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: IPR011079 Alanine racemase, C-terminal

Protein matches Help

UniProtKB

Matches:

2127 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

IPR011079 Ala_racemase_C

Secondary

IPR000821

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00842	Ala_racemase_C	2127
Signatures in BioMart

InterPro Relationships Help

Parent

IPR009006 Alanine racemase/group IV decarboxylase, C-terminal

Found in

IPR000821 Alanine racemase
IPR011248 Serine/alanine racemase

GO Term annotation Help

Process

GO:0006522 alanine metabolic process

Function

GO:0008784 alanine racemase activity

InterPro annotation

Entry Details in BioMart

Abstract

Alanine racemase (EC:5.1.1.1) plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins contains this domain are found in both prokaryotic and eukaryotic proteins [1,2]. The molecular structure of alanine racemase from Bacillus stearothermophilus (Geobacillus stearothermophilus) was determined by X-ray crystallography to a resolution of 1.9 A [3]. The alanine racemase monomer is composed of two domains, an eight-stranded alpha/beta barrel at the N terminus, and a C-terminal domain essentially composed of beta-strand. The pyridoxal 5'-phosphate (PLP) cofactor lies in and above the mouth of the alpha/beta barrel and is covalently linked via an aldimine linkage to a lysine residue, which is at the C terminus of the first beta-strand of the alpha/beta barrel.

Structural links Help

PDB - click here

SCOP: b.49.2.2

CATH: 2.40.37.10

Database links Help

Enzyme: EC:5.1.1.1

PANDIT: PF00842

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR011079

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O59828 Alanine racemase, catabolic

P0A4X2 Alanine racemase

P54918 Alanine racemase

Q7V9Z2 Alanine racemase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001608	Alanine racemase, N-terminal
IPR000821	Alanine racemase
IPR009006	Alanine racemase/group IV decarboxylase, C-terminal
IPR020622	Alanine racemase, pyridoxal-phosphate attachment site
IPR011079	Alanine racemase, C-terminal
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain

Publications Open in usermanual
1.	Whitchurch CB, Hobbs M, Livingston SP, Krishnapillai V, Mattick JS. Characterisation of a Pseudomonas aeruginosa twitching motility gene and evidence for a specialised protein export system widespread in eubacteria. Gene 101 33-44 1991 [PubMed: 1676385] http://dx.doi.org/10.1016/0378-1119(91)90221-V
2.	De Wergifosse P, Jacques B, Jonniaux JL, Purnelle B, Skala J, Goffeau A. The sequence of a 22.4 kb DNA fragment from the left arm of yeast chromosome II reveals homologues to bacterial proline synthetase and murine alpha-adaptin, as well as a new permease and a DNA-binding protein. Yeast 10 1489-96 1994 [PubMed: 7871888] http://dx.doi.org/10.1002/yea.320101113
3.	Shaw JP, Petsko GA, Ringe D. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9-A resolution. Biochemistry 36 1329-42 1997 [PubMed: 9063881] http://dx.doi.org/10.1021/bi961856c

Additional Reading Open in usermanual
	Noda M, Kawahara Y, Ichikawa A, Matoba Y, Matsuo H, Lee DG, Kumagai T, Sugiyama M. Self-protection mechanism in D-cycloserine-producing Streptomyces lavendulae. Gene cloning, characterization, and kinetics of its alanine racemase and D-alanyl-D-alanine ligase, which are target enzymes of D-cycloserine. J. Biol. Chem. 279 2004 46143-52 [PubMed: 15302885] http://dx.doi.org/10.1074/jbc.M404603200
	Noda M, Matoba Y, Kumagai T, Sugiyama M. Structural evidence that alanine racemase from a D-cycloserine-producing microorganism exhibits resistance to its own product. J. Biol. Chem. 279 2004 46153-61 [PubMed: 15302886] http://dx.doi.org/10.1074/jbc.M404605200
	Fenn TD, Holyoak T, Stamper GF, Ringe D. Effect of a Y265F mutant on the transamination-based cycloserine inactivation of alanine racemase. Biochemistry 44 2005 5317-27 [PubMed: 15807525] http://dx.doi.org/10.1021/bi047842l
	Fenn TD, Stamper GF, Morollo AA, Ringe D. A side reaction of alanine racemase: transamination of cycloserine. Biochemistry 42 2003 5775-83 [PubMed: 12741835] http://dx.doi.org/10.1021/bi027022d
	LeMagueres P, Im H, Ebalunode J, Strych U, Benedik MJ, Briggs JM, Kohn H, Krause KL. The 1.9 A crystal structure of alanine racemase from Mycobacterium tuberculosis contains a conserved entryway into the active site. Biochemistry 44 2005 1471-81 [PubMed: 15683232] http://dx.doi.org/10.1021/bi0486583

InterPro 23.1