Reviewed, UniProtKB/Swiss-Prot Q06402 (1A12_ARATH)

Names and origin

Protein names

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

Gene names

Name:	ACS2
Synonyms:	ACC1
Ordered Locus Names:	At1g01480
ORF Names:	F22L4.4

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	496 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.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.
Tissue specificity	High in developing leaves and in flowers. Expressed in roots and siliques. Ref.7
Induction	By ethylene. By indole-3-acetic acid (IAA) and cycloheximide (CHX). Ref.7
Post-translational modification	Phosphorylated on serine residue by MAP kinase (MPK6). Ref.8 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=45 µM for AdoMet Vmax=32 µM/h/mg enzyme pH dependence: Optimum pH is 8.2.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Fruit ripening
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Traceable author statement. Source: TAIR ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Ref.6 Ref.7 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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q06402-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q06402-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-106: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	1-aminocyclopropane-1-carboxylate synthase 2		PRO_0000123897
Sites
	Binding site	55	1	Substrate By similarity
	Binding site	93	1	Substrate By similarity
Amino acid modifications
	Modified residue	279	1	N6-(pyridoxal phosphate)lysine By similarity
	Modified residue	483	1	Phosphoserine Ref.8
	Modified residue	488	1	Phosphoserine Ref.8
	Modified residue	491	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1 – 106	106	Missing in isoform 2.		VSP_009111
	Natural variant	136	1	M → I
Experimental info
	Mutagenesis	206 – 208	3	Missing: Abolishes 1-aminocyclopropane-1-carboxylate synthase function. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 766318AE9B5F1566	FASTA	496	55,532
	10 20 30 40 50 60 MGLPGKNKGA VLSKIATNNQ HGENSEYFDG WKAYDKDPFH LSRNPHGIIQ MGLAENQLCL 70 80 90 100 110 120 DLIKDWVKEN PEASICTLEG IHQFSDIANF QDYHGLKKFR QAIAHFMGKA RGGRVTFDPE 130 140 150 160 170 180 RVVMSGGATG ANETIMFCLA DPGDVFLIPS PYYAAFDRDL RWRTGVEIIP VPCSSSDNFK 190 200 210 220 230 240 LTVDAAEWAY KKAQESNKKV KGLILTNPSN PLGTMLDKDT LTNLVRFVTR KNIHLVVDEI 250 260 270 280 290 300 YAATVFAGGD FVSVAEVVND VDISEVNVDL IHIVYSLSKD MGLPGFRVGI VYSFNDSVVS 310 320 330 340 350 360 CARKMSSFGL VSSQTQLMLA SMLSDDQFVD NFLMESSRRL GIRHKVFTTG IKKADIACLT 370 380 390 400 410 420 SNAGLFAWMD LRHLLRDRNS FESEIELWHI IIDRVKLNVS PGSSFRCTEP GWFRICFANM 430 440 450 460 470 480 DDDTLHVALG RIQDFVSKNK NKIVEKASEN DQVIQNKSAK KLKWTQTNLR LSFRRLYEDG 490 LSSPGIMSPH SPLLRA
	Isoform 2. Checksum: 7A7A592FBA0B70DE	FASTA	390	43,537
	10 20 30 40 50 60 MGKARGGRVT FDPERVVMSG GATGANETIM FCLADPGDVF LIPSPYYAAF DRDLRWRTGV 70 80 90 100 110 120 EIIPVPCSSS DNFKLTVDAA EWAYKKAQES NKKVKGLILT NPSNPLGTML DKDTLTNLVR 130 140 150 160 170 180 FVTRKNIHLV VDEIYAATVF AGGDFVSVAE VVNDVDISEV NVDLIHIVYS LSKDMGLPGF 190 200 210 220 230 240 RVGIVYSFND SVVSCARKMS SFGLVSSQTQ LMLASMLSDD QFVDNFLMES SRRLGIRHKV 250 260 270 280 290 300 FTTGIKKADI ACLTSNAGLF AWMDLRHLLR DRNSFESEIE LWHIIIDRVK LNVSPGSSFR 310 320 330 340 350 360 CTEPGWFRIC FANMDDDTLH VALGRIQDFV SKNKNKIVEK ASENDQVIQN KSAKKLKWTQ 370 380 390 TNLRLSFRRL YEDGLSSPGI MSPHSPLLRA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning, genetic mapping, and expression analysis of an Arabidopsis thaliana gene that encodes 1-aminocyclopropane-1-carboxylate synthase." van der Straeten D., Rodrigues-Pousada R.A., Villarroel R., Hanley S., Goodman H.M., Van Montagu M. Proc. Natl. Acad. Sci. U.S.A. 89:9969-9973(1992) [PubMed: 1357670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1), VARIANT ILE-136. Strain: cv. Columbia.
[2]	"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 / MRNA] (ISOFORM 1). Strain: cv. Columbia.
[3]	"Sequence analysis of a 40-kb Arabidopsis thaliana genomic region located at the top of chromosome 1." Terryn N., Gielen J., De Keyser A., Van Den Daele H., Ardiles W., Neyt P., De Clercq R., Coppieters J., Dehais P., Villarroel R., Rouze P., van Montagu M. Gene 215:11-17(1998) [PubMed: 9666060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORM 1). Strain: cv. Columbia.
[4]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed: 11130712] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. 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] (ISOFORMS 1 AND 2). Strain: cv. Columbia.
[6]	"Characterization of two members (ACS1 and ACS3) of the 1-aminocyclopropane-1-carboxylate synthase gene family of Arabidopsis thaliana." Liang X.-W., Oono Y., Shen N.F., Koehler C., Li K., Scolnik P.A., Theologis A. Gene 167:17-24(1995) [PubMed: 8566772] [Abstract] Cited for: MUTAGENESIS OF 206-THR--PRO-208. Strain: cv. Columbia.
[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, TISSUE SPECIFICITY, INDUCTION, PUTATIVE PROTEOLYTIC PROCESSING.
[8]	"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: PHOSPHORYLATION AT SER-483; SER-488 AND SER-491.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Z12614 Genomic DNA. Translation: CAA78260.1. M95594 Genomic DNA. Translation: AAA97516.1. M95595 mRNA. Translation: AAB59298.1. Y12776 Genomic DNA. Translation: CAA73310.1. AC061957 Genomic DNA. Translation: AAF81308.1. AF334719 mRNA. Translation: AAG50097.1. AY052207 mRNA. Translation: AAK97678.1. AY143877 mRNA. Translation: AAN28816.1.
IPI	IPI00516870. IPI00530308.
PIR	A47199.
RefSeq	NP_171655.1. NP_849572.1.
UniGene	At.164
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q06402. 1 interaction.
STRING	Q06402.
Genome annotation databases
GeneID	837082.
GenomeReviews	Gene locus AT1G01480 in contig CT485782_GR.
KEGG	ath:AT1G01480.
Organism-specific databases
GeneFarm	4049.
TAIR	At1g01480.
Phylogenomic databases
OMA	NEFREVA
Enzyme and pathway databases
BRENDA	4.4.1.14. 302.
Gene expression databases
ArrayExpress	Q06402.
Genevestigator	Q06402.
GermOnline	AT1G01480. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001176. ACC_synthase. IPR004839. Aminotransferase_I/II. IPR004838. NHTrfase_class1_PyrdxlP-BS. IPR015424. PyrdxlP-dep_Trfase_major. 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

1A12_ARATH

Accession

Primary (citable) accession number: Q06402
Secondary accession number(s): Q941E7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	November 24, 2009
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)