EBI Databases InterPro	Search Open in usermanual InterPro:
Jump to: InterProScan Databases Documentation FTP site Help Click on the icon for context sensitive help from the user manual. Advanced search

InterPro: IPR006220 Anthranilate synthase component II/delta crystallin

Protein matches Help

UniProtKB

Matches:

6034 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

IPR006220 Anth_synthII

Secondary

IPR002385

Type

Domain

Signatures Help

Database	ID	Name	Proteins
PRINTS	PR00097	ANTSNTHASEII	6034
Signatures in BioMart

InterPro Relationships Help

Parent

IPR001317 Carbamoyl phosphate synthase, GATase domain

Children

IPR004739 GMP synthase, N-terminal
IPR006221 Glutamine amidotransferase of anthranilate synthase

GO Term annotation Help

Process

GO:0009058 biosynthetic process

Function

GO:0003824 catalytic activity

InterPro annotation

Entry Details in BioMart

Abstract

Anthranilate synthase (ASase) is a tetrameric protein comprising two copies each of components I and II [1]. The protein catalyses the first step in the tryptophan biosynthetic pathway, namely the conversion of chorismate and an ammonium ion to anthranilate. Component I obtains this ion from ammonia, whereas component II obtains the ion from glutamine using the glutamine amidotransferase (GATase) activity [2].

In some bacteria, such as Escherichia coli, component II can be much larger than in other organisms, due to the presence of phosphoribosyl-anthranilate transferase (PRTase) activity. This is the second step in tryptophan biosynthesis and results in the addition of 5-phosphoribosyl-1-pyrophosphate to anthranilate to create N-5'-phosphoribosyl-anthranilate. Some studies have suggested that the larger component II could have arisen by gene fusion, a hypothesis supported by the fact that the two activities are found in discrete domains that are physically separated in the 3D model.

Structural links Help

PDB - click here

SCOP: c.23.16.1

CATH: 3.40.50.880

Database links Help

Enzyme: EC:6.3.5

Blocks: IPB006220

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR006220

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P00937 Anthranilate synthase component 2

P49057 GMP synthase [glutamine-hydrolyzing]

P49915 GMP synthase [glutamine-hydrolyzing]

Q09580 Probable GMP synthase [glutamine-hydrolyzing]

Q3THK7 GMP synthase [glutamine-hydrolyzing]

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR011702	Glutamine amidotransferase superfamily
IPR013785	Aldolase-type TIM barrel
IPR013798	Indole-3-glycerol phosphate synthase
IPR014729	Rossmann-like alpha/beta/alpha sandwich fold
IPR018317	Queuosine synthesis-like
IPR018318	tRNA methyl transferase-like
IPR017926	Glutamine amidotransferase type 1
IPR006221	Glutamine amidotransferase of anthranilate synthase
IPR004739	GMP synthase, N-terminal
IPR006220	Anthranilate synthase component II/delta crystallin
IPR001468	Indole-3-glycerol phosphate synthase, central region
IPR000991	Glutamine amidotransferase class-I, C-terminal
IPR011060	Ribulose-phosphate binding barrel
IPR001674	GMP synthase, C-terminal
IPR001317	Carbamoyl phosphate synthase, GATase domain
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL

Publications Open in usermanual
1.	Bae YM, Holmgren E, Crawford IP. Rhizobium meliloti anthranilate synthase gene: cloning, sequence, and expression in Escherichia coli. J. Bacteriol. 171 3471-8 1989 [PubMed: 2656657] http://ukpmc.ac.uk/articlerender.cgi?tool=EBI&pubmedid=2656657
2.	Horowitz H, Christie GE, Platt T. Nucleotide sequence of the trpD gene, encoding anthranilate synthetase component II of Escherichia coli. J. Mol. Biol. 156 245-56 1982 [PubMed: 6283099] http://dx.doi.org/10.1016/0022-2836(82)90326-6

Additional Reading Open in usermanual
	Morollo AA, Eck MJ. Structure of the cooperative allosteric anthranilate synthase from Salmonella typhimurium. Nat. Struct. Biol. 8 2001 243-7 [PubMed: 11224570] http://dx.doi.org/10.1038/84988
	Thoden JB, Huang X, Raushel FM, Holden HM. Carbamoyl-phosphate synthetase. Creation of an escape route for ammonia. J. Biol. Chem. 277 2002 39722-7 [PubMed: 12130656] http://dx.doi.org/10.1074/jbc.M206915200
	Thoden JB, Huang X, Kim J, Raushel FM, Holden HM. Long-range allosteric transitions in carbamoyl phosphate synthetase. Protein Sci. 13 2004 2398-405 [PubMed: 15322282] http://dx.doi.org/10.1110/ps.04822704
	Spraggon G, Kim C, Nguyen-Huu X, Yee MC, Yanofsky C, Mills SE. The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan. Proc. Natl. Acad. Sci. U.S.A. 98 2001 6021-6 [PubMed: 11371633] http://dx.doi.org/10.1073/pnas.111150298
	Miles BW, Thoden JB, Holden HM, Raushel FM. Inactivation of the amidotransferase activity of carbamoyl phosphate synthetase by the antibiotic acivicin. J. Biol. Chem. 277 2002 4368-73 [PubMed: 11729189] http://dx.doi.org/10.1074/jbc.M108582200
	Tran PV, Bannor TA, Doktor SZ, Nichols BP. Chromosomal organization and expression of Escherichia coli pabA. J. Bacteriol. 172 1990 397-410 [PubMed: 2403545] http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=2403545&action=stream&blobtype=pdf

InterPro 23.1