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1-aminocyclopropane-1-carboxylate synthase 2 (ACC synthase 2) (EC 4.4.1.14) (Le-ACS2) (ACS-2) (S-adenosyl-L-methionine methylthioadenosine-lyase 2)

 1A12_SOLLC              Reviewed;         485 AA.
P18485;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 2.
23-MAY-2018, entry version 131.
RecName: Full=1-aminocyclopropane-1-carboxylate synthase 2;
Short=ACC synthase 2;
EC=4.4.1.14;
AltName: Full=Le-ACS2;
Short=ACS-2;
AltName: Full=S-adenosyl-L-methionine methylthioadenosine-lyase 2;
Name=ACS2; Synonyms=ACC2, PCVV4A;
Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
Solaneae; Solanum; Lycopersicon.
NCBI_TaxID=4081;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Etiolated hypocotyl;
PubMed=1762159; DOI=10.1016/0022-2836(91)90587-V;
Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F.,
Nagy B.P., Taylor L.P., Campbell A.D., Theologis A.;
"1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a
multigene family whose transcription is induced during fruit and
floral senescence.";
J. Mol. Biol. 222:937-961(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. Orlando; TISSUE=Fruit;
PubMed=2191304; DOI=10.1073/pnas.87.12.4859;
van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.;
"Cloning and sequence of two different cDNAs encoding 1-
aminocyclopropane-1-carboxylate synthase in tomato.";
Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990).
[3]
HOMODIMERIZATION, AND MUTAGENESIS OF TYR-92 AND LYS-278.
PubMed=9575209; DOI=10.1074/jbc.273.20.12509;
Tarun A.S., Theologis A.;
"Complementation analysis of mutants of 1-aminocyclopropane-1-
carboxylate synthase reveals the enzyme is a dimer with shared active
sites.";
J. Biol. Chem. 273:12509-12514(1998).
[4]
MUTAGENESIS OF ARG-286.
PubMed=10557240; DOI=10.1104/pp.121.3.913;
Zhou H., Wang H.W., Zhu K., Sui S.F., Xu P., Yang S.F., Li N.;
"The multiple roles of conserved arginine 286 of 1-aminocyclopropane-
1-carboxylate synthase. Coenzyme binding, substrate binding, and
beyond.";
Plant Physiol. 121:913-919(1999).
[5]
PHOSPHORYLATION AT SER-460.
PubMed=11375393; DOI=10.1074/jbc.M101543200;
Tatsuki M., Mori H.;
"Phosphorylation of tomato 1-aminocyclopropane-1-carboxylic acid
synthase, LE-ACS2, at the C-terminal region.";
J. Biol. Chem. 276:28051-28057(2001).
[6]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-438.
PubMed=11431475; DOI=10.1074/jbc.M103840200;
Huai Q., Xia Y., Chen Y., Callahan B., Li N., Ke H.;
"Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC)
synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-
phosphate provide new insight into catalytic mechanisms.";
J. Biol. Chem. 276:38210-38216(2001).
-!- FUNCTION: 1-aminocyclopropane-1-carboxylate synthase (ACS) enzymes
catalyze the conversion of S-adenosyl-L-methionine (SAM) into 1-
aminocyclopropane-1-carboxylate (ACC), a direct precursor of
ethylene.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = 1-aminocyclopropane-
1-carboxylate + methylthioadenosine.
-!- COFACTOR:
Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
-!- PATHWAY: Alkene biosynthesis; ethylene biosynthesis via S-
adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step
1/2.
-!- SUBUNIT: Homodimer and heterodimer. In vivo, the relevance of
heterodimerization with other ACS enzymes is however unsure.
-!- INDUCTION: Hormones, such as auxin, environmental factors, such as
mechanical wounding and a number of chemicals.
-!- PTM: Phosphorylated on Ser 460; phosphorylation may regulate its
turnover. {ECO:0000269|PubMed:11375393}.
-!- PTM: May be processed at its C-terminus.
-!- MISCELLANEOUS: The stability of ACS proteins, and the regulation
of such stability, play a central role in ethylene biosynthesis.
-!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
aminotransferase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X59139; CAA41855.1; -; Genomic_DNA.
EMBL; X59145; CAA41856.1; -; mRNA.
EMBL; M34289; AAA81580.1; -; mRNA.
PIR; S19677; S19677.
RefSeq; NP_001234178.2; NM_001247249.2.
UniGene; Les.25919; -.
UniGene; Les.3662; -.
PDB; 1IAX; X-ray; 2.80 A; A/B=11-438.
PDB; 1IAY; X-ray; 2.70 A; A=11-438.
PDBsum; 1IAX; -.
PDBsum; 1IAY; -.
ProteinModelPortal; P18485; -.
SMR; P18485; -.
STRING; 4081.Solyc01g095080.2.1; -.
iPTMnet; P18485; -.
PaxDb; P18485; -.
PRIDE; P18485; -.
EnsemblPlants; Solyc01g095080.2.1; Solyc01g095080.2.1; Solyc01g095080.2.
GeneID; 606304; -.
Gramene; Solyc01g095080.2.1; Solyc01g095080.2.1; Solyc01g095080.2.
KEGG; sly:606304; -.
eggNOG; KOG0256; Eukaryota.
eggNOG; COG0436; LUCA.
InParanoid; P18485; -.
KO; K20772; -.
OMA; HFMGKAR; -.
OrthoDB; EOG0936082N; -.
BRENDA; 4.4.1.14; 3101.
UniPathway; UPA00384; UER00562.
EvolutionaryTrace; P18485; -.
Proteomes; UP000004994; Chromosome 1.
ExpressionAtlas; P18485; baseline and differential.
GO; GO:0016847; F:1-aminocyclopropane-1-carboxylate synthase activity; IEA:UniProtKB-EC.
GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
GO; GO:0009693; P:ethylene biosynthetic process; IEA:UniProtKB-UniPathway.
GO; GO:0009835; P:fruit ripening; IEA:UniProtKB-KW.
Gene3D; 3.40.640.10; -; 1.
Gene3D; 3.90.1150.10; -; 2.
InterPro; IPR004839; Aminotransferase_I/II.
InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
InterPro; IPR015424; PyrdxlP-dep_Trfase.
InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
Pfam; PF00155; Aminotran_1_2; 1.
SUPFAM; SSF53383; SSF53383; 1.
PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Direct protein sequencing;
Ethylene biosynthesis; Fruit ripening; Lyase; Phosphoprotein;
Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine.
CHAIN 1 485 1-aminocyclopropane-1-carboxylate
synthase 2.
/FTId=PRO_0000123912.
BINDING 55 55 Substrate.
BINDING 92 92 Substrate.
MOD_RES 278 278 N6-(pyridoxal phosphate)lysine.
MOD_RES 460 460 Phosphoserine.
{ECO:0000269|PubMed:11375393}.
MUTAGEN 92 92 Y->F: Loss of function; when expressed
alone in E.Coli. Partially complemented;
when coexpressed with another ACS2
protein mutated on K-278.
{ECO:0000269|PubMed:9575209}.
MUTAGEN 278 278 K->A: Loss of function; when expressed
alone in E.Coli. Partially complemented;
when coexpressed with another ACS2
protein mutated on Y-72.
{ECO:0000269|PubMed:9575209}.
MUTAGEN 286 286 R->L: Loss of function; due to a strong
reduction in both substrate and pyridoxal
phosphate binding.
{ECO:0000269|PubMed:10557240}.
MUTAGEN 460 460 S->G: Abolishes phosphorylation.
MUTAGEN 462 462 S->G: No effect.
CONFLICT 124 124 A -> V (in Ref. 1; CAA41856).
{ECO:0000305}.
CONFLICT 322 322 L -> P (in Ref. 2; AAA81580).
{ECO:0000305}.
CONFLICT 399 399 P -> L (in Ref. 2; AAA81580).
{ECO:0000305}.
HELIX 16 18 {ECO:0000244|PDB:1IAY}.
HELIX 29 36 {ECO:0000244|PDB:1IAY}.
STRAND 41 44 {ECO:0000244|PDB:1IAY}.
STRAND 47 50 {ECO:0000244|PDB:1IAY}.
HELIX 60 69 {ECO:0000244|PDB:1IAY}.
HELIX 83 88 {ECO:0000244|PDB:1IAY}.
HELIX 96 109 {ECO:0000244|PDB:1IAY}.
TURN 110 112 {ECO:0000244|PDB:1IAY}.
HELIX 118 120 {ECO:0000244|PDB:1IAX}.
STRAND 122 125 {ECO:0000244|PDB:1IAY}.
HELIX 126 138 {ECO:0000244|PDB:1IAY}.
STRAND 144 150 {ECO:0000244|PDB:1IAY}.
HELIX 155 158 {ECO:0000244|PDB:1IAY}.
TURN 159 163 {ECO:0000244|PDB:1IAY}.
STRAND 166 170 {ECO:0000244|PDB:1IAY}.
TURN 174 178 {ECO:0000244|PDB:1IAY}.
HELIX 182 194 {ECO:0000244|PDB:1IAY}.
STRAND 199 207 {ECO:0000244|PDB:1IAY}.
TURN 209 211 {ECO:0000244|PDB:1IAY}.
HELIX 217 228 {ECO:0000244|PDB:1IAY}.
TURN 229 231 {ECO:0000244|PDB:1IAY}.
STRAND 233 237 {ECO:0000244|PDB:1IAY}.
HELIX 241 243 {ECO:0000244|PDB:1IAY}.
STRAND 246 248 {ECO:0000244|PDB:1IAY}.
HELIX 253 257 {ECO:0000244|PDB:1IAY}.
HELIX 260 262 {ECO:0000244|PDB:1IAY}.
STRAND 269 276 {ECO:0000244|PDB:1IAY}.
TURN 277 279 {ECO:0000244|PDB:1IAY}.
HELIX 283 285 {ECO:0000244|PDB:1IAY}.
STRAND 287 293 {ECO:0000244|PDB:1IAY}.
HELIX 295 305 {ECO:0000244|PDB:1IAY}.
HELIX 312 321 {ECO:0000244|PDB:1IAY}.
HELIX 325 352 {ECO:0000244|PDB:1IAY}.
STRAND 361 369 {ECO:0000244|PDB:1IAY}.
HELIX 371 373 {ECO:0000244|PDB:1IAY}.
STRAND 375 378 {ECO:0000244|PDB:1IAY}.
HELIX 379 391 {ECO:0000244|PDB:1IAY}.
HELIX 400 403 {ECO:0000244|PDB:1IAY}.
STRAND 406 414 {ECO:0000244|PDB:1IAY}.
STRAND 416 418 {ECO:0000244|PDB:1IAY}.
HELIX 420 435 {ECO:0000244|PDB:1IAY}.
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


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