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Protein

1-aminocyclopropane-1-carboxylate synthase 4

Gene

ACS4

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=15 µM for AdoMet
  1. Vmax=31.20 µM/h/mg enzyme

pH dependencei

Optimum pH is 7.8.

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 sitei47 – 471SubstrateBy similarity
Binding sitei85 – 851SubstrateBy 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

  • cellular response to iron ion Source: TAIR
  • ethylene biosynthetic process Source: UniProtKB-UniPathway
  • fruit ripening Source: UniProtKB-KW
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

BioCyciMetaCyc:AT2G22810-MONOMER.
SABIO-RKQ43309.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase 4 (EC:4.4.1.14)
Short name:
ACC synthase 4
Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase 4
Gene namesi
Name:ACS4
Synonyms:ACC4
Ordered Locus Names:At2g22810
ORF Names:T20K9.2
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

TAIRiAT2G22810.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4744741-aminocyclopropane-1-carboxylate synthase 4PRO_0000123898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei273 – 2731N6-(pyridoxal phosphate)lysineBy similarity

Post-translational modificationi

Ubiquitinated by XBAT32. Ubiquitination probably leads to its subsequent degradation, thus controlling ethylene production.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

PaxDbiQ43309.
PRIDEiQ43309.

Expressioni

Tissue specificityi

Expressed in roots, leaves and flowers.1 Publication

Inductioni

By indole-3-acetic acid (IAA) and cycloheximide (CHX). By auxin.2 Publications

Gene expression databases

GenevisibleiQ43309. AT.

Interactioni

Subunit structurei

Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure (By similarity). Interacts with XBAT32. Interacts (via its C-terminal region) with ETO1 and EOL1.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-2436015,EBI-2436015
ACS6Q9SAR02EBI-2436015,EBI-2356658
ACS7Q9STR44EBI-2436015,EBI-2356842
ACS8Q9T0652EBI-2436015,EBI-2357693

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi2165. 2 interactions.
IntActiQ43309. 5 interactions.
STRINGi3702.AT2G22810.1.

Structurei

3D structure databases

ProteinModelPortaliQ43309.
SMRiQ43309. Positions 4-431.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ43309.
KOiK01762.
OMAiREFVQTC.
PhylomeDBiQ43309.

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.

Q43309-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVQLSRKATC NSHGQVSSYF LGWEEYEKNP YDVTKNPQGI IQMGLAENQL
60 70 80 90 100
CFDLLESWLA QNTDAACFKR DGQSVFRELA LFQDYHGLSS FKNAFADFMS
110 120 130 140 150
ENRGNRVSFD SNNLVLTAGA TSANETLMFC LADPGDAFLL PTPYYPGFDR
160 170 180 190 200
DLKWRTGVEI VPIQSSSTNG FRITKLALEE AYEQAKKLDL NVKGILITNP
210 220 230 240 250
SNPLGTTTTQ TELNILFDFI TKNKNIHLVS DEIYSGTVFN SSEFISVMEI
260 270 280 290 300
LKNNQLENTD VLNRVHIVCS LSKDLGLPGF RVGAIYSNDK DVISAATKMS
310 320 330 340 350
SFGLVSSQTQ YLLSSLLSDK KFTKNYLREN QKRLKNRQRK LVLGLEAIGI
360 370 380 390 400
KCLKSNAGLF CWVDMRPLLR SKTFEAEMDL WKKIVYEVKL NISPGSSCHC
410 420 430 440 450
EEPGWFRVCF ANMIDETLKL ALKRLKMLVD DENSSRRCQK SKSERLNGSR
460 470
KKTMSNVSNW VFRLSFHDRE AEER
Length:474
Mass (Da):53,795
Last modified:November 1, 1996 - v1
Checksum:i98FD27622EAF3C21
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23481 mRNA. Translation: AAC49037.1.
U23482 Genomic DNA. Translation: AAA85039.1.
AC004786 Genomic DNA. Translation: AAC32428.1.
AC005617 Genomic DNA. Translation: AAM15065.1.
CP002685 Genomic DNA. Translation: AEC07360.1.
AF332404 mRNA. Translation: AAG48767.1.
PIRiB84617.
G46376.
RefSeqiNP_179866.1. NM_127846.1.
UniGeneiAt.1549.

Genome annotation databases

EnsemblPlantsiAT2G22810.1; AT2G22810.1; AT2G22810.
GeneIDi816812.
GrameneiAT2G22810.1; AT2G22810.1; AT2G22810.
KEGGiath:AT2G22810.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U23481 mRNA. Translation: AAC49037.1.
U23482 Genomic DNA. Translation: AAA85039.1.
AC004786 Genomic DNA. Translation: AAC32428.1.
AC005617 Genomic DNA. Translation: AAM15065.1.
CP002685 Genomic DNA. Translation: AEC07360.1.
AF332404 mRNA. Translation: AAG48767.1.
PIRiB84617.
G46376.
RefSeqiNP_179866.1. NM_127846.1.
UniGeneiAt.1549.

3D structure databases

ProteinModelPortaliQ43309.
SMRiQ43309. Positions 4-431.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi2165. 2 interactions.
IntActiQ43309. 5 interactions.
STRINGi3702.AT2G22810.1.

Proteomic databases

PaxDbiQ43309.
PRIDEiQ43309.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT2G22810.1; AT2G22810.1; AT2G22810.
GeneIDi816812.
GrameneiAT2G22810.1; AT2G22810.1; AT2G22810.
KEGGiath:AT2G22810.

Organism-specific databases

TAIRiAT2G22810.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ43309.
KOiK01762.
OMAiREFVQTC.
PhylomeDBiQ43309.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
BioCyciMetaCyc:AT2G22810-MONOMER.
SABIO-RKQ43309.

Miscellaneous databases

PROiQ43309.

Gene expression databases

GenevisibleiQ43309. 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. "ACS4, a primary indoleacetic acid-responsive gene encoding 1-aminocyclopropane-1-carboxylate synthase in Arabidopsis thaliana. Structural characterization, expression in Escherichia coli, and expression characteristics in response to auxin."
    Abel S., Nguyen M.D., Chow W., Theologis A.
    J. Biol. Chem. 270:19093-19099(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION.
    Strain: cv. Columbia.
  2. Erratum
    Abel S., Nguyen M.D., Chow W., Theologis A.
    J. Biol. Chem. 270:26020-26020(1995)
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  5. "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.
  6. "The 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis thaliana."
    Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.
    Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 50-81.
  7. "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, INDUCTION.
  8. "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.
  9. "Arabidopsis RING E3 ligase XBAT32 regulates lateral root production through its role in ethylene biosynthesis."
    Prasad M.E., Schofield A., Lyzenga W., Liu H., Stone S.L.
    Plant Physiol. 153:1587-1596(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH XBAT32, UBIQUITINATION.

Entry informationi

Entry namei1A14_ARATH
AccessioniPrimary (citable) accession number: Q43309
Secondary accession number(s): Q9S9C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 120 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.