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Protein

1-aminocyclopropane-1-carboxylate synthase 2

Gene

ACS2

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=45 µM for AdoMet
  1. Vmax=32 µM/h/mg enzyme

pH dependencei

Optimum pH is 8.2.

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 sitei55 – 551SubstrateBy similarity
Binding sitei93 – 931SubstrateBy similarity

GO - Molecular functioni

GO - Biological processi

  • 1-aminocyclopropane-1-carboxylate biosynthetic process Source: GOC
  • ethylene biosynthetic process Source: TAIR
  • 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

BioCyciARA:GQT-745-MONOMER.
MetaCyc:AT1G01480-MONOMER.
BRENDAi4.4.1.14. 399.
SABIO-RKQ06402.
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):
S-adenosyl-L-methionine methylthioadenosine-lyase 2
Gene namesi
Name:ACS2
Synonyms:ACC1
Ordered Locus Names:At1g01480
ORF Names:F22L4.4
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G01480.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi206 – 2083Missing : Abolishes 1-aminocyclopropane-1-carboxylate synthase function. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4964961-aminocyclopropane-1-carboxylate synthase 2PRO_0000123897Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei279 – 2791N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei483 – 4831Phosphoserine1 Publication
Modified residuei488 – 4881Phosphoserine1 Publication
Modified residuei491 – 4911Phosphoserine1 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

PaxDbiQ06402.
PRIDEiQ06402.

PTM databases

iPTMnetiQ06402.

Expressioni

Tissue specificityi

High in developing leaves and in flowers. Expressed in roots and siliques.1 Publication

Inductioni

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

Gene expression databases

GenevisibleiQ06402. 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

BioGridi22324. 1 interaction.
IntActiQ06402. 1 interaction.
STRINGi3702.AT1G01480.1.

Structurei

3D structure databases

ProteinModelPortaliQ06402.
SMRiQ06402. Positions 11-440.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ06402.
KOiK01762.
OMAiGENSEYF.
PhylomeDBiQ06402.

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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06402-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MGLPGKNKGA VLSKIATNNQ HGENSEYFDG WKAYDKDPFH LSRNPHGIIQ
60 70 80 90 100
MGLAENQLCL DLIKDWVKEN PEASICTLEG IHQFSDIANF QDYHGLKKFR
110 120 130 140 150
QAIAHFMGKA RGGRVTFDPE RVVMSGGATG ANETIMFCLA DPGDVFLIPS
160 170 180 190 200
PYYAAFDRDL RWRTGVEIIP VPCSSSDNFK LTVDAAEWAY KKAQESNKKV
210 220 230 240 250
KGLILTNPSN PLGTMLDKDT LTNLVRFVTR KNIHLVVDEI YAATVFAGGD
260 270 280 290 300
FVSVAEVVND VDISEVNVDL IHIVYSLSKD MGLPGFRVGI VYSFNDSVVS
310 320 330 340 350
CARKMSSFGL VSSQTQLMLA SMLSDDQFVD NFLMESSRRL GIRHKVFTTG
360 370 380 390 400
IKKADIACLT SNAGLFAWMD LRHLLRDRNS FESEIELWHI IIDRVKLNVS
410 420 430 440 450
PGSSFRCTEP GWFRICFANM DDDTLHVALG RIQDFVSKNK NKIVEKASEN
460 470 480 490
DQVIQNKSAK KLKWTQTNLR LSFRRLYEDG LSSPGIMSPH SPLLRA
Length:496
Mass (Da):55,532
Last modified:June 1, 1994 - v1
Checksum:i766318AE9B5F1566
GO
Isoform 2 (identifier: Q06402-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Show »
Length:390
Mass (Da):43,537
Checksum:i7A7A592FBA0B70DE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti136 – 1361M → I.1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 106106Missing in isoform 2. 1 PublicationVSP_009111Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12614 Genomic DNA. Translation: CAA78260.1.
M95594 Genomic DNA. Translation: AAA97516.1.
M95595 mRNA. Translation: AAB59298.1.
Y12776 Genomic DNA. Translation: CAA73310.1.
AC061957 Genomic DNA. Translation: AAF81308.1.
CP002684 Genomic DNA. Translation: AEE27293.1.
CP002684 Genomic DNA. Translation: AEE27294.1.
AF334719 mRNA. Translation: AAG50097.1.
AY052207 mRNA. Translation: AAK97678.1.
AY143877 mRNA. Translation: AAN28816.1.
PIRiA47199.
RefSeqiNP_171655.1. NM_100030.3. [Q06402-1]
NP_849572.1. NM_179241.1. [Q06402-2]
UniGeneiAt.164.

Genome annotation databases

EnsemblPlantsiAT1G01480.1; AT1G01480.1; AT1G01480. [Q06402-1]
GeneIDi837082.
KEGGiath:AT1G01480.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z12614 Genomic DNA. Translation: CAA78260.1.
M95594 Genomic DNA. Translation: AAA97516.1.
M95595 mRNA. Translation: AAB59298.1.
Y12776 Genomic DNA. Translation: CAA73310.1.
AC061957 Genomic DNA. Translation: AAF81308.1.
CP002684 Genomic DNA. Translation: AEE27293.1.
CP002684 Genomic DNA. Translation: AEE27294.1.
AF334719 mRNA. Translation: AAG50097.1.
AY052207 mRNA. Translation: AAK97678.1.
AY143877 mRNA. Translation: AAN28816.1.
PIRiA47199.
RefSeqiNP_171655.1. NM_100030.3. [Q06402-1]
NP_849572.1. NM_179241.1. [Q06402-2]
UniGeneiAt.164.

3D structure databases

ProteinModelPortaliQ06402.
SMRiQ06402. Positions 11-440.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi22324. 1 interaction.
IntActiQ06402. 1 interaction.
STRINGi3702.AT1G01480.1.

PTM databases

iPTMnetiQ06402.

Proteomic databases

PaxDbiQ06402.
PRIDEiQ06402.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G01480.1; AT1G01480.1; AT1G01480. [Q06402-1]
GeneIDi837082.
KEGGiath:AT1G01480.

Organism-specific databases

TAIRiAT1G01480.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ06402.
KOiK01762.
OMAiGENSEYF.
PhylomeDBiQ06402.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
BioCyciARA:GQT-745-MONOMER.
MetaCyc:AT1G01480-MONOMER.
BRENDAi4.4.1.14. 399.
SABIO-RKQ06402.

Miscellaneous databases

PROiQ06402.

Gene expression databases

GenevisibleiQ06402. 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. "Cloning, genetic mapping, and expression analysis of an Arabidopsis thaliana gene that encodes 1-aminocyclopropane-1-carboxylate synthase."
    van der Straeten D., Rodrigues-Pousada R.A., Villarroel R., Hanley S., Goodman H.M., Van Montagu M.
    Proc. Natl. Acad. Sci. U.S.A. 89:9969-9973(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), VARIANT ILE-136.
    Strain: cv. Columbia.
  2. "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 [GENOMIC DNA / MRNA] (ISOFORM 1).
    Strain: cv. Columbia.
  3. "Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located at the top of chromosome 1."
    Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P., De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P., van Montagu M.
    Gene 215:11-17(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1).
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
    Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K.
    , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
    Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  5. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  6. "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] (ISOFORMS 1 AND 2).
    Strain: cv. Columbia.
  7. "Characterization of two members (ACS1 and ACS3) of the 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis thaliana."
    Liang X.-W., Oono Y., Shen N.F., Koehler C., Li K., Scolnik P.A., Theologis A.
    Gene 167:17-24(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 206-THR--PRO-208.
    Strain: cv. Columbia.
  8. "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.
  9. "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: PHOSPHORYLATION AT SER-483; SER-488 AND SER-491.
  10. "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 namei1A12_ARATH
AccessioniPrimary (citable) accession number: Q06402
Secondary accession number(s): Q941E7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: February 17, 2016
This is version 128 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.