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InterPro: IPR000192 Aminotransferase, class V/Cysteine desulfurase

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9687 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

IPR000192 Aminotrans_V/Cys_dSase

Type

Family

Signatures Help

Database	ID	Name	Proteins
Pfam	PF00266	Aminotran_5	9687
Signatures in BioMart

InterPro Relationships Help

Children

IPR003248 Phosphoserine aminotransferase
IPR010969 Cysteine desulfurase-related, unknown function
IPR010970 Cysteine desulfurase, SufS
IPR011340 Cysteine desulfurase-related
IPR012703 2-aminoethylphosphonate--pyruvate transaminase
IPR016454 Cysteine desulfurase, NifS
IPR017688 2-aminoethylphosphonate aminotransferase

Contains

IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR015424 Pyridoxal phosphate-dependent transferase, major domain
IPR020578 Aminotransferase class-V pyridoxal-phosphate binding site

GO Term annotation Help

Process

GO:0008152 metabolic process

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.

Structural links Help

PDB - click here

SCOP: c.67.1.3 , c.67.1.4

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

PDBe-motif: PS00595

Enzyme: EC:2

PROSITE doc: PDOC00514

PANDIT: PF00266

Blocks: IPB000192

Pfam Clan: CL0061.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR000192

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35423 Serine--pyruvate aminotransferase, mitochondrial

P21549 Serine--pyruvate aminotransferase

P43567 Alanine--glyoxylate aminotransferase 1

P91856 Probable phosphoserine aminotransferase

Q9VAN0 Probable phosphoserine aminotransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
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
	Meyer P, Liger D, Leulliot N, Quevillon-Cheruel S, Zhou CZ, Borel F, Ferrer JL, Poupon A, Janin J, van Tilbeurgh H. Crystal structure and confirmation of the alanine:glyoxylate aminotransferase activity of the YFL030w yeast protein. Biochimie 87 2005 1041-7 [PubMed: 16226833] http://dx.doi.org/10.1016/j.biochi.2005.09.001
	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, 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

InterPro 23.1