Reviewed, UniProtKB/Swiss-Prot Q9SAR0 (1A16_ARATH)

Names and origin

Protein names

Recommended name:
    1-aminocyclopropane-1-carboxylate synthase 6
      Short name=ACC synthase 6
    EC=4.4.1.14
Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase 6

Gene names

Name:	ACS6
Synonyms:	ACC6
Ordered Locus Names:	At4g11280
ORF Names:	F8L21.70

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	495 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. Involved in bacterial flagellin-induced ethylene production. Ref.6
Catalytic activity	S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine. Ref.5
Cofactor	Pyridoxal phosphate.
Pathway	Alkene biosynthesis; ethylene biosynthesis via S-adenosyl-L-methionine; ethylene from S-adenosyl-L-methionine: step 1/2.
Subunit structure	Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure By similarity.
Tissue specificity	Expressed in roots and flowers. Ref.5
Induction	By indole-3-acetic acid (IAA) and cycloheximide (CHX). By auxin. By treatment with ozone. Ref.5 Ref.3 Ref.4
Post-translational modification	Phosphorylated on serine residue by MAP kinase (MPK6). Ref.6 May be processed at its C-terminus.
Miscellaneous	The stability of ACS proteins, and the regulation of such stability, play a central role in ethylene biosynthesis. The phosphorylation of serine residues on the C-terminus increases protein stability.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Biophysicochemical properties	Kinetic parameters: KM=23 µM for AdoMet Vmax=120.60 µM/h/mg enzyme pH dependence: Optimum pH is 7.3.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Fruit ripening Plant defense
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	defense response Inferred from electronic annotation. Source: UniProtKB-KW ethylene biosynthetic process Ref.3 Traceable author statement. Source: TAIR induction of apoptosis by oxidative stress Inferred from expression pattern. Source: TAIR response to auxin stimulus Inferred from expression pattern. Source: TAIR response to jasmonic acid stimulus Inferred from expression pattern. Source: TAIR response to mechanical stimulus Ref.3 Inferred from expression pattern. Source: TAIR response to wounding Inferred from expression pattern. Source: TAIR ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Ref.5 Inferred from direct assay. Source: TAIR identical protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-2356658,EBI-2356658
ACS1	Q06429	1	EBI-2356658,EBI-2436157
ACS4	Q43309	2	EBI-2356658,EBI-2436015

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 495	495	1-aminocyclopropane-1-carboxylate synthase 6		PRO_0000123900
Sites
	Binding site	58	1	Substrate By similarity
	Binding site	96	1	Substrate By similarity
Amino acid modifications
	Modified residue	280	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	480	1	Phosphoserine Ref.6
	Modified residue	483	1	Phosphoserine Ref.6
	Modified residue	488	1	Phosphoserine Ref.6
Experimental info
	Mutagenesis	480	1	S → D: 40-fold increase in ethylene production; when associated with D-483 and D-488. Ref.6
	Mutagenesis	483	1	S → D: 40-fold increase in ethylene production; when associated with D-480 and D-488. Ref.6
	Mutagenesis	488	1	S → D: 40-fold increase in ethylene production; when associated with D-480 and D-483. Ref.6
	Sequence conflict	56	1	L → F in AAC32251. Ref.4
	Sequence conflict	433	1	R → K in AAC63850. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q9SAR0-1 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 7FA94D3EABBCB4AB	FASTA	495	55,524
	10 20 30 40 50 60 MVAFATEKKQ DLNLLSKIAS GDGHGENSSY FDGWKAYEEN PFHPIDRPDG VIQMGLAENQ 70 80 90 100 110 120 LCGDLMRKWV LKHPEASICT SEGVNQFSDI AIFQDYHGLP EFRQAVAKFM EKTRNNKVKF 130 140 150 160 170 180 DPDRIVMSGG ATGAHETVAF CLANPGDGFL VPTPYYPGFD RDLRWRTGVN LVPVTCHSSN 190 200 210 220 230 240 GFKITVEALE AAYENARKSN IPVKGLLVTN PSNPLGTTLD RECLKSLVNF TNDKGIHLIA 250 260 270 280 290 300 DEIYAATTFG QSEFISVAEV IEEIEDCNRD LIHIVYSLSK DMGLPGLRVG IVYSYNDRVV 310 320 330 340 350 360 QIARKMSSFG LVSSQTQHLI AKMLSDEEFV DEFIRESKLR LAARHAEITT GLDGLGIGWL 370 380 390 400 410 420 KAKAGLFLWM DLRNLLKTAT FDSETELWRV IVHQVKLNVS PGGSFHCHEP GWFRVCFANM 430 440 450 460 470 480 DHKTMETALE RIRVFTSQLE EETKPMAATT MMAKKKKKCW QSNLRLSFSD TRRFDDGFFS 490 PHSPVPPSPL VRAQT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	"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: 14593172] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[3]	"A multi-responsive gene encoding 1-aminocyclopropane-1-carboxylate synthase (ACS6) in mature Arabidopsis leaves." Arteca J.M., Arteca R.N. Plant Mol. Biol. 39:209-219(1999) [PubMed: 10080689] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-495, INDUCTION. Strain: cv. Columbia.
[4]	"Induction of an ACC synthase cDNA by ozone in light-grown Arabidopsis thaliana leaves." Vahala J., Schlagnhaufer C.D., Pell E.J. Physiol. Plantarum 103:45-50(1998) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 53-418, INDUCTION.
[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: 12968022] [Abstract] Cited for: ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, PUTATIVE PROTEOLYTIC PROCESSING.
[6]	"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: 15539472] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-480; SER-483 AND SER-488, MUTAGENESIS OF SER-480; SER-483 AND SER-488.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL096882 Genomic DNA. Translation: CAB51412.1. AL161531 Genomic DNA. Translation: CAB81229.1. AF361097 mRNA. Translation: AAK27237.1. AF428292 mRNA. Translation: AAL16124.1. BT000487 mRNA. Translation: AAN18056.1. U73786 mRNA. Translation: AAC63850.1. U79524 mRNA. Translation: AAC32251.1.
IPI	IPI00518893.
PIR	T13019.
RefSeq	NP_192867.1.
UniGene	At.3654
3D structure databases
SMR	Q9SAR0. Positions 14-435.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9SAR0. 5 interactions.
STRING	Q9SAR0.
Genome annotation databases
GeneID	826730.
GenomeReviews	Gene locus AT4G11280 in contig CT486007_GR.
KEGG	ath:AT4G11280.
NMPDR	fig|3702.1.peg.18796.
Organism-specific databases
TAIR	At4g11280.
Phylogenomic databases
eggNOG	KOG0256.
HOGENOM	HBG317030.
InParanoid	Q9SAR0.
OMA	HPEASIC.
PhylomeDB	Q9SAR0.
Enzyme and pathway databases
BRENDA	4.4.1.14. 302.
Gene expression databases
ArrayExpress	Q9SAR0.
Genevestigator	Q9SAR0.
GermOnline	AT4G11280. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase_major_dom. IPR015421. PyrdxlP-dep_Trfase_major_sub1. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

1A16_ARATH

Accession

Primary (citable) accession number: Q9SAR0
Secondary accession number(s): O82719, Q9SUT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	February 9, 2010
This is version 64 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)