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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)DescriptionActionsGraphical viewLength
Binding sitei55Substrate1
Binding sitei92Substrate1

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)DescriptionActionsGraphical viewLength
Mutagenesisi92Y → F: Loss of function; when expressed alone in E.Coli. Partially complemented; when coexpressed with another ACS2 protein mutated on K-278. 1 Publication1
Mutagenesisi278K → A: Loss of function; when expressed alone in E.Coli. Partially complemented; when coexpressed with another ACS2 protein mutated on Y-72. 1 Publication1
Mutagenesisi286R → L: Loss of function; due to a strong reduction in both substrate and pyridoxal phosphate binding. 1 Publication1
Mutagenesisi460S → G: Abolishes phosphorylation. 1
Mutagenesisi462S → G: No effect. 1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001239121 – 4851-aminocyclopropane-1-carboxylate synthase 2Add BLAST485

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei278N6-(pyridoxal phosphate)lysine1
Modified residuei460Phosphoserine1 Publication1

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

1485
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi16 – 18Combined sources3
Helixi29 – 36Combined sources8
Beta strandi41 – 44Combined sources4
Beta strandi47 – 50Combined sources4
Helixi60 – 69Combined sources10
Helixi83 – 88Combined sources6
Helixi96 – 109Combined sources14
Turni110 – 112Combined sources3
Helixi118 – 120Combined sources3
Beta strandi122 – 125Combined sources4
Helixi126 – 138Combined sources13
Beta strandi144 – 150Combined sources7
Helixi155 – 158Combined sources4
Turni159 – 163Combined sources5
Beta strandi166 – 170Combined sources5
Turni174 – 178Combined sources5
Helixi182 – 194Combined sources13
Beta strandi199 – 207Combined sources9
Turni209 – 211Combined sources3
Helixi217 – 228Combined sources12
Turni229 – 231Combined sources3
Beta strandi233 – 237Combined sources5
Helixi241 – 243Combined sources3
Beta strandi246 – 248Combined sources3
Helixi253 – 257Combined sources5
Helixi260 – 262Combined sources3
Beta strandi269 – 276Combined sources8
Turni277 – 279Combined sources3
Helixi283 – 285Combined sources3
Beta strandi287 – 293Combined sources7
Helixi295 – 305Combined sources11
Helixi312 – 321Combined sources10
Helixi325 – 352Combined sources28
Beta strandi361 – 369Combined sources9
Helixi371 – 373Combined sources3
Beta strandi375 – 378Combined sources4
Helixi379 – 391Combined sources13
Helixi400 – 403Combined sources4
Beta strandi406 – 414Combined sources9
Beta strandi416 – 418Combined sources3
Helixi420 – 435Combined sources16

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP18485.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
InParanoidiP18485.
KOiK20772.
OMAiDISALYH.
OrthoDBiEOG0936082N.

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)DescriptionActionsGraphical viewLength
Sequence conflicti124A → V in CAA41856 (PubMed:1762159).Curated1
Sequence conflicti322L → P in AAA81580 (PubMed:2191304).Curated1
Sequence conflicti399P → L in AAA81580 (PubMed:2191304).Curated1

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.25919.
Les.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.25919.
Les.3662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1IAXX-ray2.80A/B11-438[»]
1IAYX-ray2.70A11-438[»]
ProteinModelPortaliP18485.
SMRiP18485.
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.
KOiK20772.
OMAiDISALYH.
OrthoDBiEOG0936082N.

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...

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: November 30, 2016
This is version 125 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.