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Protein

1-aminocyclopropane-1-carboxylate synthase 2

Gene

ACS2

Organism
Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine.

Cofactori

Pathwayi: ethylene biosynthesis via S-adenosyl-L-methionine

This protein is involved in step 1 of the subpathway that synthesizes ethylene from S-adenosyl-L-methionine.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. 1-aminocyclopropane-1-carboxylate synthase 2 (ACS2), 1-aminocyclopropane-1-carboxylate synthase 3 (ACS3), 1-aminocyclopropane-1-carboxylate synthase 4 (ACS4)
  2. 1-aminocyclopropane-1-carboxylate oxidase 1 (ACO1), 1-aminocyclopropane-1-carboxylate oxidase 2 (ACO2), 1-aminocyclopropane-1-carboxylate oxidase 4 (ACO4)
This subpathway is part of the pathway ethylene biosynthesis via S-adenosyl-L-methionine, which is itself part of Alkene biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ethylene from S-adenosyl-L-methionine, the pathway ethylene biosynthesis via S-adenosyl-L-methionine and in Alkene biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei55 – 551Substrate
Binding sitei92 – 921Substrate

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Ethylene biosynthesis, Fruit ripening

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi4.4.1.14. 3101.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase 2 (EC:4.4.1.14)
Short name:
ACC synthase 2
Alternative name(s):
Le-ACS2
Short name:
ACS-2
S-adenosyl-L-methionine methylthioadenosine-lyase 2
Gene namesi
Name:ACS2
Synonyms:ACC2, PCVV4A
OrganismiSolanum lycopersicum (Tomato) (Lycopersicon esculentum)
Taxonomic identifieri4081 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanumLycopersicon
Proteomesi
  • UP000004994 Componenti: Chromosome 1

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi92 – 921Y → F: Loss of function; when expressed alone in E.Coli. Partially complemented; when coexpressed with another ACS2 protein mutated on K-278. 1 Publication
Mutagenesisi278 – 2781K → A: Loss of function; when expressed alone in E.Coli. Partially complemented; when coexpressed with another ACS2 protein mutated on Y-72. 1 Publication
Mutagenesisi286 – 2861R → L: Loss of function; due to a strong reduction in both substrate and pyridoxal phosphate binding. 1 Publication
Mutagenesisi460 – 4601S → G: Abolishes phosphorylation.
Mutagenesisi462 – 4621S → G: No effect.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4854851-aminocyclopropane-1-carboxylate synthase 2PRO_0000123912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei278 – 2781N6-(pyridoxal phosphate)lysine
Modified residuei460 – 4601Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on Ser 460; phosphorylation may regulate its turnover.1 Publication
May be processed at its C-terminus.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP18485.

PTM databases

iPTMnetiP18485.

Expressioni

Inductioni

Hormones, such as auxin, environmental factors, such as mechanical wounding and a number of chemicals.

Interactioni

Subunit structurei

Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure.

Protein-protein interaction databases

STRINGi4081.Solyc01g095080.2.1.

Structurei

Secondary structure

1
485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183Combined sources
Helixi29 – 368Combined sources
Beta strandi41 – 444Combined sources
Beta strandi47 – 504Combined sources
Helixi60 – 6910Combined sources
Helixi83 – 886Combined sources
Helixi96 – 10914Combined sources
Turni110 – 1123Combined sources
Helixi118 – 1203Combined sources
Beta strandi122 – 1254Combined sources
Helixi126 – 13813Combined sources
Beta strandi144 – 1507Combined sources
Helixi155 – 1584Combined sources
Turni159 – 1635Combined sources
Beta strandi166 – 1705Combined sources
Turni174 – 1785Combined sources
Helixi182 – 19413Combined sources
Beta strandi199 – 2079Combined sources
Turni209 – 2113Combined sources
Helixi217 – 22812Combined sources
Turni229 – 2313Combined sources
Beta strandi233 – 2375Combined sources
Helixi241 – 2433Combined sources
Beta strandi246 – 2483Combined sources
Helixi253 – 2575Combined sources
Helixi260 – 2623Combined sources
Beta strandi269 – 2768Combined sources
Turni277 – 2793Combined sources
Helixi283 – 2853Combined sources
Beta strandi287 – 2937Combined sources
Helixi295 – 30511Combined sources
Helixi312 – 32110Combined sources
Helixi325 – 35228Combined sources
Beta strandi361 – 3699Combined sources
Helixi371 – 3733Combined sources
Beta strandi375 – 3784Combined sources
Helixi379 – 39113Combined sources
Helixi400 – 4034Combined sources
Beta strandi406 – 4149Combined sources
Beta strandi416 – 4183Combined sources
Helixi420 – 43516Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IAXX-ray2.80A/B11-438[»]
1IAYX-ray2.70A11-438[»]
ProteinModelPortaliP18485.
SMRiP18485. Positions 11-438.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18485.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
InParanoidiP18485.
KOiK01762.
OMAiDISALYH.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P18485-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGFEIAKTNS ILSKLATNEE HGENSPYFDG WKAYDSDPFH PLKNPNGVIQ
60 70 80 90 100
MGLAENQLCL DLIEDWIKRN PKGSICSEGI KSFKAIANFQ DYHGLPEFRK
110 120 130 140 150
AIAKFMEKTR GGRVRFDPER VVMAGGATGA NETIIFCLAD PGDAFLVPSP
160 170 180 190 200
YYPAFNRDLR WRTGVQLIPI HCESSNNFKI TSKAVKEAYE NAQKSNIKVK
210 220 230 240 250
GLILTNPSNP LGTTLDKDTL KSVLSFTNQH NIHLVCDEIY AATVFDTPQF
260 270 280 290 300
VSIAEILDEQ EMTYCNKDLV HIVYSLSKDM GLPGFRVGII YSFNDDVVNC
310 320 330 340 350
ARKMSSFGLV STQTQYFLAA MLSDEKFVDN FLRESAMRLG KRHKHFTNGL
360 370 380 390 400
EVVGIKCLKN NAGLFCWMDL RPLLRESTFD SEMSLWRVII NDVKLNVSPG
410 420 430 440 450
SSFECQEPGW FRVCFANMDD GTVDIALARI RRFVGVEKSG DKSSSMEKKQ
460 470 480
QWKKNNLRLS FSKRMYDESV LSPLSSPIPP SPLVR
Length:485
Mass (Da):54,663
Last modified:October 1, 1994 - v2
Checksum:i40B3F55B5EF0D9C7
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241A → V in CAA41856 (PubMed:1762159).Curated
Sequence conflicti322 – 3221L → P in AAA81580 (PubMed:2191304).Curated
Sequence conflicti399 – 3991P → L in AAA81580 (PubMed:2191304).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59139 Genomic DNA. Translation: CAA41855.1.
X59145 mRNA. Translation: CAA41856.1.
M34289 mRNA. Translation: AAA81580.1.
PIRiS19677.
RefSeqiNP_001234178.2. NM_001247249.2.
UniGeneiLes.3662.

Genome annotation databases

EnsemblPlantsiSolyc01g095080.2.1; Solyc01g095080.2.1; Solyc01g095080.2.
GeneIDi606304.
GrameneiSolyc01g095080.2.1; Solyc01g095080.2.1; Solyc01g095080.2.
KEGGisly:606304.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X59139 Genomic DNA. Translation: CAA41855.1.
X59145 mRNA. Translation: CAA41856.1.
M34289 mRNA. Translation: AAA81580.1.
PIRiS19677.
RefSeqiNP_001234178.2. NM_001247249.2.
UniGeneiLes.3662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1IAXX-ray2.80A/B11-438[»]
1IAYX-ray2.70A11-438[»]
ProteinModelPortaliP18485.
SMRiP18485. Positions 11-438.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi4081.Solyc01g095080.2.1.

PTM databases

iPTMnetiP18485.

Proteomic databases

PaxDbiP18485.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiSolyc01g095080.2.1; Solyc01g095080.2.1; Solyc01g095080.2.
GeneIDi606304.
GrameneiSolyc01g095080.2.1; Solyc01g095080.2.1; Solyc01g095080.2.
KEGGisly:606304.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
InParanoidiP18485.
KOiK01762.
OMAiDISALYH.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
BRENDAi4.4.1.14. 3101.

Miscellaneous databases

EvolutionaryTraceiP18485.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
InterProiIPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00155. Aminotran_1_2. 1 hit.
[Graphical view]
SUPFAMiSSF53383. SSF53383. 1 hit.
PROSITEiPS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a multigene family whose transcription is induced during fruit and floral senescence."
    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.
    J. Mol. Biol. 222:937-961(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Etiolated hypocotyl.
  2. "Cloning and sequence of two different cDNAs encoding 1-aminocyclopropane-1-carboxylate synthase in tomato."
    van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.
    Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: cv. Orlando.
    Tissue: Fruit.
  3. "Complementation analysis of mutants of 1-aminocyclopropane-1-carboxylate synthase reveals the enzyme is a dimer with shared active sites."
    Tarun A.S., Theologis A.
    J. Biol. Chem. 273:12509-12514(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, MUTAGENESIS OF TYR-92 AND LYS-278.
  4. "The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-carboxylate synthase. Coenzyme binding, substrate binding, and beyond."
    Zhou H., Wang H.W., Zhu K., Sui S.F., Xu P., Yang S.F., Li N.
    Plant Physiol. 121:913-919(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-286.
  5. "Phosphorylation of tomato 1-aminocyclopropane-1-carboxylic acid synthase, LE-ACS2, at the C-terminal region."
    Tatsuki M., Mori H.
    J. Biol. Chem. 276:28051-28057(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-460.
  6. "Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms."
    Huai Q., Xia Y., Chen Y., Callahan B., Li N., Ke H.
    J. Biol. Chem. 276:38210-38216(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-438.

Entry informationi

Entry namei1A12_SOLLC
AccessioniPrimary (citable) accession number: P18485
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: October 1, 1994
Last modified: March 16, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

The stability of ACS proteins, and the regulation of such stability, play a central role in ethylene biosynthesis.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.