Summary: UTP--glucose-1-phosphate uridylyltransferase
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UTP--glucose-1-phosphate uridylyltransferase Provide feedback
This family consists of UTP--glucose-1-phosphate uridylyltransferases, EC:22.214.171.124. 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 . UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type . In Dictyostelium (slime mold) mutants in this enzyme abort the development cycle . Also within the family is UDP-N-acetylglucosamine Q16222 or AGX1  and two hypothetical proteins from Borrelia burgdorferi the lyme disease spirochaete O51893 and O51036.
Duggleby RG, Chao YC, Huang JG, Peng HL, Chang HY; , Eur J Biochem 1996;235:173-179.: Sequence differences between human muscle and liver cDNAs for UDPglucose pyrophosphorylase and kinetic properties of the recombinant enzymes expressed in Escherichia coli. PUBMED:8631325 EPMC:8631325
Mio T, Yabe T, Arisawa M, Yamada-Okabe H; , J Biol Chem 1998;273:14392-14397.: The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism. PUBMED:9603950 EPMC:9603950
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002618This family consists of UTP--glucose-1-phosphate uridylyltransferases (EC). 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 [PUBMED:8631325]. UDP-glucose is an important intermediate in mammalian carbohydrate interconversion involved in various metabolic roles depending on tissue type [PUBMED:8631325]. In Dictyostelium discoideum (Slime mold), mutants in this enzyme abort the development cycle [PUBMED:3035502]. Also within this family is UDP-N-acetylglucosamine pyrophosphorylase (SWISSPROT) [PUBMED:9603950] and two hypothetical proteins from Borrelia burgdorferi, the Lyme disease spirochaete (SWISSPROT and SWISSPROT).
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||nucleotidyltransferase activity (GO:0016779)|
|Biological process||metabolic process (GO:0008152)|
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This is the GT-A clan that contains diverse glycosyltransferases that possess a Rossmann like fold .
The clan contains the following 44 members:Anp1 Caps_synth Cellulose_synt CgtA CHGN Chitin_synth_1 Chitin_synth_2 CofC CTP_transf_3 DUF2064 DUF273 DUF604 Fringe Galactosyl_T GlcNAc Gly_transf_sug Glyco_tranf_2_2 Glyco_tranf_2_3 Glyco_tranf_2_4 Glyco_tranf_2_5 Glyco_trans_2_3 Glyco_transf_21 Glyco_transf_25 Glyco_transf_34 Glyco_transf_43 Glyco_transf_49 Glyco_transf_6 Glyco_transf_64 Glyco_transf_7C Glyco_transf_7N Glyco_transf_8 Glyco_transf_92 Glycos_transf_2 GNT-I IspD Mannosyl_trans3 MGAT2 NTP_transf_3 NTP_transferase Nucleotid_trans Pox_P35 Rhamno_transf TcdA_TcdB UDPGP
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Curation and family details
|Seed source:||Pfam-B_1634 (release 4.1)|
|Author:||Bashton M, Bateman A|
|Number in seed:||8|
|Number in full:||1651|
|Average length of the domain:||349.50 aa|
|Average identity of full alignment:||26 %|
|Average coverage of the sequence by the domain:||75.79 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the UDPGP domain has been found. There are 45 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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