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InterPro: IPR002618 UTP--glucose-1-phosphate uridylyltransferase

Protein matchesHelp
UniProtKB
Matches:
702 proteins
AccessionHelp IPR002618 UDPGP_trans
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Children IPR016267 UTP--glucose-1-phosphate uridylyltransferase, subgroup
GO Term annotationHelp
Process GO:0008152 metabolic process
Function GO:0016779 nucleotidyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

This family consists of UTP--glucose-1-phosphate uridylyltransferases (EC:2.7.7.9). Also known as UDP-glucose pyrophosphorylase (UDPGP) and Glucose-1-phosphate uridylyltransferase. UTP--glucose-1-phosphate uridylyltransferase catalyses the interconversion of MgUTP + glucose-1-phosphate and UDP-glucose + MgPPi [1]. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type [1]. In Dictyostelium discoideum (Slime mold), mutants in this enzyme abort the development cycle [2]. Also within this family is UDP-N-acetylglucosamine pyrophosphorylase (Q16222) [3] and two hypothetical proteins from Borrelia burgdorferi, the Lyme disease spirochaete (O51893 and O51036).

Structural linksHelp
SCOP: b.81.1.4 , c.68.1.5
CATH: 3.90.550.10
Database linksHelp
Enzyme: EC:2.7.7
PANDIT: PF01704
Blocks: IPB002618
Pfam Clan: CL0110.8

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR002618 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P32861 UTP--glucose-1-phosphate uridylyltransferase

Q16222 UDP-N-acetylhexosamine pyrophosphorylase

Q18493 Probable UDP-N-acetylglucosamine pyrophosphorylase

Q91YN5 UDP-N-acetylhexosamine pyrophosphorylase

Q9M9P3 Probable UTP--glucose-1-phosphate uridylyltransferase 2

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR002618 UTP--glucose-1-phosphate uridylyltransferase
IPR016267 UTP--glucose-1-phosphate uridylyltransferase, subgroup
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Duggleby RG, Chao YC, Huang JG, Peng HL, Chang HY.
Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli.
Eur. J. Biochem. 235 173-9 1996 [PubMed: 8631325]
http://dx.doi.org/10.1111/j.1432-1033.1996.00173.x
2. Ragheb JA, Dottin RP.
Structure and sequence of a UDP glucose pyrophosphorylase gene of Dictyostelium discoideum.
Nucleic Acids Res. 15 3891-906 1987 [PubMed: 3035502]
http://dx.doi.org/10.1093/nar/15.9.3891
3. Mio T, Yabe T, Arisawa M, Yamada-Okabe H.
The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism.
J. Biol. Chem. 273 14392-7 1998 [PubMed: 9603950]
http://dx.doi.org/10.1074/jbc.273.23.14392

Additional ReadingHelp
Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN Jr.
Ensemble refinement of protein crystal structures: validation and application.
Structure 15 2007 1040-52 [PubMed: 17850744]
http://dx.doi.org/10.1016/j.str.2007.06.019
Peneff C, Ferrari P, Charrier V, Taburet Y, Monnier C, Zamboni V, Winter J, Harnois M, Fassy F, Bourne Y.
Crystal structures of two human pyrophosphorylase isoforms in complexes with UDPGlc(Gal)NAc: role of the alternatively spliced insert in the enzyme oligomeric assembly and active site architecture.
EMBO J. 20 2001 6191-202 [PubMed: 11707391]
http://dx.doi.org/10.1093/emboj/20.22.6191
Maruyama D, Nishitani Y, Nonaka T, Kita A, Fukami TA, Mio T, Yamada-Okabe H, Yamada-Okabe T, Miki K.
Crystal structure of uridine-diphospho-N-acetylglucosamine pyrophosphorylase from Candida albicans and catalytic reaction mechanism.
J. Biol. Chem. 282 2007 17221-30 [PubMed: 17392279]
http://dx.doi.org/10.1074/jbc.M611873200
McCoy JG, Bitto E, Bingman CA, Wesenberg GE, Bannen RM, Kondrashov DA, Phillips GN Jr.
Structure and dynamics of UDP-glucose pyrophosphorylase from Arabidopsis thaliana with bound UDP-glucose and UTP.
J. Mol. Biol. 366 2007 830-41 [PubMed: 17178129]
http://dx.doi.org/10.1016/j.jmb.2006.11.059
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InterPro 23.1