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

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) (Pyrus malus)

Taxonomic identifier

3750 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › fabids › Rosales › Rosaceae › Amygdaloideae › Maleae › Malus

Protein attributes

Sequence length	473 AA.
Sequence status	Complete.
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 Inferred by curator PubMed 11470512. Source: UniProtKB fruit ripening Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	1-aminocyclopropane-1-carboxylate synthase activity Inferred from direct assay PubMed 11470512. Source: UniProtKB protein homodimerization activity Non-traceable author statement PubMed 11470512. Source: UniProtKB pyridoxal phosphate binding Non-traceable author statement PubMed 11470512. Source: UniProtKB
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...

Turn

6 – 8

3

Helix

18 – 28

11

Beta strand

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

137 – 143

7

Helix

148 – 151

4

Turn

152 – 156

5

Beta strand

159 – 164

6

Helix

167 – 169

3

Helix

175 – 187

13

Beta strand

192 – 200

9

Turn

202 – 204

3

Helix

210 – 223

14

Beta strand

226 – 230

5

Helix

234 – 236

3

Beta strand

239 – 241

3

Helix

246 – 249

4

Turn

250 – 254

5

Beta strand

256 – 260

5

Helix

261 – 264

4

Beta strand

265 – 275

11

Helix

278 – 280

3

Beta strand

282 – 288

7

Helix

290 – 299

10

Helix

300 – 302

3

Helix

307 – 318

12

Helix

320 – 346

27

Turn

347 – 349

3

Beta strand

357 – 364

8

Helix

366 – 368

3

Beta strand

369 – 373

5

Helix

374 – 386

13

Helix

395 – 398

4

Beta strand

405 – 409

5

Beta strand

411 – 413

3

Helix

415 – 432

18

Sequences

	Sequence		Length	Mass (Da)
	P37821 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PIR

T16999.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]
3PIU	X-ray	1.35	A	1-435	[»]

ProteinModelPortal

P37821.

SMR

P37821. Positions 3-431.

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Enzyme and pathway databases

SABIO-RK

P37821.

UniPathway

UPA00384; UER00562.

Family and domain databases

Gene3D

3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.

InterPro

IPR004839. Aminotransferase_I/II.
IPR004838. NHTrfase_class1_PyrdxlP-BS.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Pfam

PF00155. Aminotran_1_2. 1 hit.
[Graphical view]

SUPFAM

SSF53383. PyrdxlP-dep_Trfase_major. 1 hit.

PROSITE

PS00105. AA_TRANSFER_CLASS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P37821.

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:	April 3, 2013
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program