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InterPro: IPR001176 1-aminocyclopropane-1-carboxylate synthase

Protein matches Help

UniProtKB

Matches:

5765 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR001176 ACC_synthase

Type

Family

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00753	ACCSYNTHASE	5765
Signatures in BioMart

InterPro Relationships Help

Contains

IPR004839 Aminotransferase, class I/II
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0016847 1-aminocyclopropane-1-carboxylate synthase activity

InterPro annotation

Entry Details in BioMart

Abstract

1-aminocyclopropane-1-carboxylate (ACC) synthase (EC:4.4.1.14), a Class I aminotransferase, is the key regulatory enzyme in the biosynthetic pathway of the plant hormone ethylene. It catalyses the formation of 1-aminocyclopropane-1-carboxylate, a direct precursor of ethylene in higher plants. The enzyme functions as a homodimer and requires pyridoxal-5'-phosphate as a cofactor [1].

Structural links Help

PDB - click here

SCOP: c.67.1.1 , c.67.1.4

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

Blocks: IPB001176

COMe: PRX000830

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001176

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2XLL2 1-aminocyclopropane-1-carboxylate synthase 1

P17735 Tyrosine aminotransferase

P47039 Probable kynurenine--oxoglutarate transaminase BNA3

Q06402 1-aminocyclopropane-1-carboxylate synthase 2

Q71RI9 Kynurenine--oxoglutarate transaminase 3

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR005957	Tyrosine aminotransferase
IPR011715	Tyrosine aminotransferase ubiquitination region
IPR004838	Aminotransferases, class-I, pyridoxal-phosphate-binding site
IPR004839	Aminotransferase, class I/II
IPR015424	Pyridoxal phosphate-dependent transferase, major domain
IPR005958	Tyrosine/nicotianamine aminotransferase
IPR015422	Pyridoxal phosphate-dependent transferase, major region, subdomain 2
IPR001176	1-aminocyclopropane-1-carboxylate synthase
IPR015421	Pyridoxal phosphate-dependent transferase, major region, subdomain 1
	SWISS-MODEL
	PDB Chain
	ModBase

Publications Open in usermanual
1.	Rottmann WH, Peter GF, Oeller PW, Keller JA, Shen NF, Nagy BP, Taylor LP, Campbell AD, Theologis A. 1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a multigene family whose transcription is induced during fruit and floral senescence. J. Mol. Biol. 222 937-61 1991 [PubMed: 1762159] http://dx.doi.org/10.1016/0022-2836(91)90587-V

Additional Reading Open in usermanual
	Capitani G, Tschopp M, Eliot AC, Kirsch JF, Grutter MG. Structure of ACC synthase inactivated by the mechanism-based inhibitor L-vinylglycine. FEBS Lett. 579 2005 2458-62 [PubMed: 15848188] http://dx.doi.org/10.1016/j.febslet.2005.03.048
	Rossi F, Han Q, Li J, Li J, Rizzi M. Crystal structure of human kynurenine aminotransferase I. J. Biol. Chem. 279 2004 50214-20 [PubMed: 15364907] http://dx.doi.org/10.1074/jbc.M409291200
	Han Q, Gao YG, Robinson H, Li J. Structural insight into the mechanism of substrate specificity of aedes kynurenine aminotransferase. Biochemistry 47 2008 1622-30 [PubMed: 18186649] http://dx.doi.org/10.1021/bi701800j
	Schwarzenbacher R, Jaroszewski L, von Delft F, Abdubek P, Ambing E, Biorac T, Brinen LS, Canaves JM, Cambell J, Chiu HJ, Dai X, Deacon AM, DiDonato M, Elsliger MA, Eshagi S, Floyd R, Godzik A, Grittini C, Grzechnik SK, Hampton E, Karlak C, Klock HE, Koesema E, Kovarik JS, Kreusch A, Kuhn P, Lesley SA, Levin I, McMullan D, McPhillips TM, Miller MD, Morse A, Moy K, Ouyang J, Page R, Quijano K, Robb A, Spraggon G, Stevens RC, van den Bedem H, Velasquez J, Vincent J, Wang X, West B, Wolf G, Xu Q, Hodgson KO, Wooley J, Wilson IA. Crystal structure of an aspartate aminotransferase (TM1255) from Thermotoga maritima at 1.90 A resolution. Proteins 55 2004 759-63 [PubMed: 15103638] http://dx.doi.org/10.1002/prot.10646
	Han Q, Gao YG, Robinson H, Ding H, Wilson S, Li J. Crystal structures of Aedes aegypti kynurenine aminotransferase. FEBS J. 272 2005 2198-206 [PubMed: 15853804] http://dx.doi.org/10.1111/j.1742-4658.2005.04643.x

InterPro 23.1