Reviewed, UniProtKB/Swiss-Prot Q9M2Y8 (1A19_ARATH)

Names and origin

Protein names

Recommended name:
    1-aminocyclopropane-1-carboxylate synthase 9
      Short name=ACC synthase 9
    EC=4.4.1.14
Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase 9
    Ethylene-overproduction protein 3

Gene names

Name:	ACS9
Synonyms:	ETO3
Ordered Locus Names:	At3g49700
ORF Names:	T16K5.50

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 › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	470 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Catalytic activity	S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine. Ref.4
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. Interacts (via its C-terminal region) with FEI1 and FEI2.
Tissue specificity	Expressed in roots and siliques. Ref.4
Induction	By cycloheximide (CHX). Ref.4
Post-translational modification	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.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Biophysicochemical properties	Kinetic parameters: KM=40 µM for AdoMet Vmax=324.5 µM/h/mg enzyme pH dependence: Optimum pH is 8.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Fruit ripening
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Inferred from mutant phenotype. Source: TAIR regulation of translation Inferred from direct assay. Source: TAIR ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Ref.4 Inferred from direct assay. Source: TAIR pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro transferase activity, transferring nitrogenous groups Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 470	470	1-aminocyclopropane-1-carboxylate synthase 9		PRO_0000123903
Sites
	Binding site	47	1	Substrate By similarity
	Binding site	85	1	Substrate By similarity
Amino acid modifications
	Modified residue	272	1	N6-(pyridoxal phosphate)lysine By similarity
Experimental info
	Mutagenesis	457	1	V → D in eto3; increases its stability heading to ethylene overproduction.

Sequences

	Sequence		Length	Mass (Da)
	Q9M2Y8-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 2110331C76ACED4E	FASTA	470	53,170
	10 20 30 40 50 60 MKQLSRKVTS NAHGQDSSYF LGWEEYEKNP YDEIKNPNGI IQMGLAENQL CFDLIETWLA 70 80 90 100 110 120 KNPDAAGLKK DGQSIFKELA LFQDYHGLPE FKKALAEFME EIRGNRVTFD PSKIVLAAGS 130 140 150 160 170 180 TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ 190 200 210 220 230 240 AYQQAQKLDL KVKGVLVTNP SNPLGTMLTR RELNLLVDFI TSKNIHLISD EIYSGTVFGF 250 260 270 280 290 300 EQFVSVMDVL KDKNLENSEV SKRVHIVYSL SKDLGLPGFR VGAIYSNDEM VVSAATKMSS 310 320 330 340 350 360 FGLVSSQTQY LLSALLSDKK FTSTYLDENQ KRLKIRQKKL VSGLEAAGIT CLKSNAGLFC 370 380 390 400 410 420 WVDMRHLLDT NTFEAELELW KKIVYDVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA 430 440 450 460 470 MKRLKEYVES TDSRRVISKS SHDRIKSLRK RTVSNWVFRV SWTDRVPDER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 11130713] [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]	"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: 12566591] [Abstract] Cited for: MUTANT ETO3.
[4]	"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.
[5]	"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: 19017745] [Abstract] Cited for: INTERACTION WITH FEI1 AND FEI2.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AL132965 Genomic DNA. Translation: CAB66908.1. AF332391 mRNA. Translation: AAG48755.1.
IPI	IPI00537517.
PIR	T46036.
RefSeq	NP_190539.1.
UniGene	At.743
3D structure databases
HSSP	HSSP built from PDB template 1M7Y based on UniProtKB P37821.
SMR	Q9M2Y8. Positions 10-428.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9M2Y8.
Genome annotation databases
GeneID	824132.
GenomeReviews	Gene locus AT3G49700 in contig BA000014_GR.
KEGG	ath:AT3G49700.
NMPDR	fig|3702.1.peg.16218.
Organism-specific databases
TAIR	At3g49700.
Phylogenomic databases
OMA	IANDESK.
Enzyme and pathway databases
BRENDA	4.4.1.14. 302.
Gene expression databases
ArrayExpress	Q9M2Y8.
Genevestigator	Q9M2Y8.
GermOnline	AT3G49700. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. 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

1A19_ARATH

Accession

Primary (citable) accession number: Q9M2Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	October 1, 2000
Last modified:	November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)