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InterPro: IPR001608 Alanine racemase, N-terminal

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UniProtKB

Matches:

4794 proteins

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

Accession

IPR001608 Ala_racemase_N

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01168	Ala_racemase_N	4794
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000821 Alanine racemase
IPR011078 Predicted pyridoxal phosphate-dependent enzyme, YBL036C type
IPR011248 Serine/alanine racemase

Contains

IPR020622 Alanine racemase, pyridoxal-phosphate attachment site

InterPro annotation

Entry Details in BioMart

Abstract

Alanine racemase plays a role in providing the D-alanine required for cell wall biosynthesis by isomerising L-alanine to D-alanine. Proteins containing this domain are found in both prokaryotes and eukaryotes [1,2]. The molecular structure of alanine racemase from Bacillus 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-strands. 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.

This domain is also found in the PROSC (proline synthetase co-transcribed bacterial homolog) family of proteins, which are not known to have alanine racemase activity.

Structural links Help

PDB - click here

SCOP: b.49.2.2 , c.1.6.1 , c.1.6.2

CATH: 2.40.37.10 , 3.20.20.10

Database links Help

Enzyme: EC:5.1.1.1

PANDIT: PF01168

Blocks: IPB001608

Pfam Clan: CL0152.8

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001608

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O94903 Proline synthetase co-transcribed bacterial homolog protein

P38197 UPF0001 protein YBL036C

P52056 UPF0001 protein slr0556

P52057 Proline synthetase co-transcribed bacterial homolog protein

Q9Z2Y8 Proline synthetase co-transcribed bacterial homolog protein

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR001608	Alanine racemase, N-terminal
IPR011078	Predicted pyridoxal phosphate-dependent enzyme, YBL036C type
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP 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
	Eswaramoorthy S, Gerchman S, Graziano V, Kycia H, Studier FW, Swaminathan S. Structure of a yeast hypothetical protein selected by a structural genomics approach. Acta Crystallogr. D Biol. Crystallogr. 59 2003 127-35 [PubMed: 12499548]
	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