Summary: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
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2,3-bisphosphoglycerate-independent phosphoglycerate mutase Provide feedback
Members of this family are found in various bacterial 2,3-bisphosphoglycerate-independent phosphoglycerate mutase enzymes, which catalyse the interconversion of 2-phosphoglycerate and 3-phosphoglycerate in the reaction: [2-phospho-D-glycerate + 2,3-diphosphoglycerate = 3-phospho-D-glycerate + 2,3-diphosphoglycerate].
Internal database links
|Similarity to PfamA using HHSearch:||Metalloenzyme|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004456
This family represents 2,3-bisphosphoglycerate-independent phosphoglycerate mutase (iPGAM), it is a metalloenzyme found particularly in archaea and some eubacteria. It is responsble for the interconversion of 2-phosphoglycerate and 3-phosphoglycerate [PUBMED:17576516]. It is distantly related to the iPGAM (INTERPRO) characteristic of plants and many eubacteria. The common active site and metal-binding residues of the phosphatase domain are easily identified, but the putative phosphotransferase domain is highly diverged. These proteins are unrelated to the cofactor-dependent PGAM (). Activity has been demonstrated for proteins from Methanocaldococcus jannaschii (Methanococcus jannaschii) [PUBMED:12062435, PUBMED:12076796], Pyrococcus furiosus [PUBMED:12076796], and Sulfolobus solfataricus [PUBMED:12644480]. These proteins were initially misidentified as phosphonopyruvate decarboxylase.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Molecular function||metal ion binding (GO:0046872)|
|catalytic activity (GO:0003824)|
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This large superfamily of TIM barrel enzymes all contain a common phosphate binding site. The phosphate is found in a variety of cofactors and ligands such as FMN [1,2].
The clan contains the following 57 members:Ala_racemase_N ALAD Aldolase AP_endonuc_2 BtpA CdhD CutC DAHP_synth_1 DAHP_synth_2 DeoC DHDPS DHO_dh DHquinase_I DUF1341 DUF2090 DUF556 DUF561 DUF692 DUF993 Dus F_bP_aldolase FMN_dh G3P_antiterm Glu_syn_central Glu_synthase His_biosynth HMGL-like IGPS IMPDH iPGM_N MtrH NanE NAPRTase NeuB NMO OMPdecase Orn_Arg_deC_N Oxidored_FMN PcrB PdxJ PhosphMutase PRAI Pterin_bind QRPTase_C Racemase_4 RhaA Ribul_P_3_epim SOR_SNZ Tagatose_6_P_K ThiG TIM TIM-br_sig_trns TMP-TENI Transaldolase Trp_syntA UvdE UxuA
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Curation and family details
|Seed source:||COGs (COG4255)|
|Author:||COGs, Finn RD, Sammut SJ|
|Number in seed:||92|
|Number in full:||556|
|Average length of the domain:||172.10 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||41.38 %|
|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:||4|
|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 PhosphMutase domain has been found. There are 6 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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