Summary: Glycosyltransferase family 52
Glycosyltransferase family 52 Provide feedback
This family features glycosyltransferases belonging to glycosyltransferase family 52  which have alpha-2,3- sialyltransferase ( EC:220.127.116.11) and alpha-glucosyltransferase (EC 2.4.1.-) activity. For example, beta-galactoside alpha-2,3- sialyltransferase expressed by Neisseria meningitidis (P72097) is a member of this family and is involved in a step of lipooligosaccharide biosynthesis requiring sialic acid transfer; these lipooligosaccharides are thought to be important in the process of pathogenesis . This family includes several bacterial lipooligosaccharide sialyltransferases similar to the Haemophilus ducreyi LST protein. Haemophilus ducreyi is the cause of the sexually transmitted disease chancroid and produces a lipooligosaccharide (LOS) containing a terminal sialyl N-acetyllactosamine trisaccharide .
Gilbert M, Watson DC, Cunningham AM, Jennings MP, Young NM, Wakarchuk WW; , J Biol Chem 1996;271:28271-28276.: Cloning of the lipooligosaccharide alpha-2,3-sialyltransferase from the bacterial pathogens Neisseria meningitidis and Neisseria gonorrhoeae. PUBMED:8910446 EPMC:8910446
Bozue JA, Tullius MV, Wang J, Gibson BW, Munson RS Jr; , J Biol Chem 1999;274:4106-4114.: Haemophilus ducreyi produces a novel sialyltransferase. Identification of the sialyltransferase gene and construction of mutants deficient in the production of the sialic acid-containing glycoform of the lipooligosaccharide. PUBMED:9933604 EPMC:9933604
Jones PA, Samuels NM, Phillips NJ, Munson RS Jr, Bozue JA, Arseneau JA, Nichols WA, Zaleski A, Gibson BW, Apicella MA; , J Biol Chem 2002;277:14598-14611.: Haemophilus influenzae type b strain A2 has multiple sialyltransferases involved in lipooligosaccharide sialylation. PUBMED:11842084 EPMC:11842084
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR012477
This family features glycosyltransferases belonging to glycosyltransferase family 52 [PUBMED:12691742], which have alpha-2,3- sialyltransferase (EC) and alpha-glucosyltransferase (EC) activity. For example, beta-galactoside alpha-2,3- sialyltransferase expressed by Neisseria meningitidis (SWISSPROT) is a member of this family and is involved in a step of lipooligosaccharide biosynthesis requiring sialic acid transfer; these lipooligosaccharides are thought to be important in the process of pathogenesis [PUBMED:8910446]. This family includes several bacterial lipooligosaccharide sialyltransferases similar to the Haemophilus ducreyi LST protein. Haemophilus ducreyi is the cause of the sexually transmitted disease chancroid and produces a lipooligosaccharide (LOS) containing a terminal sialyl N-acetyllactosamine trisaccharide [PUBMED:9933604].
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This example describes an architecture with one
Gladomain, followed by two consecutive
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We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_2778 (release 14.0)|
|Number in seed:||16|
|Number in full:||318|
|Average length of the domain:||254.60 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||82.76 %|
|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:||6|
|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 Glyco_transf_52 domain has been found. There are 4 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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