Q43309 (1A14_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
1-aminocyclopropane-1-carboxylate synthase 4
Short name=ACC synthase 4
EC=4.4.1.14

Alternative name(s):
S-adenosyl-L-methionine methylthioadenosine-lyase 4

Gene names

Name:	ACS4
Synonyms:	ACC4
Ordered Locus Names:	At2g22810
ORF Names:	T20K9.2

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	474 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.
Catalytic activity	S-adenosyl-L-methionine = 1-aminocyclopropane-1-carboxylate + methylthioadenosine. Ref.7
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 with XBAT32. Interacts (via its C-terminal region) with ETO1 and EOL1. Ref.8 Ref.9
Tissue specificity	Expressed in roots, leaves and flowers. Ref.1
Induction	By indole-3-acetic acid (IAA) and cycloheximide (CHX). By auxin. Ref.1 Ref.7
Post-translational modification	Ubiquitinated by XBAT32. Ubiquitination probably leads to its subsequent degradation, thus controlling ethylene production. Ref.9
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=15 µM for AdoMet Vmax=31.20 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 Reference proteome
Gene Ontology (GO)
Biological process	cellular response to iron ion Inferred from expression pattern. Source: TAIR 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 Inferred from direct assay Ref.7. Source: TAIR identical protein binding Inferred from physical interaction. Source: IntAct pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-2436015,EBI-2436015
ACS6	Q9SAR0	2	EBI-2436015,EBI-2356658
ACS7	Q9STR4	4	EBI-2436015,EBI-2356842
ACS8	Q9T065	2	EBI-2436015,EBI-2357693

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 474	474	1-aminocyclopropane-1-carboxylate synthase 4		PRO_0000123898
Sites
	Binding site	47	1	Substrate By similarity
	Binding site	85	1	Substrate By similarity
Amino acid modifications
	Modified residue	273	1	N6-(pyridoxal phosphate)lysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q43309 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 98FD27622EAF3C21	FASTA	474	53,795
	10 20 30 40 50 60 MVQLSRKATC NSHGQVSSYF LGWEEYEKNP YDVTKNPQGI IQMGLAENQL CFDLLESWLA 70 80 90 100 110 120 QNTDAACFKR DGQSVFRELA LFQDYHGLSS FKNAFADFMS ENRGNRVSFD SNNLVLTAGA 130 140 150 160 170 180 TSANETLMFC LADPGDAFLL PTPYYPGFDR DLKWRTGVEI VPIQSSSTNG FRITKLALEE 190 200 210 220 230 240 AYEQAKKLDL NVKGILITNP SNPLGTTTTQ TELNILFDFI TKNKNIHLVS DEIYSGTVFN 250 260 270 280 290 300 SSEFISVMEI LKNNQLENTD VLNRVHIVCS LSKDLGLPGF RVGAIYSNDK DVISAATKMS 310 320 330 340 350 360 SFGLVSSQTQ YLLSSLLSDK KFTKNYLREN QKRLKNRQRK LVLGLEAIGI KCLKSNAGLF 370 380 390 400 410 420 CWVDMRPLLR SKTFEAEMDL WKKIVYEVKL NISPGSSCHC EEPGWFRVCF ANMIDETLKL 430 440 450 460 470 ALKRLKMLVD DENSSRRCQK SKSERLNGSR KKTMSNVSNW VFRLSFHDRE AEER

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"ACS4, a primary indoleacetic acid-responsive gene encoding 1-aminocyclopropane-1-carboxylate synthase in Arabidopsis thaliana. Structural characterization, expression in Escherichia coli, and expression characteristics in response to auxin." Abel S., Nguyen M.D., Chow W., Theologis A. J. Biol. Chem. 270:19093-19099(1995) [PubMed: 7642574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia.
[2]	Erratum Abel S., Nguyen M.D., Chow W., Theologis A. J. Biol. Chem. 270:26020-26020(1995)
[3]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"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.
[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 OF 50-81.
[7]	"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, INDUCTION.
[8]	"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: 18808454] [Abstract] Cited for: INTERACTION WITH ETO1 AND EOL1.
[9]	"Arabidopsis RING E3 ligase XBAT32 regulates lateral root production through its role in ethylene biosynthesis." Prasad M.E., Schofield A., Lyzenga W., Liu H., Stone S.L. Plant Physiol. 153:1587-1596(2010) [PubMed: 20511490] [Abstract] Cited for: INTERACTION WITH XBAT32, UBIQUITINATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U23481 mRNA. Translation: AAC49037.1. U23482 Genomic DNA. Translation: AAA85039.1. AC004786 Genomic DNA. Translation: AAC32428.1. AC005617 Genomic DNA. Translation: AAM15065.1. CP002685 Genomic DNA. Translation: AEC07360.1. AF332404 mRNA. Translation: AAG48767.1.
IPI	IPI00519589.
PIR	B84617. G46376.
RefSeq	NP_179866.1. NM_127846.1.
UniGene	At.1549.
3D structure databases
ProteinModelPortal	Q43309.
SMR	Q43309. Positions 4-431.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q43309. 7 interactions.
STRING	Q43309.
Proteomic databases
PRIDE	Q43309.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G22810.1; AT2G22810.1; AT2G22810.
GeneID	816812.
GenomeReviews	Gene locus AT2G22810 in contig CT485783_GR.
KEGG	ath:AT2G22810.
NMPDR	fig|3702.1.peg.9299.
Organism-specific databases
GeneFarm	4050.
TAIR	At2g22810.
Phylogenomic databases
eggNOG	KOG0256.
GeneTree	EPGT00070000028140.
HOGENOM	HBG317030.
InParanoid	Q43309.
OMA	SSCHCEE.
PhylomeDB	Q43309.
ProtClustDB	PLN02450.
Gene expression databases
ArrayExpress	Q43309.
Genevestigator	Q43309.
GermOnline	AT2G22810. 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. IPR015422. PyrdxlP-dep_Trfase_major_sub2. [Graphical view]
Gene3D	G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 2 hits.
KO	K01762.
Pfam	PF00155. Aminotran_1_2. 1 hit. [Graphical view]
PRINTS	PR00753. ACCSYNTHASE.
SUPFAM	SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.
PROSITE	PS00105. AA_TRANSFER_CLASS_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

1A14_ARATH

Accession

Primary (citable) accession number: Q43309
Secondary accession number(s): Q9S9C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	November 1, 1996
Last modified:	December 14, 2011
This is version 86 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program