TISSUE=Leaf, and Root;
RX PubMed=7775465; DOI=10.1074/jbc.270.23.14056;
RA Olson D.C., Oetiker J.H., Yang S.F.;
RT "Analysis of LE-ACS3, a 1-aminocyclopropane-1-carboxylic acid synthase gene
RT expressed during flooding in the roots of tomato plants.";
RL J. Biol. Chem. 270:14056-14061(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Rutgers;
RA Kawakita K., Hennig L., Rottmann W.R., Yu G.X., Zarembinski T.I.,
RA Taylor L.D., Theologis A.;
RT "The tomato 1-aminocyclopropane-1-carboxylate (ACC) synthase multigene
RT family is encoded by at least eight members.";
RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2122449; DOI=10.1073/pnas.87.20.7930;
RA Yip W.K., Dong J.G., Kenny J.W., Thompson G.A., Yang S.F.;
RT "Characterization and sequencing of the active site of 1-aminocyclopropane-
RT 1-carboxylate synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:7930-7934(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. {ECO:0000250}.
CC -!- INDUCTION: By flooding.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; L34171; AAA78789.1; -; Genomic_DNA.
DR EMBL; U18055; AAB48946.1; -; Genomic_DNA.
DR EMBL; U17972; AAB48945.1; -; mRNA.
DR PIR; A57540; A57540.
DR RefSeq; NP_001234026.2; NM_001247097.2.
DR AlphaFoldDB; Q42881; -.
DR SMR; Q42881; -.
DR STRING; 4081.Solyc02g091990.2.1; -.
DR PaxDb; Q42881; -.
DR PRIDE; Q42881; -.
DR EnsemblPlants; Solyc02g091990.3.1; Solyc02g091990.3.1; Solyc02g091990.3.
DR GeneID; 778292; -.
DR Gramene; Solyc02g091990.3.1; Solyc02g091990.3.1; Solyc02g091990.3.
DR KEGG; sly:778292; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; Q42881; -.
DR OMA; EEFGWFR; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; Q42881; -.
DR BRENDA; 4.4.1.14; 3101.
DR UniPathway; UPA00384; UER00562.
DR Proteomes; UP000004994; Chromosome 2.
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 1: Evidence at protein level;
KW Direct protein sequencing; Ethylene biosynthesis; Fruit ripening; Lyase;
KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..469
FT /note="1-aminocyclopropane-1-carboxylate synthase 3"
FT /id="PRO_0000123913"
FT REGION 432..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 272
FT /note="N6-(pyridoxal phosphate)lysine"
FT CONFLICT 243
FT /note="F -> L (in Ref. 2; AAB48945)"
FT /evidence="ECO:0000305"
FT CONFLICT 335
FT /note="K -> R (in Ref. 2; AAB48945)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 53094 MW; FA5ADCCE3F54F5BC CRC64;
MKLLSEKATC NSHGQDSSYF LGWQEYEKNP YDEIQNPKGI IQMGLAENQL SFDLLESWLA
QNPDAAGFKR NGESIFRELA LFQDYHGLPA FKNAMTKFMS EIRGNRVSFD SNNLVLTAGA
TSANETLMFC LANQGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FRITESALEE
AYLDAKKRNL KVKGVLVTNP SNPLGTTLNR NELELLLTFI DEKGIHLISD EIYSGTVFNS
PGFVSVMEVL IEKNYMKTRV WERVHIVYSL SKDLGLPGFR IGAIYSNDEM VVSAATKMSS
FGLVSSQTQY LLSCMLSDKK FTKKYISENQ KRLKKRHAML VKGLKSAGIN CLESNAGLFC
WVDMRHLLSS NNFDAEMDLW KKIVYDVGLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA
MRRIKDFVES TAPNATNHQN QQQSNANSKK KSFSKWVFRL SFNDRQRER
