Reviewed, UniProtKB/Swiss-Prot Q37001 (1A15_ARATH)

Names and origin

Protein names

Recommended name:
    1-aminocyclopropane-1-carboxylate synthase 5
      Short name=ACC synthase 5
    EC=4.4.1.14
Alternative name(s):
    S-adenosyl-L-methionine methylthioadenosine-lyase 5
    Ethylene-overproduction protein 2

Gene names

Name:	ACS5
Synonyms:	ACC5, ETO2
Ordered Locus Names:	At5g65800
ORF Names:	MPA24.15, F6H11.90

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.8
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, FEI2, ETO1, EOL1 and EOL2.
Tissue specificity	Expressed in roots and siliques. Ref.8
Induction	By indole-3-acetic acid (IAA) and cycloheximide (CHX). In response to low dose of cytokinin. Ref.8
Post-translational modification	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.
Sequence similarities	Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family.
Biophysicochemical properties	Kinetic parameters: KM=37 µM for S-adenosyl-L-methionine Vmax=81.70 µM/h/mg enzyme pH dependence: Optimum pH is 7.8.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Fruit ripening
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Lyase
PTM	Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Inferred from mutant phenotype. Source: TAIR response to cytokinin stimulus Inferred from mutant phenotype. Source: TAIR ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Ref.8 Inferred from direct assay. Source: TAIR protein binding Ref.9 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
ETO1	O65020	2	EBI-593450,EBI-593440

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 470	470	1-aminocyclopropane-1-carboxylate synthase 5		PRO_0000123899
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	201	1	S → F in cin5-3; defective in cytokinin induced ethylene.
	Mutagenesis	269	1	S → N in cin5-2; defective in cytokinin induced ethylene.
	Mutagenesis	459 – 470	12	RVSWT…VPDER → PGFMDRSCT in eto2; increases its stability leading to ethylene overproduction.

Sequences

	Sequence		Length	Mass (Da)
	Q37001-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 8B2527C9B52AE19A	FASTA	470	53,313
	10 20 30 40 50 60 MKQLSTKVTS NGHGQDSSYF LGWEEYEKNP YDEIKNPNGM IQMGLAENQL CFDLIESWLT 70 80 90 100 110 120 KNPDAASLKR NGQSIFRELA LFQDYHGMPE FKKAMAEFME EIRGNRVTFD PKKIVLAAGS 130 140 150 160 170 180 TSANETLMFC LAEPGDAFLL PTPYYPGFDR DLKWRTGAEI VPIHCSSSNG FQITESALQQ 190 200 210 220 230 240 AYQQAQKLDL KVKGVLVTNP SNPLGTALTR RELNLLVDFI TSKNIHLISD EIYSGTMFGF 250 260 270 280 290 300 EQFISVMDVL KDKKLEDTEV SKRVHVVYSL SKDLGLPGFR VGAIYSNDEM IVSAATKMSS 310 320 330 340 350 360 FGLVSSQTQY LLSALLSDKK FTSQYLEENQ KRLKSRQRRL VSGLESAGIT CLRSNAGLFC 370 380 390 400 410 420 WVDMRHLLDT NTFEAELDLW KKIVYNVKLN ISPGSSCHCT EPGWFRVCFA NMSEDTLDLA 430 440 450 460 470 LKRLKTFVES TDCGRMISRS SHERLKSLRK KTVSNWVFRV SWTDRVPDER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 9011084] [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: 9628582] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"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.
[5]	"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.
[6]	"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: 1438312] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 50-81. Strain: cv. Columbia.
[7]	"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 ETO2.
[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: 12968022] [Abstract] Cited for: ENZYME ACTIVITY, TISSUE SPECIFICITY, INDUCTION, PUTATIVE PROTEOLYTIC PROCESSING.
[9]	"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: 15118728] [Abstract] Cited for: DEGRADATION, INTERACTION WITH ETO1; EOL1 AND EOL2.
[10]	"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	L29261 mRNA. Translation: AAA87292.1. L29260 Genomic DNA. Translation: AAA87291.1. AB010075, AB020743 Genomic DNA. Translation: BAB10687.1. AL021684 Genomic DNA. Translation: CAA16680.1. AF334720 mRNA. Translation: AAG50098.1. AK229087 mRNA. Translation: BAF00967.1.
IPI	IPI00534058.
PIR	S71174.
RefSeq	NP_201381.1.
UniGene	At.1918
3D structure databases
HSSP	HSSP built from PDB template 1B8G based on UniProtKB P37821.
SMR	Q37001. Positions 17-428.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q37001. 3 interactions.
STRING	Q37001.
Genome annotation databases
GeneID	836709.
GenomeReviews	Gene locus AT5G65800 in contig BA000015_GR.
KEGG	ath:AT5G65800.
NMPDR	fig|3702.1.peg.28666.
Organism-specific databases
TAIR	At5g65800.
Phylogenomic databases
OMA	PVHLESE.
Enzyme and pathway databases
BRENDA	4.4.1.14. 302.
Gene expression databases
ArrayExpress	Q37001.
Genevestigator	Q37001.
GermOnline	AT5G65800. 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

1A15_ARATH

Accession

Primary (citable) accession number: Q37001
Secondary accession number(s): O49537, Q0WPI2, Q9S9C3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)