Summary: Eukaryotic phosphomannomutase
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This enzyme EC:18.104.22.168 is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Carchon H, Van Schaftingen E, Matthijs G, Jaeken J; , Biochim Biophys Acta 1999;1455:155-165.: Carbohydrate-deficient glycoprotein syndrome type IA (phosphomannomutase-deficiency). PUBMED:10571009 EPMC:10571009
Internal database links
|Similarity to PfamA using HHSearch:||Hydrolase_3|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR005002This enzyme (EC) is involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||cytoplasm (GO:0005737)|
|Molecular function||phosphomannomutase activity (GO:0004615)|
|Biological process||mannose biosynthetic process (GO:0019307)|
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This example describes an architecture with one
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This clan represents the haloacid dehalogenase (HAD) superfamily that includes a diverse range of enzymes that use an asp carboxylate as a nucleophile .
The clan contains the following 21 members:5_nucleotid Acid_phosphat_B Acid_PPase DUF705 HAD HAD_2 Hydrolase Hydrolase_3 Hydrolase_6 Hydrolase_like Hydrolase_like2 LNS2 NIF NT5C PGP_phosphatase PMM PNK3P Put_Phosphatase S6PP Trehalose_PPase UMPH-1
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Curation and family details
|Seed source:||Pfam-B_3713 (release 6.5)|
|Number in seed:||9|
|Number in full:||691|
|Average length of the domain:||202.50 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||83.41 %|
|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:||8|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. 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 PMM 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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