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InterPro: IPR005861 Histidinol-phosphate aminotransferase

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UniProtKB

Matches:

1817 proteins

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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

IPR005861 HisP_aminotrans

Type

Family

Signatures Help

Database	ID	Name	Proteins
TIGRFAMs	TIGR01141	hisC	1817
Signatures in BioMart

InterPro Relationships Help

Contains

IPR001917 Aminotransferase, class-II, pyridoxal-phosphate binding site
IPR004839 Aminotransferase, class I/II
IPR015421 Pyridoxal phosphate-dependent transferase, major region, subdomain 1

GO Term annotation Help

Process

GO:0000105 histidine biosynthetic process

Function

GO:0004400 histidinol-phosphate transaminase activity

InterPro annotation

Entry Details in BioMart

Abstract

The biosynthesis of histidine is a central metabolic process in organisms ranging from bacteria to yeast and plants. The seventh step in the synthesis of histidine within eubacteria is carried out by a pyridoxal-5'-phosphate (PLP)-dependent l-histidinol phosphate aminotransferase (HisC, EC:2.6.1.9). HisC is a dimeric enzyme with a mass of approximately 80 kDa. Like most PLP-dependent enzymes, each HisC monomer consists of two domains, a larger PLP-binding domain having an alpha/beta/alpha topology, and a smaller domain. An N-terminal arm contributes to the dimerization of the two monomers [1].

Structural links Help

PDB - click here

SCOP: c.67.1.1

CATH: 3.40.640.10 , 3.90.1150.10

Database links Help

Enzyme: EC:2.6.1.9

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR005861

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

A2SSJ1 Histidinol-phosphate aminotransferase

P06986 Histidinol-phosphate aminotransferase

P07172 Histidinol-phosphate aminotransferase

P73807 Histidinol-phosphate aminotransferase

Q949X3 Histidinol-phosphate aminotransferase, chloroplastic

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR004839	Aminotransferase, class I/II
IPR015424	Pyridoxal phosphate-dependent transferase, major domain
IPR015422	Pyridoxal phosphate-dependent transferase, major region, subdomain 2
IPR005861	Histidinol-phosphate aminotransferase
IPR015421	Pyridoxal phosphate-dependent transferase, major region, subdomain 1
IPR001917	Aminotransferase, class-II, pyridoxal-phosphate binding site
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Sivaraman J, Li Y, Larocque R, Schrag JD, Cygler M, Matte A. Crystal structure of histidinol phosphate aminotransferase (HisC) from Escherichia coli, and its covalent complex with pyridoxal-5'-phosphate and l-histidinol phosphate. J. Mol. Biol. 311 761-76 2001 [PubMed: 11518529] http://dx.doi.org/10.1006/jmbi.2001.4882

Additional Reading Open in usermanual
	Haruyama K, Nakai T, Miyahara I, Hirotsu K, Mizuguchi H, Hayashi H, Kagamiyama H. Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Biochemistry 40 2001 4633-44 [PubMed: 11294630] http://dx.doi.org/10.1021/bi002769u
	Fernandez FJ, Vega MC, Lehmann F, Sandmeier E, Gehring H, Christen P, Wilmanns M. Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase. J. Biol. Chem. 279 2004 21478-88 [PubMed: 15007066] http://dx.doi.org/10.1074/jbc.M400291200

InterPro 23.1