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InterPro: IPR004467 Orotate phosphoribosyl transferase

Protein matchesHelp
UniProtKB
Matches:
1734 proteins
AccessionHelp IPR004467 Or_phspho_trans
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Parent IPR000836 Phosphoribosyltransferase
GO Term annotationHelp
Process GO:0006221 pyrimidine nucleotide biosynthetic process
Function GO:0004588 orotate phosphoribosyltransferase activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Orotate phosphoribosyl transferase (OPRTase) is involved in the biosynthesis of pyrimidine nucleotides. Alpha-D-ribosyldiphosphate 5-phosphate (PRPP) and orotate are utilised to form pyrophosphate and orotidine 5 -monophosphate (OMP) in the presence of divalent cations, preferably Mg2+. In a number of eukaryotes, this protein is fused to a domain that catalyses the reaction (EC:4.1.1.23). The combined activity of EC:2.4.2.10 and EC:4.1.1.23 is termed uridine 5 -monophosphate synthase. The conserved Lys (K) residue at position 101 of the seed alignment has been proposed as the active site for the enzyme.

Structural linksHelp
SCOP: c.61.1.1
CATH: 3.40.50.2020
Database linksHelp
Enzyme: EC:2.4.2.10

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR004467 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P11172 Uridine 5'-monophosphate synthase

P13298 Orotate phosphoribosyltransferase 1

P13439 Uridine 5'-monophosphate synthase

Q01637 Uridine 5'-monophosphate synthase

Q42586 Uridine 5'-monophosphate synthase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR013785 Aldolase-type TIM barrel
IPR001754 Orotidine 5'-phosphate decarboxylase, core
IPR004467 Orotate phosphoribosyl transferase
IPR018089 Orotidine 5'-phosphate decarboxylase, active site
IPR011060 Ribulose-phosphate binding barrel
IPR000836 Phosphoribosyltransferase
IPR014732 Orotidine 5'-phosphate decarboxylase, subfamily 1, core
SWISS-MODEL
PDB Chain
ModBase
CATH Domain

PublicationsHelp

Additional ReadingHelp
Scapin G, Grubmeyer C, Sacchettini JC.
Crystal structure of orotate phosphoribosyltransferase.
Biochemistry 33 1994 1287-94 [PubMed: 8312245]
http://dx.doi.org/10.1021/bi00172a001
Gonzalez-Segura L, Witte JF, McClard RW, Hurley TD.
Ternary complex formation and induced asymmetry in orotate phosphoribosyltransferase.
Biochemistry 46 2007 14075-86 [PubMed: 18020427]
http://dx.doi.org/10.1021/bi701023z
Henriksen A, Aghajari N, Jensen KF, Gajhede M.
A flexible loop at the dimer interface is a part of the active site of the adjacent monomer of Escherichia coli orotate phosphoribosyltransferase.
Biochemistry 35 1996 3803-9 [PubMed: 8620002]
http://dx.doi.org/10.1021/bi952226y
Scapin G, Ozturk DH, Grubmeyer C, Sacchettini JC.
The crystal structure of the orotate phosphoribosyltransferase complexed with orotate and alpha-D-5-phosphoribosyl-1-pyrophosphate.
Biochemistry 34 1995 10744-54 [PubMed: 7545004]
http://dx.doi.org/10.1021/bi00034a006
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InterPro 23.1