1A12_SOLLC
ID 1A12_SOLLC Reviewed; 485 AA.
AC P18485;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=1-aminocyclopropane-1-carboxylate synthase 2;
DE Short=ACC synthase 2;
DE EC=4.4.1.14;
DE AltName: Full=Le-ACS2;
DE Short=ACS-2;
DE AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 2;
GN Name=ACS2; Synonyms=ACC2, PCVV4A;
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 / 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
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 [3]
RP HOMODIMERIZATION, AND MUTAGENESIS OF TYR-92 AND LYS-278.
RX PubMed=9575209; DOI=10.1074/jbc.273.20.12509;
RA Tarun A.S., Theologis A.;
RT "Complementation analysis of mutants of 1-aminocyclopropane-1-carboxylate
RT synthase reveals the enzyme is a dimer with shared active sites.";
RL J. Biol. Chem. 273:12509-12514(1998).
RN [4]
RP MUTAGENESIS OF ARG-286.
RX PubMed=10557240; DOI=10.1104/pp.121.3.913;
RA Zhou H., Wang H.W., Zhu K., Sui S.F., Xu P., Yang S.F., Li N.;
RT "The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-
RT carboxylate synthase. Coenzyme binding, substrate binding, and beyond.";
RL Plant Physiol. 121:913-919(1999).
RN [5]
RP PHOSPHORYLATION AT SER-460.
RX PubMed=11375393; DOI=10.1074/jbc.m101543200;
RA Tatsuki M., Mori H.;
RT "Phosphorylation of tomato 1-aminocyclopropane-1-carboxylic acid synthase,
RT LE-ACS2, at the C-terminal region.";
RL J. Biol. Chem. 276:28051-28057(2001).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-438.
RX PubMed=11431475; DOI=10.1074/jbc.m103840200;
RA Huai Q., Xia Y., Chen Y., Callahan B., Li N., Ke H.;
RT "Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in
RT complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new
RT insight into catalytic mechanisms.";
RL J. Biol. Chem. 276:38210-38216(2001).
CC -!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes
CC catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-
CC aminocyclopropane-1-carboxylate (ACC), a direct precursor of ethylene.
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 and heterodimer. In vivo, the relevance of
CC heterodimerization with other ACS enzymes is however unsure.
CC -!- INDUCTION: Hormones, such as auxin, environmental factors, such as
CC mechanical wounding and a number of chemicals.
CC -!- PTM: Phosphorylated on Ser 460; phosphorylation may regulate its
CC turnover. {ECO:0000269|PubMed:11375393}.
CC -!- PTM: May be processed at its C-terminus.
CC -!- MISCELLANEOUS: The stability of ACS proteins, and the regulation of
CC such stability, play a central role in ethylene biosynthesis.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; X59139; CAA41855.1; -; Genomic_DNA.
DR EMBL; X59145; CAA41856.1; -; mRNA.
DR EMBL; M34289; AAA81580.1; -; mRNA.
DR PIR; S19677; S19677.
DR RefSeq; NP_001234178.2; NM_001247249.2.
DR PDB; 1IAX; X-ray; 2.80 A; A/B=11-438.
DR PDB; 1IAY; X-ray; 2.70 A; A=11-438.
DR PDBsum; 1IAX; -.
DR PDBsum; 1IAY; -.
DR AlphaFoldDB; P18485; -.
DR SMR; P18485; -.
DR STRING; 4081.Solyc01g095080.2.1; -.
DR iPTMnet; P18485; -.
DR PaxDb; P18485; -.
DR PRIDE; P18485; -.
DR EnsemblPlants; Solyc01g095080.3.1; Solyc01g095080.3.1; Solyc01g095080.3.
DR GeneID; 606304; -.
DR Gramene; Solyc01g095080.3.1; Solyc01g095080.3.1; Solyc01g095080.3.
DR KEGG; sly:606304; -.
DR eggNOG; KOG0256; Eukaryota.
DR HOGENOM; CLU_017584_1_0_1; -.
DR InParanoid; P18485; -.
DR OMA; EMSHCNK; -.
DR OrthoDB; 1156861at2759; -.
DR PhylomeDB; P18485; -.
DR BRENDA; 4.4.1.14; 3101.
DR UniPathway; UPA00384; UER00562.
DR EvolutionaryTrace; P18485; -.
DR Proteomes; UP000004994; Chromosome 1.
DR ExpressionAtlas; P18485; baseline and differential.
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 3D-structure; Direct protein sequencing; Ethylene biosynthesis;
KW Fruit ripening; Lyase; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..485
FT /note="1-aminocyclopropane-1-carboxylate synthase 2"
FT /id="PRO_0000123912"
FT BINDING 55
FT /ligand="substrate"
FT BINDING 92
FT /ligand="substrate"
FT MOD_RES 278
FT /note="N6-(pyridoxal phosphate)lysine"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11375393"
FT MUTAGEN 92
FT /note="Y->F: Loss of function; when expressed alone in
FT E.Coli. Partially complemented; when coexpressed with
FT another ACS2 protein mutated on K-278."
FT /evidence="ECO:0000269|PubMed:9575209"
FT MUTAGEN 278
FT /note="K->A: Loss of function; when expressed alone in
FT E.Coli. Partially complemented; when coexpressed with
FT another ACS2 protein mutated on Y-72."
FT /evidence="ECO:0000269|PubMed:9575209"
FT MUTAGEN 286
FT /note="R->L: Loss of function; due to a strong reduction in
FT both substrate and pyridoxal phosphate binding."
FT /evidence="ECO:0000269|PubMed:10557240"
FT MUTAGEN 460
FT /note="S->G: Abolishes phosphorylation."
FT MUTAGEN 462
FT /note="S->G: No effect."
FT CONFLICT 124
FT /note="A -> V (in Ref. 1; CAA41856)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="L -> P (in Ref. 2; AAA81580)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="P -> L (in Ref. 2; AAA81580)"
FT /evidence="ECO:0000305"
FT HELIX 16..18
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 29..36
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 60..69
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 83..88
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 96..109
FT /evidence="ECO:0007829|PDB:1IAY"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 118..120
FT /evidence="ECO:0007829|PDB:1IAX"
FT STRAND 122..125
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 126..138
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 155..158
FT /evidence="ECO:0007829|PDB:1IAY"
FT TURN 159..163
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:1IAY"
FT TURN 174..178
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 182..194
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:1IAY"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 217..228
FT /evidence="ECO:0007829|PDB:1IAY"
FT TURN 229..231
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 233..237
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 253..257
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 260..262
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 269..276
FT /evidence="ECO:0007829|PDB:1IAY"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 295..305
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 312..321
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 325..352
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 361..369
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 375..378
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 379..391
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 400..403
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 406..414
FT /evidence="ECO:0007829|PDB:1IAY"
FT STRAND 416..418
FT /evidence="ECO:0007829|PDB:1IAY"
FT HELIX 420..435
FT /evidence="ECO:0007829|PDB:1IAY"
SQ SEQUENCE 485 AA; 54663 MW; 40B3F55B5EF0D9C7 CRC64;
MGFEIAKTNS ILSKLATNEE HGENSPYFDG WKAYDSDPFH PLKNPNGVIQ MGLAENQLCL
DLIEDWIKRN PKGSICSEGI KSFKAIANFQ DYHGLPEFRK AIAKFMEKTR GGRVRFDPER
VVMAGGATGA NETIIFCLAD PGDAFLVPSP YYPAFNRDLR WRTGVQLIPI HCESSNNFKI
TSKAVKEAYE NAQKSNIKVK GLILTNPSNP LGTTLDKDTL KSVLSFTNQH NIHLVCDEIY
AATVFDTPQF VSIAEILDEQ EMTYCNKDLV HIVYSLSKDM GLPGFRVGII YSFNDDVVNC
ARKMSSFGLV STQTQYFLAA MLSDEKFVDN FLRESAMRLG KRHKHFTNGL EVVGIKCLKN
NAGLFCWMDL RPLLRESTFD SEMSLWRVII NDVKLNVSPG SSFECQEPGW FRVCFANMDD
GTVDIALARI RRFVGVEKSG DKSSSMEKKQ QWKKNNLRLS FSKRMYDESV LSPLSSPIPP
SPLVR
