P18485 (1A12_SOLLC) Reviewed, UniProtKB/Swiss-Prot

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):
Le-ACS2
Short name=ACS-2
S-adenosyl-L-methionine methylthioadenosine-lyase 2

Gene names

Name:	ACS2
Synonyms:	ACC2, PCVV4A

Organism

Solanum lycopersicum (Tomato) (Lycopersicon esculentum)

Taxonomic identifier

4081 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Solanales › Solanaceae › Solanoideae › Solaneae › Solanum › Lycopersicon

Protein attributes

Sequence length	485 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.
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. Ref.3
Induction	Hormones, such as auxin, environmental factors, such as mechanical wounding and a number of chemicals.
Post-translational modification	Phosphorylated on Ser 460; phosphorylation may regulate its turnover. Ref.5 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.

Ontologies

Keywords
Biological process	Ethylene biosynthesis Fruit ripening
Ligand	Pyridoxal phosphate S-adenosyl-L-methionine
Molecular function	Lyase
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
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 Inferred from electronic annotation. Source: EC 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 – 485

485

1-aminocyclopropane-1-carboxylate synthase 2

PRO_0000123912

Sites

Binding site

55

1

Substrate

Binding site

92

1

Substrate

Amino acid modifications

Modified residue

278

1

N6-(pyridoxal phosphate)lysine

Modified residue

460

1

Phosphoserine Ref.5

Experimental info

Mutagenesis

92

1

Y → F: Loss of function; when expressed alone in E.Coli. Partially complemented; when coexpressed with another ACS2 protein mutated on K-278. Ref.3

Mutagenesis

278

1

K → A: Loss of function; when expressed alone in E.Coli. Partially complemented; when coexpressed with another ACS2 protein mutated on Y-72. Ref.3

Mutagenesis

286

1

R → L: Loss of function; due to a strong reduction in both substrate and pyridoxal phosphate binding. Ref.4

Mutagenesis

460

1

S → G: Abolishes phosphorylation.

Mutagenesis

462

1

S → G: No effect.

Sequence conflict

124

1

A → V in CAA41856. Ref.1

Sequence conflict

322

1

L → P in AAA81580. Ref.2

Sequence conflict

399

1

P → L in AAA81580. Ref.2

Secondary structure

1

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485

Helix Strand Turn

Details...

Helix

14 – 17

4

Helix

29 – 36

8

Turn

41 – 43

3

Beta strand

47 – 50

4

Helix

60 – 66

7

Beta strand

69 – 71

3

Helix

83 – 88

6

Helix

96 – 109

14

Turn

110 – 113

4

Helix

118 – 120

3

Beta strand

122 – 125

4

Helix

126 – 138

13

Beta strand

144 – 150

7

Helix

155 – 158

4

Turn

159 – 163

5

Beta strand

166 – 170

5

Helix

174 – 176

3

Helix

182 – 194

13

Beta strand

199 – 207

9

Turn

209 – 211

3

Helix

217 – 228

12

Turn

229 – 231

3

Beta strand

233 – 237

5

Helix

241 – 243

3

Beta strand

246 – 248

3

Helix

253 – 256

4

Helix

260 – 262

3

Helix

267 – 269

3

Beta strand

270 – 281

12

Helix

283 – 285

3

Beta strand

287 – 293

7

Helix

295 – 304

10

Helix

305 – 308

4

Helix

312 – 322

11

Helix

325 – 352

28

Beta strand

361 – 369

9

Helix

371 – 373

3

Beta strand

375 – 378

4

Helix

379 – 391

13

Helix

400 – 403

4

Beta strand

410 – 414

5

Beta strand

416 – 418

3

Helix

420 – 435

16

Sequences

	Sequence		Length	Mass (Da)
	P18485 [UniParc]. Last modified October 1, 1994. Version 2. Checksum: 40B3F55B5EF0D9C7	FASTA	485	54,663
	10 20 30 40 50 60 MGFEIAKTNS ILSKLATNEE HGENSPYFDG WKAYDSDPFH PLKNPNGVIQ MGLAENQLCL 70 80 90 100 110 120 DLIEDWIKRN PKGSICSEGI KSFKAIANFQ DYHGLPEFRK AIAKFMEKTR GGRVRFDPER 130 140 150 160 170 180 VVMAGGATGA NETIIFCLAD PGDAFLVPSP YYPAFNRDLR WRTGVQLIPI HCESSNNFKI 190 200 210 220 230 240 TSKAVKEAYE NAQKSNIKVK GLILTNPSNP LGTTLDKDTL KSVLSFTNQH NIHLVCDEIY 250 260 270 280 290 300 AATVFDTPQF VSIAEILDEQ EMTYCNKDLV HIVYSLSKDM GLPGFRVGII YSFNDDVVNC 310 320 330 340 350 360 ARKMSSFGLV STQTQYFLAA MLSDEKFVDN FLRESAMRLG KRHKHFTNGL EVVGIKCLKN 370 380 390 400 410 420 NAGLFCWMDL RPLLRESTFD SEMSLWRVII NDVKLNVSPG SSFECQEPGW FRVCFANMDD 430 440 450 460 470 480 GTVDIALARI RRFVGVEKSG DKSSSMEKKQ QWKKNNLRLS FSKRMYDESV LSPLSSPIPP SPLVR

References

[1]	"1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a multigene family whose transcription is induced during fruit and floral senescence." Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F., Nagy B.P., Taylor L.P., Campbell A.D., Theologis A. J. Mol. Biol. 222:937-961(1991) [PubMed: 1762159] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA]. Tissue: Etiolated hypocotyl.
[2]	"Cloning and sequence of two different cDNAs encoding 1-aminocyclopropane-1-carboxylate synthase in tomato." van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M. Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990) [PubMed: 2191304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: cv. Orlando. Tissue: Fruit.
[3]	"Complementation analysis of mutants of 1-aminocyclopropane-1-carboxylate synthase reveals the enzyme is a dimer with shared active sites." Tarun A.S., Theologis A. J. Biol. Chem. 273:12509-12514(1998) [PubMed: 9575209] [Abstract] Cited for: HOMODIMERIZATION, MUTAGENESIS OF TYR-92 AND LYS-278.
[4]	"The multiple roles of conserved arginine 286 of 1-aminocyclopropane-1-carboxylate synthase. Coenzyme binding, substrate binding, and beyond." Zhou H., Wang H.W., Zhu K., Sui S.F., Xu P., Yang S.F., Li N. Plant Physiol. 121:913-919(1999) [PubMed: 10557240] [Abstract] Cited for: MUTAGENESIS OF ARG-286.
[5]	"Phosphorylation of tomato 1-aminocyclopropane-1-carboxylic acid synthase, LE-ACS2, at the C-terminal region." Tatsuki M., Mori H. J. Biol. Chem. 276:28051-28057(2001) [PubMed: 11375393] [Abstract] Cited for: PHOSPHORYLATION AT SER-460.
[6]	"Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms." Huai Q., Xia Y., Chen Y., Callahan B., Li N., Ke H. J. Biol. Chem. 276:38210-38216(2001) [PubMed: 11431475] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-438.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X59139 Genomic DNA. Translation: CAA41855.1.
X59145 mRNA. Translation: CAA41856.1.
M34289 mRNA. Translation: AAA81580.1.

PIR

S19677.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IAX	X-ray	2.80	A/B	11-438	[»]
1IAY	X-ray	2.70	A	11-438	[»]

ProteinModelPortal

P18485.

SMR

P18485. Positions 11-438.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

BRENDA

4.4.1.14. 3101.

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.

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

1A12_SOLLC

Accession

Primary (citable) accession number: P18485

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	October 1, 1994
Last modified:	May 31, 2011
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program