Summary: Galactose-1-phosphate uridyl transferase, C-terminal domain
This is the Wikipedia entry entitled "Galactose-1-phosphate uridylyltransferase". More...
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Galactose-1-phosphate uridyl transferase, C-terminal domain Provide feedback
SCOP reports fold duplication with N-terminal domain. Both involved in Zn and Fe binding.
Wedekind JE, Frey PA, Rayment I; , Biochemistry 1995;34:11049-11061.: Three-dimensional structure of galactose-1-phosphate uridylyltransferase from Escherichia coli at 1.8 A resolution. PUBMED:7669762 EPMC:7669762
Internal database links
|SCOOP:||KNOX2 CwfJ_C_1 DcpS_C DUF4921|
|Similarity to PfamA using HHSearch:||DcpS_C|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005850
Galactose-1-phosphate uridyl transferase catalyses the conversion of UDP-glucose and alpha-D-galactose 1-phosphate to alpha-D-glucose 1-phosphate and UDP-galactose during galactose metabolism. The enzyme is present in prokaryotes and eukaryotes. Defects in GalT in humans is the cause of galactosemia, an inherited disorder of galactose metabolism that leads to jaundice, cataracts and mental retardation.
This domain describes the C-terminal of Galactose-1-phosphate uridyl transferase. SCOP reports fold duplication of the C-terminal with the N-terminal domain. Both are involved in Zn and Fe binding
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||UDP-glucose:hexose-1-phosphate uridylyltransferase activity (GO:0008108)|
|Biological process||galactose metabolic process (GO:0006012)|
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The HIT superfamily are a superfamily of nucleotide hydrolases and transferases, which act on the alpha-phosphate of ribonucleotides .
The clan contains the following 8 members:CDH CwfJ_C_1 DcpS_C DUF4921 DUF4931 GalP_UDP_tr_C GalP_UDP_transf HIT
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Curation and family details
|Author:||Finn RD, Bateman A, Griffiths-Jones SR|
|Number in seed:||8|
|Number in full:||9204|
|Average length of the domain:||171.60 aa|
|Average identity of full alignment:||36 %|
|Average coverage of the sequence by the domain:||48.28 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||13|
|Download:||download the raw HMM for this family|
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 GalP_UDP_tr_C domain has been found. There are 12 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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