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Protein

1-aminocyclopropane-1-carboxylate synthase 6

Gene

ACS6

Organism
Arabidopsis thaliana (Mouse-ear cress)
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. Involved in bacterial flagellin-induced ethylene production.1 Publication

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=23 µM for AdoMet
  1. Vmax=120.60 µM/h/mg enzyme

pH dependencei

Optimum pH is 7.3.

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 8 (ACS8), 1-aminocyclopropane-1-carboxylate synthase 4 (ACS4), 1-aminocyclopropane-1-carboxylate synthase 2 (ACS2), 1-aminocyclopropane-1-carboxylate synthase 7 (ACS7), 1-aminocyclopropane-1-carboxylate synthase 11 (ACS11), 1-aminocyclopropane-1-carboxylate synthase 9 (ACS9), 1-aminocyclopropane-1-carboxylate synthase 6 (ACS6), 1-aminocyclopropane-1-carboxylate synthase 5 (ACS5)
  2. 1-aminocyclopropane-1-carboxylate oxidase 2 (ACO2), 1-aminocyclopropane-1-carboxylate oxidase 3 (At1g12010), 1-aminocyclopropane-1-carboxylate oxidase 4 (ACO4), 1-aminocyclopropane-1-carboxylate oxidase 1 (ACO1), 1-aminocyclopropane-1-carboxylate oxidase 5 (At1g77330)
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 sitei58 – 581SubstrateBy similarity
Binding sitei96 – 961SubstrateBy similarity

GO - Molecular functioni

  • 1-aminocyclopropane-1-carboxylate synthase activity Source: TAIR
  • identical protein binding Source: IntAct
  • pyridoxal phosphate binding Source: InterPro

GO - Biological processi

  • 1-aminocyclopropane-1-carboxylate biosynthetic process Source: GOC
  • cell division Source: TAIR
  • cellular response to iron ion Source: TAIR
  • defense response Source: UniProtKB-KW
  • ethylene biosynthetic process Source: TAIR
  • fruit ripening Source: UniProtKB-KW
  • response to auxin Source: TAIR
  • response to jasmonic acid Source: TAIR
  • response to mechanical stimulus Source: TAIR
  • response to oxidative stress Source: TAIR
  • response to wounding Source: TAIR
  • vasculature development Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Ethylene biosynthesis, Fruit ripening, Plant defense

Keywords - Ligandi

Pyridoxal phosphate, S-adenosyl-L-methionine

Enzyme and pathway databases

BRENDAi4.4.1.14. 399.
SABIO-RKQ9SAR0.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase 6 (EC:4.4.1.14)
Short name:
ACC synthase 6
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase 6
Gene namesi
Name:ACS6
Synonyms:ACC6
Ordered Locus Names:At4g11280
ORF Names:F8L21.70
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G11280.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi480 – 4801S → D: 40-fold increase in ethylene production; when associated with D-483 and D-488. 1 Publication
Mutagenesisi483 – 4831S → D: 40-fold increase in ethylene production; when associated with D-480 and D-488. 1 Publication
Mutagenesisi488 – 4881S → D: 40-fold increase in ethylene production; when associated with D-480 and D-483. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4954951-aminocyclopropane-1-carboxylate synthase 6PRO_0000123900Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei280 – 2801N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei480 – 4801Phosphoserine1 Publication
Modified residuei483 – 4831Phosphoserine1 Publication
Modified residuei488 – 4881Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residue by MAP kinase (MPK6).1 Publication
May be processed at its C-terminus.

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9SAR0.
PRIDEiQ9SAR0.

PTM databases

iPTMnetiQ9SAR0.

Expressioni

Tissue specificityi

Expressed in roots and flowers.1 Publication

Inductioni

By indole-3-acetic acid (IAA) and cycloheximide (CHX). By auxin. By treatment with ozone.3 Publications

Gene expression databases

GenevisibleiQ9SAR0. AT.

Interactioni

Subunit structurei

Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure (By similarity). Interacts with GRF3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-2356658,EBI-2356658
ACS4Q433092EBI-2356658,EBI-2436015

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi12029. 4 interactions.
IntActiQ9SAR0. 4 interactions.
MINTiMINT-8065925.
STRINGi3702.AT4G11280.1.

Structurei

3D structure databases

ProteinModelPortaliQ9SAR0.
SMRiQ9SAR0. Positions 14-435.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ9SAR0.
KOiK01762.
OMAiDISALYH.
PhylomeDBiQ9SAR0.

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.

Q9SAR0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVAFATEKKQ DLNLLSKIAS GDGHGENSSY FDGWKAYEEN PFHPIDRPDG
60 70 80 90 100
VIQMGLAENQ LCGDLMRKWV LKHPEASICT SEGVNQFSDI AIFQDYHGLP
110 120 130 140 150
EFRQAVAKFM EKTRNNKVKF DPDRIVMSGG ATGAHETVAF CLANPGDGFL
160 170 180 190 200
VPTPYYPGFD RDLRWRTGVN LVPVTCHSSN GFKITVEALE AAYENARKSN
210 220 230 240 250
IPVKGLLVTN PSNPLGTTLD RECLKSLVNF TNDKGIHLIA DEIYAATTFG
260 270 280 290 300
QSEFISVAEV IEEIEDCNRD LIHIVYSLSK DMGLPGLRVG IVYSYNDRVV
310 320 330 340 350
QIARKMSSFG LVSSQTQHLI AKMLSDEEFV DEFIRESKLR LAARHAEITT
360 370 380 390 400
GLDGLGIGWL KAKAGLFLWM DLRNLLKTAT FDSETELWRV IVHQVKLNVS
410 420 430 440 450
PGGSFHCHEP GWFRVCFANM DHKTMETALE RIRVFTSQLE EETKPMAATT
460 470 480 490
MMAKKKKKCW QSNLRLSFSD TRRFDDGFFS PHSPVPPSPL VRAQT
Length:495
Mass (Da):55,524
Last modified:July 19, 2004 - v2
Checksum:i7FA94D3EABBCB4AB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti56 – 561L → F in AAC32251 (Ref. 5) Curated
Sequence conflicti433 – 4331R → K in AAC63850 (PubMed:10080689).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096882 Genomic DNA. Translation: CAB51412.1.
AL161531 Genomic DNA. Translation: CAB81229.1.
CP002687 Genomic DNA. Translation: AEE82992.1.
AF361097 mRNA. Translation: AAK27237.1.
AF428292 mRNA. Translation: AAL16124.1.
BT000487 mRNA. Translation: AAN18056.1.
U73786 mRNA. Translation: AAC63850.1.
U79524 mRNA. Translation: AAC32251.1.
PIRiT13019.
RefSeqiNP_192867.1. NM_117199.1.
UniGeneiAt.3654.

Genome annotation databases

EnsemblPlantsiAT4G11280.1; AT4G11280.1; AT4G11280.
GeneIDi826730.
GrameneiAT4G11280.1; AT4G11280.1; AT4G11280.
KEGGiath:AT4G11280.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL096882 Genomic DNA. Translation: CAB51412.1.
AL161531 Genomic DNA. Translation: CAB81229.1.
CP002687 Genomic DNA. Translation: AEE82992.1.
AF361097 mRNA. Translation: AAK27237.1.
AF428292 mRNA. Translation: AAL16124.1.
BT000487 mRNA. Translation: AAN18056.1.
U73786 mRNA. Translation: AAC63850.1.
U79524 mRNA. Translation: AAC32251.1.
PIRiT13019.
RefSeqiNP_192867.1. NM_117199.1.
UniGeneiAt.3654.

3D structure databases

ProteinModelPortaliQ9SAR0.
SMRiQ9SAR0. Positions 14-435.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi12029. 4 interactions.
IntActiQ9SAR0. 4 interactions.
MINTiMINT-8065925.
STRINGi3702.AT4G11280.1.

PTM databases

iPTMnetiQ9SAR0.

Proteomic databases

PaxDbiQ9SAR0.
PRIDEiQ9SAR0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G11280.1; AT4G11280.1; AT4G11280.
GeneIDi826730.
GrameneiAT4G11280.1; AT4G11280.1; AT4G11280.
KEGGiath:AT4G11280.

Organism-specific databases

TAIRiAT4G11280.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ9SAR0.
KOiK01762.
OMAiDISALYH.
PhylomeDBiQ9SAR0.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
BRENDAi4.4.1.14. 399.
SABIO-RKQ9SAR0.

Miscellaneous databases

PROiQ9SAR0.

Gene expression databases

GenevisibleiQ9SAR0. AT.

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

« Hide 'large scale' publications
  1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  4. "A multi-responsive gene encoding 1-aminocyclopropane-1-carboxylate synthase (ACS6) in mature Arabidopsis leaves."
    Arteca J.M., Arteca R.N.
    Plant Mol. Biol. 39:209-219(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-495, INDUCTION.
    Strain: cv. Columbia.
  5. "Induction of an ACC synthase cDNA by ozone in light-grown Arabidopsis thaliana leaves."
    Vahala J., Schlagnhaufer C.D., Pell E.J.
    Physiol. Plantarum 103:45-50(1998)
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-418, INDUCTION.
  6. "Biochemical diversity among the 1-amino-cyclopropane-1-carboxylate synthase isozymes encoded by the Arabidopsis gene family."
    Yamagami T., Tsuchisaka A., Yamada K., Haddon W.F., Harden L.A., Theologis A.
    J. Biol. Chem. 278:49102-49112(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, PUTATIVE PROTEOLYTIC PROCESSING.
  7. "Phosphorylation of 1-aminocyclopropane-1-carboxylic acid synthase by MPK6, a stress-responsive mitogen-activated protein kinase, induces ethylene biosynthesis in Arabidopsis."
    Liu Y., Zhang S.
    Plant Cell 16:3386-3399(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-480; SER-483 AND SER-488, MUTAGENESIS OF SER-480; SER-483 AND SER-488.
  8. "The Arabidopsis 14-3-3 protein RARE COLD INDUCIBLE 1A links low-temperature response and ethylene biosynthesis to regulate freezing tolerance and cold acclimation."
    Catala R., Lopez-Cobollo R., Mar Castellano M., Angosto T., Alonso J.M., Ecker J.R., Salinas J.
    Plant Cell 26:3326-3342(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GRF3.

Entry informationi

Entry namei1A16_ARATH
AccessioniPrimary (citable) accession number: Q9SAR0
Secondary accession number(s): O82719, Q9SUT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: February 17, 2016
This is version 112 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. The phosphorylation of serine residues on the C-terminus increases protein stability.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.