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106  structures 8841  species 0  interactions 27095  sequences 124  architectures

Family: PGM_PMM_II (PF02879)

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

  1. 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

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.

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

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Representative proteomes UniProt

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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...


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.

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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 View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Bateman A , Finn RD , Griffiths-Jones SR
Number in seed: 57
Number in full: 27095
Average length of the domain: 104.2 aa
Average identity of full alignment: 26 %
Average coverage of the sequence by the domain: 20.02 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 29.3 29.3
Trusted cut-off 29.3 29.3
Noise cut-off 29.2 29.2
Model length: 103
Family (HMM) version: 19
Download: download the raw HMM for this family

Species distribution

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Archea Archea Eukaryota Eukaryota
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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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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 PGM_PMM_II domain has been found. There are 106 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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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
A0A044R287 View 3D Structure Click here
A0A077YY22 View 3D Structure Click here
A0A077Z5X3 View 3D Structure Click here
A0A077Z9C5 View 3D Structure Click here
A0A077ZJ80 View 3D Structure Click here
A0A077ZM17 View 3D Structure Click here
A0A0A2V6U8 View 3D Structure Click here
A0A0D2GZA8 View 3D Structure Click here
A0A0H3GPZ1 View 3D Structure Click here
A0A0H3GW58 View 3D Structure Click here
A0A0J9YAB6 View 3D Structure Click here
A0A0K0DZU4 View 3D Structure Click here
A0A0K0ES09 View 3D Structure Click here
A0A0R0ELF0 View 3D Structure Click here
A0A158Q2N4 View 3D Structure Click here
A0A158Q5W4 View 3D Structure Click here
A0A175WD44 View 3D Structure Click here
A0A1C1CEG0 View 3D Structure Click here
A0A1D6GJ73 View 3D Structure Click here
A0A1D6HYS5 View 3D Structure Click here
A0A1D6I1B6 View 3D Structure Click here
A0A1D6L1Y9 View 3D Structure Click here
A0A1D6LQ82 View 3D Structure Click here
A0A1D6LQ83 View 3D Structure Click here
A0A1D6NJK9 View 3D Structure Click here
A0A1D8PSA9 View 3D Structure Click here
A0A1P8BGI7 View 3D Structure Click here
A0A2K6WEB6 View 3D Structure Click here
A0A3P7FFD1 View 3D Structure Click here
A0A3Q0KIP8 View 3D Structure Click here
A0A5K4FE41 View 3D Structure Click here
A0A5S6PAF8 View 3D Structure Click here
A0JZ25 View 3D Structure Click here
A0KNE8 View 3D Structure Click here
A0L4J3 View 3D Structure Click here
A0LMD8 View 3D Structure Click here
A0LRQ7 View 3D Structure Click here
A0PXZ6 View 3D Structure Click here
A0QSQ1 View 3D Structure Click here
A1A2Z2 View 3D Structure Click here