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InterPro: IPR019779 Galactose-1-phosphate uridyl transferase, class I His-active site

Protein matches Help

UniProtKB

Matches:

480 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

IPR019779 GalP_UDPtransf1_His-AS

Type

Active_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS00117	GAL_P_UDP_TRANSF_I	480
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001937 Galactose-1-phosphate uridyl transferase, class I
IPR005849 Galactose-1-phosphate uridyl transferase, N-terminal
IPR011146 Histidine triad-like motif
IPR011151 Histidine triad motif

GO Term annotation Help

Process

GO:0006012 galactose metabolic process

Function

GO:0008108 UDP-glucose:hexose-1-phosphate uridylyltransferase activity
GO:0008270 zinc ion binding

InterPro annotation

Entry Details in BioMart

Abstract

Galactose-1-phosphate uridyl transferase EC:2.7.7.12 (galT) catalyses the transfer of an uridyldiphosphate group on galactose (or glucose) 1-phosphate. During the reaction, the uridyl moiety links to a histidine residue. In the Escherichia coli enzyme, it has been shown [1] that two histidine residues separated by a single proline residue are essential for enzyme activity. The first H binds zinc and the second H is an active site residue.

On the basis of sequence similarities, two apparently unrelated families seem to exist. Class-I enzymes are found in eukaryotes as well as some bacteria such as E. coli or Streptomyces lividans, while class-II enzymes have been found so far only in bacteria such as Bacillus subtilis or Lactobacillus helveticus [2].

Structural links Help

PDB - click here

SCOP: d.13.1.2

CATH: 3.30.428.10

Database links Help

Enzyme: EC:2.7.7.12

CluSTr: ALLvsALL:41196:49.4

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR019779

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P07902 Galactose-1-phosphate uridylyltransferase

P08431 Galactose-1-phosphate uridylyltransferase

Q03249 Galactose-1-phosphate uridylyltransferase

Q27536 Probable galactose-1-phosphate uridylyltransferase

Q9VMA2 Probable galactose-1-phosphate uridylyltransferase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR019779	Galactose-1-phosphate uridyl transferase, class I His-active site
IPR001937	Galactose-1-phosphate uridyl transferase, class I
IPR005850	Galactose-1-phosphate uridyl transferase, C-terminal
IPR011146	Histidine triad-like motif
IPR011151	Histidine triad motif
IPR005849	Galactose-1-phosphate uridyl transferase, N-terminal
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Reichardt JK, Berg P. Conservation of short patches of amino acid sequence amongst proteins with a common function but evolutionarily distinct origins: implications for cloning genes and for structure-function analysis. Nucleic Acids Res. 16 9017-26 1988 [PubMed: 2845364] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=2845364&action=stream&blobtype=pdf
2.	Mollet B, Pilloud N. Galactose utilization in Lactobacillus helveticus: isolation and characterization of the galactokinase (galK) and galactose-1-phosphate uridyl transferase (galT) genes. J. Bacteriol. 173 4464-73 1991 [PubMed: 2066342] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=2066342

Additional Reading Open in usermanual
	Wedekind JE, Frey PA, Rayment I. Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. Biochemistry 34 1995 11049-61 [PubMed: 7669762] http://dx.doi.org/10.1021/bi00035a010
	Thoden JB, Ruzicka FJ, Frey PA, Rayment I, Holden HM. Structural analysis of the H166G site-directed mutant of galactose-1-phosphate uridylyltransferase complexed with either UDP-glucose or UDP-galactose: detailed description of the nucleotide sugar binding site. Biochemistry 36 1997 1212-22 [PubMed: 9063869] http://dx.doi.org/10.1021/bi9626517
	Wedekind JE, Frey PA, Rayment I. The structure of nucleotidylated histidine-166 of galactose-1-phosphate uridylyltransferase provides insight into phosphoryl group transfer. Biochemistry 35 1996 11560-9 [PubMed: 8794735] http://dx.doi.org/10.1021/bi9612677

InterPro 23.1