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InterPro: IPR020578 Aminotransferase class-V pyridoxal-phosphate binding site

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5095 proteins

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

IPR020578 Aminotrans_V_PyrdxlP_BS

Type

Binding_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00595	AA_TRANSFER_CLASS_5	5095
Signatures in BioMart

InterPro Relationships Help

Found in

IPR000192 Aminotransferase, class V/Cysteine desulfurase
IPR010240 Cysteine desulfurase
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR015424 Pyridoxal phosphate-dependent transferase, major domain
IPR016454 Cysteine desulfurase, NifS

InterPro annotation

Entry Details in BioMart

Abstract

Aminotransferases share certain mechanistic features with other pyridoxal- phosphate dependent enzymes, such as the covalent binding of the pyridoxal- phosphate group to a lysine residue. On the basis of sequence similarity, these various enzymes can be grouped [1] into subfamilies. This entry represents the class V aminotransferases and the related, though functionally distinct, cysteine desulfurases.

This signature represents a conserved region surrounding the lysine residue that binds the pyridoxal-phosphate [1].

Structural links Help

PDB - click here

SCOP: c.67.1.3 , c.67.1.4

CATH: 3.40.640.10

Database links Help

Enzyme: EC:2

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR020578

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35423 Serine--pyruvate aminotransferase, mitochondrial

P21549 Serine--pyruvate aminotransferase

P25374 Cysteine desulfurase, mitochondrial

P91856 Probable phosphoserine aminotransferase

Q9VAN0 Probable phosphoserine aminotransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010240	Cysteine desulfurase
IPR015424	Pyridoxal phosphate-dependent transferase, major domain
IPR015422	Pyridoxal phosphate-dependent transferase, major region, subdomain 2
IPR020578	Aminotransferase class-V pyridoxal-phosphate binding site
IPR015421	Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR003248	Phosphoserine aminotransferase
IPR000192	Aminotransferase, class V/Cysteine desulfurase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Ouzounis C, Sander C. Homology of the NifS family of proteins to a new class of pyridoxal phosphate-dependent enzymes. FEBS Lett. 322 159-64 1993 [PubMed: 8482384] http://dx.doi.org/10.1016/0014-5793(93)81559-I

Additional Reading Open in usermanual
	Han Q, Robinson H, Gao YG, Vogelaar N, Wilson SR, Rizzi M, Li J. Crystal structures of Aedes aegypti alanine glyoxylate aminotransferase. J. Biol. Chem. 281 2006 37175-82 [PubMed: 16990263] http://dx.doi.org/10.1074/jbc.M607032200
	Kapetaniou EG, Thanassoulas A, Dubnovitsky AP, Nounesis G, Papageorgiou AC. Effect of pH on the structure and stability of Bacillus circulans ssp. alkalophilus phosphoserine aminotransferase: thermodynamic and crystallographic studies. Proteins 63 2006 742-53 [PubMed: 16532449] http://dx.doi.org/10.1002/prot.20935
	Rossi F, Garavaglia S, Giovenzana GB, Arca B, Li J, Rizzi M. Crystal structure of the Anopheles gambiae 3-hydroxykynurenine transaminase. Proc. Natl. Acad. Sci. U.S.A. 103 2006 5711-6 [PubMed: 16585514] http://dx.doi.org/10.1073/pnas.0510233103
	Dubnovitsky AP, Ravelli RB, Popov AN, Papageorgiou AC. Strain relief at the active site of phosphoserine aminotransferase induced by radiation damage. Protein Sci. 14 2005 1498-507 [PubMed: 15883191] http://dx.doi.org/10.1110/ps.051397905
	Dubnovitsky AP, Kapetaniou EG, Papageorgiou AC. Enzyme adaptation to alkaline pH: atomic resolution (1.08 A) structure of phosphoserine aminotransferase from Bacillus alcalophilus. Protein Sci. 14 2005 97-110 [PubMed: 15608117] http://dx.doi.org/10.1110/ps.041029805

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