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Protein

1-aminocyclopropane-1-carboxylate synthase 9

Gene

ACS9

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=40 µM for AdoMet
  1. Vmax=324.5 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 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 sitei47 – 471SubstrateBy similarity
Binding sitei85 – 851SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • 1-aminocyclopropane-1-carboxylate biosynthetic process Source: GOC
  • cellular response to iron ion Source: TAIR
  • ethylene biosynthetic process Source: TAIR
  • fruit ripening Source: UniProtKB-KW
  • regulation of translation Source: TAIR
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-RKQ9M2Y8.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase 9 (EC:4.4.1.14)
Short name:
ACC synthase 9
Alternative name(s):
Ethylene-overproduction protein 3
S-adenosyl-L-methionine methylthioadenosine-lyase 9
Gene namesi
Name:ACS9
Synonyms:ETO3
Ordered Locus Names:At3g49700
ORF Names:T16K5.50
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 3

Organism-specific databases

TAIRiAT3G49700.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi457 – 4571V → D in eto3; increases its stability heading to ethylene overproduction. Impairs the binding to ETO1 and slightly affects the binding to EOL1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4704701-aminocyclopropane-1-carboxylate synthase 9PRO_0000123903Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

May be processed at its C-terminus.

Proteomic databases

PaxDbiQ9M2Y8.
PRIDEiQ9M2Y8.

Expressioni

Tissue specificityi

Expressed in roots and siliques.1 Publication

Inductioni

By cycloheximide (CHX).1 Publication

Gene expression databases

GenevisibleiQ9M2Y8. AT.

Interactioni

Subunit structurei

Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure (By similarity). Interacts (via its C-terminal region) with FEI1, FEI2, ETO1 and EOL1.By similarity2 Publications

Protein-protein interaction databases

STRINGi3702.AT3G49700.1.

Structurei

3D structure databases

ProteinModelPortaliQ9M2Y8.
SMRiQ9M2Y8. Positions 15-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ9M2Y8.
KOiK01762.
OMAiCDPGDGY.
PhylomeDBiQ9M2Y8.

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.

Q9M2Y8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQLSRKVTS NAHGQDSSYF LGWEEYEKNP YDEIKNPNGI IQMGLAENQL
60 70 80 90 100
CFDLIETWLA KNPDAAGLKK DGQSIFKELA LFQDYHGLPE FKKALAEFME
110 120 130 140 150
EIRGNRVTFD PSKIVLAAGS TSANETLMFC LAEPGDAFLL PTPYYPGFDR
160 170 180 190 200
DLKWRTGAEI VPIHCSSSNG FQITESALQQ AYQQAQKLDL KVKGVLVTNP
210 220 230 240 250
SNPLGTMLTR RELNLLVDFI TSKNIHLISD EIYSGTVFGF EQFVSVMDVL
260 270 280 290 300
KDKNLENSEV SKRVHIVYSL SKDLGLPGFR VGAIYSNDEM VVSAATKMSS
310 320 330 340 350
FGLVSSQTQY LLSALLSDKK FTSTYLDENQ KRLKIRQKKL VSGLEAAGIT
360 370 380 390 400
CLKSNAGLFC WVDMRHLLDT NTFEAELELW KKIVYDVKLN ISPGSSCHCT
410 420 430 440 450
EPGWFRVCFA NMSEDTLDLA MKRLKEYVES TDSRRVISKS SHDRIKSLRK
460 470
RTVSNWVFRV SWTDRVPDER
Length:470
Mass (Da):53,170
Last modified:October 1, 2000 - v1
Checksum:i2110331C76ACED4E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132965 Genomic DNA. Translation: CAB66908.1.
CP002686 Genomic DNA. Translation: AEE78578.1.
AF332391 mRNA. Translation: AAG48755.1.
PIRiT46036.
RefSeqiNP_190539.1. NM_114830.1.
UniGeneiAt.743.

Genome annotation databases

EnsemblPlantsiAT3G49700.1; AT3G49700.1; AT3G49700.
GeneIDi824132.
GrameneiAT3G49700.1; AT3G49700.1; AT3G49700.
KEGGiath:AT3G49700.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL132965 Genomic DNA. Translation: CAB66908.1.
CP002686 Genomic DNA. Translation: AEE78578.1.
AF332391 mRNA. Translation: AAG48755.1.
PIRiT46036.
RefSeqiNP_190539.1. NM_114830.1.
UniGeneiAt.743.

3D structure databases

ProteinModelPortaliQ9M2Y8.
SMRiQ9M2Y8. Positions 15-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT3G49700.1.

Proteomic databases

PaxDbiQ9M2Y8.
PRIDEiQ9M2Y8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT3G49700.1; AT3G49700.1; AT3G49700.
GeneIDi824132.
GrameneiAT3G49700.1; AT3G49700.1; AT3G49700.
KEGGiath:AT3G49700.

Organism-specific databases

TAIRiAT3G49700.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ9M2Y8.
KOiK01762.
OMAiCDPGDGY.
PhylomeDBiQ9M2Y8.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
SABIO-RKQ9M2Y8.

Miscellaneous databases

PROiQ9M2Y8.

Gene expression databases

GenevisibleiQ9M2Y8. 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 3 of the plant Arabidopsis thaliana."
    Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F.
    , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
    Nature 408:820-822(2000) [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. "The eto1, eto2, and eto3 mutations and cytokinin treatment increase ethylene biosynthesis in Arabidopsis by increasing the stability of ACS protein."
    Chae H.S., Faure F., Kieber J.J.
    Plant Cell 15:545-559(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTANT ETO3.
  5. "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.
  6. "Two leucine-rich repeat receptor kinases mediate signaling, linking cell wall biosynthesis and ACC synthase in Arabidopsis."
    Xu S.-L., Rahman A., Baskin T.I., Kieber J.J.
    Plant Cell 20:3065-3079(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FEI1 AND FEI2.
  7. "The BTB ubiquitin ligases ETO1, EOL1 and EOL2 act collectively to regulate ethylene biosynthesis in Arabidopsis by controlling type-2 ACC synthase levels."
    Christians M.J., Gingerich D.J., Hansen M., Binder B.M., Kieber J.J., Vierstra R.D.
    Plant J. 57:332-345(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ETO1 AND EOL1, MUTAGENESIS OF VAL-457.

Entry informationi

Entry namei1A19_ARATH
AccessioniPrimary (citable) accession number: Q9M2Y8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2000
Last modified: February 17, 2016
This is version 107 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.