Summary: BPG-independent PGAM N-terminus (iPGM_N)
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BPG-independent PGAM N-terminus (iPGM_N) Provide feedback
This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein ( EC:220.127.116.11). The family is found in conjunction with PF01676 (located in the C-terminal region of the protein).
Jedrzejas MJ, Chander M, Setlow P, Krishnasamy G; , J Biol Chem 2000;275:23146-23153.: Mechanism of catalysis of the cofactor-independent phosphoglycerate mutase from Bacillus stearothermophilus. Crystal structure of the complex with 2-phosphoglycerate. PUBMED:10764795 EPMC:10764795
Internal database links
|SCOOP:||Metalloenzyme Phosphodiest Sulfatase|
|Similarity to PfamA using HHSearch:||Metalloenzyme|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR011258
This family represents the N-terminal region of the 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (or phosphoglyceromutase or BPG-independent PGAM) protein (EC). The family is found in conjunction with Metalloenzyme (located in the C-terminal region of the protein).
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||phosphoglycerate mutase activity (GO:0004619)|
|manganese ion binding (GO:0030145)|
|Biological process||glucose catabolic process (GO:0006007)|
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Curation and family details
|Seed source:||Pfam-B_1338 (release 10.0)|
|Number in seed:||708|
|Number in full:||3247|
|Average length of the domain:||210.20 aa|
|Average identity of full alignment:||39 %|
|Average coverage of the sequence by the domain:||41.60 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 26740544 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||12|
|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 iPGM_N domain has been found. There are 13 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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