Summary: Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II
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Phosphoglucomutase/phosphomannomutase, alpha/beta/alpha domain II Provide feedback
No Pfam abstract.
Literature references
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Dai JB, Liu Y, Ray WJ Jr, Konno M; , J Biol Chem 1992;267:6322-6337.: The crystal structure of muscle phosphoglucomutase refined at 2.7-angstrom resolution. PUBMED:1532581 EPMC:1532581
External database links
PRINTS: | PR00509 |
PROSITE: | PDOC00589 |
SCOP: | 3pmg |
This tab holds annotation information from the InterPro database.
InterPro entry IPR005845
The alpha-D-phosphohexomutase superfamily is composed of four related enzymes, each of which catalyses a phosphoryl transfer on their sugar substrates: phosphoglucomutase (PGM), phosphoglucomutase/phosphomannomutase (PGM/PMM), phosphoglucosamine mutase (PNGM), and phosphoacetylglucosamine mutase (PAGM) [PUBMED:10506283]. PGM (EC) converts D-glucose 1-phosphate into D-glucose 6-phosphate, and participates in both the breakdown and synthesis of glucose [PUBMED:15299905]. PGM/PMM (EC; EC) are primarily bacterial enzymes that use either glucose or mannose as substrate, participating in the biosynthesis of a variety of carbohydrates such as lipopolysaccharides and alginate [PUBMED:16595672, PUBMED:14725765]. Both PNGM (EC) and PAGM (EC) are involved in the biosynthesis of UDP-N-acetylglucosamine [PUBMED:10913078, PUBMED:11004509].
Despite differences in substrate specificity, these enzymes share a similar catalytic mechanism, converting 1-phospho-sugars to 6-phospho-sugars via a biphosphorylated 1,6-phospho-sugar. The active enzyme is phosphorylated at a conserved serine residue and binds one magnesium ion; residues around the active site serine are well conserved among family members. The reaction mechanism involves phosphoryl transfer from the phosphoserine to the substrate to create a biophosphorylated sugar, followed by a phosphoryl transfer from the substrate back to the enzyme [PUBMED:15238632].
The structures of PGM and PGM/PMM have been determined, and were found to be very similar in topology. These enzymes are both composed of four domains and a large central active site cleft, where each domain contains residues essential for catalysis and/or substrate recognition. Domain I contains the catalytic phosphoserine, domain II contains a metal-binding loop to coordinate the magnesium ion, domain III contains the sugar-binding loop that recognises the two different binding orientations of the 1- and 6-phospho-sugars, and domain IV contains a phosphate-binding site required for orienting the incoming phospho-sugar substrate.
This entry represents domain II found in alpha-D-phosphohexomutase enzymes. This domain has a 3-layer alpha/beta/alpha topology.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Biological process | carbohydrate metabolic process (GO:0005975) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
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Seed (59) |
Full (21881) |
Representative proteomes | UniProt (96842) |
NCBI (133869) |
Meta (4472) |
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RP15 (2815) |
RP35 (10289) |
RP55 (21242) |
RP75 (36411) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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Seed (59) |
Full (21881) |
Representative proteomes | UniProt (96842) |
NCBI (133869) |
Meta (4472) |
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RP15 (2815) |
RP35 (10289) |
RP55 (21242) |
RP75 (36411) |
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Raw Stockholm | |||||||||
Gzipped |
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
Seed source: | Prosite |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Bateman A |
Number in seed: | 59 |
Number in full: | 21881 |
Average length of the domain: | 104.00 aa |
Average identity of full alignment: | 26 % |
Average coverage of the sequence by the domain: | 20.07 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 47079205 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 103 | ||||||||||||
Family (HMM) version: | 17 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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Interactions
There are 6 interactions for this family. More...
PGM_PMM_III PGM_PMM_IV PGM_PMM_I PGM_PMM_II PGM_PMM_IV PGM_PMM_IIIStructures
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 PGM_PMM_II domain has been found. There are 100 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 sequence.
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