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Protein

1-aminocyclopropane-1-carboxylate synthase 11

Gene

ACS11

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.

Catalytic activityi

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

Cofactori

Kineticsi

  1. KM=25 µM for AdoMet
  1. Vmax=25.20 µM/h/mg enzyme

pH dependencei

Optimum pH is 8.

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 4 (ACS4), 1-aminocyclopropane-1-carboxylate synthase 8 (ACS8), 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 sitei45 – 451SubstrateBy similarity
Binding sitei83 – 831SubstrateBy similarity

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

SABIO-RKQ9S9U6.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase 11 (EC:4.4.1.14)
Short name:
ACC synthase 11
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase 11
Gene namesi
Name:ACS11
Ordered Locus Names:At4g08040
ORF Names:T17A2.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 4

Organism-specific databases

TAIRiAT4G08040.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4604601-aminocyclopropane-1-carboxylate synthase 11PRO_0000123905Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei267 – 2671N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

May be processed at its C-terminus.

Proteomic databases

PaxDbiQ9S9U6.
PRIDEiQ9S9U6.

Expressioni

Tissue specificityi

Expressed in roots.1 Publication

Inductioni

By indole-3-acetic acid (IAA) and cycloheximide (CHX).1 Publication

Gene expression databases

GenevisibleiQ9S9U6. 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

Protein-protein interaction databases

BioGridi11617. 1 interaction.
IntActiQ9S9U6. 1 interaction.
STRINGi3702.AT4G08040.1.

Structurei

3D structure databases

ProteinModelPortaliQ9S9U6.
SMRiQ9S9U6. Positions 10-423.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ9S9U6.
KOiK01762.
OMAiCWVDLRH.
PhylomeDBiQ9S9U6.

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.

Q9S9U6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSKVVGDS HGQDSSYFLG WQEYEKNPFH ESFNTSGIVQ MGLAENQLSF
60 70 80 90 100
DLIEKWLEEH PEVLGLKKND ESVFRQLALF QDYHGLPAFK DAMAKFMGKI
110 120 130 140 150
RENKVKFDTN KMVLTAGSTS ANETLMFCLA NPGDAFLIPA PYYPGFDRDL
160 170 180 190 200
KWRTGVEIVP IHCVSSNGYK ITEDALEDAY ERALKHNLNV KGVLITNPSN
210 220 230 240 250
PLGTSTTREE LDLLLTFTST KKIHMVSDEI YSGTVFDSPE FTSVLEVAKD
260 270 280 290 300
KNMGLDGKIH VVYSLSKDLG LPGFRVGLIY SNNEKVVSAA TKMSSFGLIS
310 320 330 340 350
SQTQHLLANL LSDERFTTNY LEENKKRLRE RKDRLVSGLK EAGISCLKSN
360 370 380 390 400
AGLFCWVDLR HLLKSNTFEA EHSLWTKIVC EVGLNISPGS SCHCDEPGWF
410 420 430 440 450
RVCFANMSDQ TMEVAMDRVK GFVDNNNGGK QKRTMWDTRR RSLINKWVSK
460
LSSVTCESER
Length:460
Mass (Da):51,799
Last modified:May 1, 2000 - v1
Checksum:i1A056347680E7E2F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160183 Genomic DNA. Translation: AAD48074.1.
AL161509 Genomic DNA. Translation: CAB81141.1.
CP002687 Genomic DNA. Translation: AEE82593.1.
AF332405 mRNA. Translation: AAG48768.1.
PIRiB85079.
RefSeqiNP_567330.1. NM_116873.1.
UniGeneiAt.4151.

Genome annotation databases

EnsemblPlantsiAT4G08040.1; AT4G08040.1; AT4G08040.
GeneIDi826317.
GrameneiAT4G08040.1; AT4G08040.1; AT4G08040.
KEGGiath:AT4G08040.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF160183 Genomic DNA. Translation: AAD48074.1.
AL161509 Genomic DNA. Translation: CAB81141.1.
CP002687 Genomic DNA. Translation: AEE82593.1.
AF332405 mRNA. Translation: AAG48768.1.
PIRiB85079.
RefSeqiNP_567330.1. NM_116873.1.
UniGeneiAt.4151.

3D structure databases

ProteinModelPortaliQ9S9U6.
SMRiQ9S9U6. Positions 10-423.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi11617. 1 interaction.
IntActiQ9S9U6. 1 interaction.
STRINGi3702.AT4G08040.1.

Proteomic databases

PaxDbiQ9S9U6.
PRIDEiQ9S9U6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT4G08040.1; AT4G08040.1; AT4G08040.
GeneIDi826317.
GrameneiAT4G08040.1; AT4G08040.1; AT4G08040.
KEGGiath:AT4G08040.

Organism-specific databases

TAIRiAT4G08040.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ9S9U6.
KOiK01762.
OMAiCWVDLRH.
PhylomeDBiQ9S9U6.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
SABIO-RKQ9S9U6.

Miscellaneous databases

PROiQ9S9U6.

Gene expression databases

GenevisibleiQ9S9U6. 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. "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.
  5. "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 namei1A111_ARATH
AccessioniPrimary (citable) accession number: Q9S9U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: July 6, 2016
This is version 105 of the entry and version 1 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

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.