Reviewed, UniProtKB/Swiss-Prot Q9S9U6 (1A111_ARATH)

Names and origin

Protein names

Recommended name:
    1-aminocyclopropane-1-carboxylate synthase 11
      Short name=ACC synthase 11
    EC=4.4.1.14
Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase 11

Gene names

Name:	ACS11
Ordered Locus Names:	At4g08040
ORF Names:	T17A2.2

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	460 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.3
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. Ref.3
Induction	By indole-3-acetic acid (IAA) and cycloheximide (CHX). Ref.3
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=25 µM for AdoMet Vmax=25.20 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 electronic annotation. Source: UniProtKB-KW ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Ref.3 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 – 460	460	1-aminocyclopropane-1-carboxylate synthase 11		PRO_0000123905
Sites
	Binding site	45	1	Substrate By similarity
	Binding site	83	1	Substrate By similarity
Amino acid modifications
	Modified residue	267	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9S9U6-1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 1A056347680E7E2F	FASTA	460	51,799
	10 20 30 40 50 60 MLSSKVVGDS HGQDSSYFLG WQEYEKNPFH ESFNTSGIVQ MGLAENQLSF DLIEKWLEEH 70 80 90 100 110 120 PEVLGLKKND ESVFRQLALF QDYHGLPAFK DAMAKFMGKI RENKVKFDTN KMVLTAGSTS 130 140 150 160 170 180 ANETLMFCLA NPGDAFLIPA PYYPGFDRDL KWRTGVEIVP IHCVSSNGYK ITEDALEDAY 190 200 210 220 230 240 ERALKHNLNV KGVLITNPSN PLGTSTTREE LDLLLTFTST KKIHMVSDEI YSGTVFDSPE 250 260 270 280 290 300 FTSVLEVAKD KNMGLDGKIH VVYSLSKDLG LPGFRVGLIY SNNEKVVSAA TKMSSFGLIS 310 320 330 340 350 360 SQTQHLLANL LSDERFTTNY LEENKKRLRE RKDRLVSGLK EAGISCLKSN AGLFCWVDLR 370 380 390 400 410 420 HLLKSNTFEA EHSLWTKIVC EVGLNISPGS SCHCDEPGWF RVCFANMSDQ TMEVAMDRVK 430 440 450 460 GFVDNNNGGK QKRTMWDTRR RSLINKWVSK LSSVTCESER

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]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF160183 Genomic DNA. Translation: AAD48074.1. AL161509 Genomic DNA. Translation: CAB81141.1. AF332405 mRNA. Translation: AAG48768.1.
IPI	IPI00525915.
PIR	B85079.
RefSeq	NP_567330.1.
UniGene	At.4151
3D structure databases
HSSP	HSSP built from PDB template 1B8G based on UniProtKB P37821.
SMR	Q9S9U6. Positions 10-423.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9S9U6.
Genome annotation databases
GeneID	826317.
GenomeReviews	Gene locus AT4G08040 in contig CT486007_GR.
KEGG	ath:AT4G08040.
NMPDR	fig|3702.1.peg.18455.
Organism-specific databases
TAIR	At4g08040.
Phylogenomic databases
OMA	VEIVPIH.
Enzyme and pathway databases
BRENDA	4.4.1.14. 302.
Gene expression databases
ArrayExpress	Q9S9U6.
Genevestigator	Q9S9U6.
GermOnline	AT4G08040. 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. 2 hits.
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

1A111_ARATH

Accession

Primary (citable) accession number: Q9S9U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	May 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)