Reviewed, UniProtKB/Swiss-Prot P37821 (1A1C_MALDO)

Names and origin

Protein names

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

Gene names

Name:

ACS-1

Organism

Malus domestica (Apple) (Malus sylvestris)

Taxonomic identifier

3750 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids I › Rosales › Rosaceae › Maloideae › Malus

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants.
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.
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
Technical term	3D-structure
Gene Ontology (GO)
Biological process	ethylene biosynthetic process Non-traceable author statement. Source: UniProtKB ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from direct assay. Source: UniProtKB protein homodimerization activity Non-traceable author statement. Source: UniProtKB pyridoxal phosphate binding Non-traceable author statement. Source: UniProtKB 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 – 473

473

1-aminocyclopropane-1-carboxylate synthase

PRO_0000123915

Amino acid modifications

Modified residue

273

1

N6-(pyridoxal phosphate)lysine

Experimental info

Sequence conflict

15

1

Q → E in AAA03472. Ref.3

Sequence conflict

101

1

E → K in AAA03472. Ref.3

Secondary structure

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473

Helix Strand Turn

Details...

Helix

21 – 28

8

Turn

33 – 35

3

Beta strand

39 – 42

4

Helix

52 – 61

10

Helix

65 – 67

3

Helix

76 – 81

6

Helix

89 – 102

14

Turn

103 – 105

3

Helix

111 – 113

3

Beta strand

114 – 118

5

Helix

119 – 131

13

Beta strand

136 – 143

8

Helix

148 – 151

4

Turn

152 – 156

5

Beta strand

159 – 163

5

Helix

167 – 169

3

Helix

175 – 187

13

Beta strand

191 – 200

10

Turn

202 – 204

3

Helix

210 – 223

14

Beta strand

226 – 230

5

Helix

234 – 236

3

Beta strand

239 – 241

3

Helix

246 – 252

7

Helix

261 – 263

3

Beta strand

264 – 271

8

Turn

272 – 274

3

Helix

278 – 280

3

Beta strand

282 – 288

7

Helix

290 – 299

10

Helix

300 – 303

4

Helix

307 – 317

11

Helix

320 – 346

27

Turn

347 – 349

3

Beta strand

357 – 364

8

Helix

366 – 368

3

Beta strand

370 – 373

4

Helix

374 – 386

13

Helix

395 – 398

4

Beta strand

405 – 409

5

Helix

415 – 428

14

Sequences

	Sequence		Length	Mass (Da)
	P37821-1 [UniParc]. Last modified July 15, 1998. Version 2. Checksum: 6ACA20759615E75D	FASTA	473	53,251
	10 20 30 40 50 60 MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL CFDLLESWLA 70 80 90 100 110 120 KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA EIRGNKVTFD PNHLVLTAGA 130 140 150 160 170 180 TSANETFIFC LADPGEAVLI PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITETALEE 190 200 210 220 230 240 AYQEAEKRNL RVKGVLVTNP SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS 250 260 270 280 290 300 PSFISVMEVL KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS 310 320 330 340 350 360 SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI SCLNGNAGLF 370 380 390 400 410 420 CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC TEPGWFRVCF ANLPERTLDL 430 440 450 460 470 AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS RRQSLTKWVS RLSFDDRGPI PGR

References

[1]	"A full-length cDNA encoding 1-aminocyclopropane-1-carboxylate synthase from apple." Lay-Yee M., Knighton M.L. Plant Physiol. 107:1017-1018(1995) [PubMed: 7716231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: cv. Golden Delicious. Tissue: Fruit cortical tissue.
[2]	Harada T., Sunako T., Sakuraba W., Goto S., Senda M., Akada S., Ishikawa R., Niizeki M. Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: cv. Golden Delicious.
[3]	"Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase and expression of its mRNA in ripening apple fruit." Dong J.G., Kim W.T., Yip W.K., Thompson G.A., Li L., Bennett A.B., Yang S.F. Planta 185:38-45(1991) Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-473. Strain: cv. Golden Delicious. Tissue: Fruit.
[4]	"Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene." Capitani G., Hohenester E., Feng L., Storici P., Kirsch J.F., Jansonius J.N. J. Mol. Biol. 294:745-756(1999) [PubMed: 10610793] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

L31347 mRNA. Translation: AAA73941.1.
U89156 Genomic DNA. Translation: AAB68617.1.
U03294 mRNA. Translation: AAA03472.1.

PIR

T16999.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1B8G	X-ray	2.37	A/B	3-431	[»]
1M4N	X-ray	2.01	A	1-435	[»]
1M7Y	X-ray	1.60	A	1-435	[»]
1YNU	X-ray	2.25	A	1-473	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

4.4.1.14. 66979.

Family and domain databases

InterPro

IPR001176. ACC_synthase.
IPR004839. Aminotrans_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

1A1C_MALDO

Accession

Primary (citable) accession number: P37821
Secondary accession number(s): O04993, Q40278

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 15, 1998
Last modified:	June 16, 2009
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)