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Protein

1-aminocyclopropane-1-carboxylate synthase 5

Gene

ACS5

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=37 µM for S-adenosyl-L-methionine
  1. Vmax=81.70 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

GO - Biological processi

  • cell division Source: TAIR
  • ethylene biosynthetic process Source: TAIR
  • fruit ripening Source: UniProtKB-KW
  • response to cytokinin Source: TAIR
  • vasculature development 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

BRENDAi4.4.1.14. 399.
SABIO-RKQ37001.
UniPathwayiUPA00384; UER00562.

Names & Taxonomyi

Protein namesi
Recommended name:
1-aminocyclopropane-1-carboxylate synthase 5 (EC:4.4.1.14)
Short name:
ACC synthase 5
Alternative name(s):
Ethylene-overproduction protein 2
S-adenosyl-L-methionine methylthioadenosine-lyase 5
Gene namesi
Name:ACS5
Synonyms:ACC5, ETO2
Ordered Locus Names:At5g65800
ORF Names:F6H11.90, MPA24.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G65800.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi201 – 2011S → F in cin5-3; defective in cytokinin induced ethylene.
Mutagenesisi269 – 2691S → N in cin5-2; defective in cytokinin induced ethylene.
Mutagenesisi459 – 47012RVSWT…VPDER → PGFMDRSCT in eto2; increases its stability leading to ethylene overproduction. Add
BLAST

Chemistry

ChEMBLiCHEMBL2242742.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 4704701-aminocyclopropane-1-carboxylate synthase 5PRO_0000123899Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei272 – 2721N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei461 – 4611PhosphoserineBy similarity

Post-translational modificationi

May be processed at its C-terminus.
Ubiquitinated (Probable). The interaction with ETO1 (and possibly EOL1 and EOL2) mediate its proteasome-dependent degradation. Its stability and degradation plays a central role in ethylene biosynthesis.Curated

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ37001.
PRIDEiQ37001.

PTM databases

iPTMnetiQ37001.

Expressioni

Tissue specificityi

Expressed in roots and siliques.1 Publication

Inductioni

By indole-3-acetic acid (IAA) and cycloheximide (CHX). In response to low dose of cytokinin.1 Publication

Gene expression databases

GenevisibleiQ37001. 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, EOL1 and EOL2 (PubMed:15118728, PubMed:19017745, PubMed:18808454). Interacts with GRF3 (PubMed:25122152).By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ETO1O650203EBI-593450,EBI-593440

Protein-protein interaction databases

BioGridi21951. 6 interactions.
IntActiQ37001. 3 interactions.
STRINGi3702.AT5G65800.1.

Structurei

3D structure databases

ProteinModelPortaliQ37001.
SMRiQ37001. Positions 17-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ37001.
KOiK01762.
OMAiSHHQMLK.
PhylomeDBiQ37001.

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.

Q37001-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKQLSTKVTS NGHGQDSSYF LGWEEYEKNP YDEIKNPNGM IQMGLAENQL
60 70 80 90 100
CFDLIESWLT KNPDAASLKR NGQSIFRELA LFQDYHGMPE FKKAMAEFME
110 120 130 140 150
EIRGNRVTFD PKKIVLAAGS TSANETLMFC LAEPGDAFLL PTPYYPGFDR
160 170 180 190 200
DLKWRTGAEI VPIHCSSSNG FQITESALQQ AYQQAQKLDL KVKGVLVTNP
210 220 230 240 250
SNPLGTALTR RELNLLVDFI TSKNIHLISD EIYSGTMFGF EQFISVMDVL
260 270 280 290 300
KDKKLEDTEV SKRVHVVYSL SKDLGLPGFR VGAIYSNDEM IVSAATKMSS
310 320 330 340 350
FGLVSSQTQY LLSALLSDKK FTSQYLEENQ KRLKSRQRRL VSGLESAGIT
360 370 380 390 400
CLRSNAGLFC WVDMRHLLDT NTFEAELDLW KKIVYNVKLN ISPGSSCHCT
410 420 430 440 450
EPGWFRVCFA NMSEDTLDLA LKRLKTFVES TDCGRMISRS SHERLKSLRK
460 470
KTVSNWVFRV SWTDRVPDER
Length:470
Mass (Da):53,313
Last modified:November 1, 1996 - v1
Checksum:i8B2527C9B52AE19A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29261 mRNA. Translation: AAA87292.1.
L29260 Genomic DNA. Translation: AAA87291.1.
AB010075, AB020743 Genomic DNA. Translation: BAB10687.1.
AL021684 Genomic DNA. Translation: CAA16680.1.
CP002688 Genomic DNA. Translation: AED98109.1.
AF334720 mRNA. Translation: AAG50098.1.
AK229087 mRNA. Translation: BAF00967.1.
PIRiS71174.
RefSeqiNP_201381.1. NM_125977.2.
UniGeneiAt.1918.

Genome annotation databases

EnsemblPlantsiAT5G65800.1; AT5G65800.1; AT5G65800.
GeneIDi836709.
GrameneiAT5G65800.1; AT5G65800.1; AT5G65800.
KEGGiath:AT5G65800.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L29261 mRNA. Translation: AAA87292.1.
L29260 Genomic DNA. Translation: AAA87291.1.
AB010075, AB020743 Genomic DNA. Translation: BAB10687.1.
AL021684 Genomic DNA. Translation: CAA16680.1.
CP002688 Genomic DNA. Translation: AED98109.1.
AF334720 mRNA. Translation: AAG50098.1.
AK229087 mRNA. Translation: BAF00967.1.
PIRiS71174.
RefSeqiNP_201381.1. NM_125977.2.
UniGeneiAt.1918.

3D structure databases

ProteinModelPortaliQ37001.
SMRiQ37001. Positions 17-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi21951. 6 interactions.
IntActiQ37001. 3 interactions.
STRINGi3702.AT5G65800.1.

Chemistry

ChEMBLiCHEMBL2242742.

PTM databases

iPTMnetiQ37001.

Proteomic databases

PaxDbiQ37001.
PRIDEiQ37001.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G65800.1; AT5G65800.1; AT5G65800.
GeneIDi836709.
GrameneiAT5G65800.1; AT5G65800.1; AT5G65800.
KEGGiath:AT5G65800.

Organism-specific databases

TAIRiAT5G65800.

Phylogenomic databases

eggNOGiKOG0256. Eukaryota.
COG0436. LUCA.
HOGENOMiHOG000011234.
InParanoidiQ37001.
KOiK01762.
OMAiSHHQMLK.
PhylomeDBiQ37001.

Enzyme and pathway databases

UniPathwayiUPA00384; UER00562.
BRENDAi4.4.1.14. 399.
SABIO-RKQ37001.

Miscellaneous databases

PROiQ37001.

Gene expression databases

GenevisibleiQ37001. 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. "Li(+)-regulated 1-aminocyclopropane-1-carboxylate synthase gene expression in Arabidopsis thaliana."
    Liang X.-W., Shen N.F., Theologis A.
    Plant J. 10:1027-1036(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: cv. Columbia.
    Tissue: Seedling.
  2. "Structural analysis of Arabidopsis thaliana chromosome 5. IV. Sequence features of the regions of 1,456,315 bp covered by nineteen physically assigned P1 and TAC clones."
    Sato S., Kaneko T., Kotani H., Nakamura Y., Asamizu E., Miyajima N., Tabata S.
    DNA Res. 5:41-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence features of the regions of 3,076,755 bp covered by sixty P1 and TAC clones."
    Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H., Tabata S.
    DNA Res. 7:31-63(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  4. "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana."
    Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.
    , Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A., Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.
    Nature 408:823-826(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].
    Strain: cv. Columbia.
  7. "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs."
    Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.
    , Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y., Shinozaki K.
    Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: cv. Columbia.
  8. "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] OF 50-81.
    Strain: cv. Columbia.
  9. "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 ETO2.
  10. "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.
  11. "Regulation of ethylene gas biosynthesis by the Arabidopsis ETO1 protein."
    Wang K.L.-C., Yoshida H., Lurin C., Ecker J.R.
    Nature 428:945-950(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEGRADATION, INTERACTION WITH ETO1; EOL1 AND EOL2.
  12. "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.
  13. "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.
  14. "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 namei1A15_ARATH
AccessioniPrimary (citable) accession number: Q37001
Secondary accession number(s): O49537, Q0WPI2, Q9S9C3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: November 1, 1996
Last modified: July 6, 2016
This is version 122 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

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.