Summary: Glycerol-3-phosphate responsive antiterminator
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Intracellular glycerol is usually converted to glycerol-3-phosphate in an ATP-requiring phosphorylation reaction catalysed by glycerol kinase (GlpK) glycerol-3-phosphate activates the antiterminator GlpP .
Holmberg C, Rutberg B; , Mol Microbiol 1991;5:2891-2900.: Expression of the gene encoding glycerol-3-phosphate dehydrogenase (glpD) in Bacillus subtilis is controlled by antitermination. PUBMED:1809833 EPMC:1809833
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This tab holds annotation information from the InterPro database.
InterPro entry IPR006699
Glycerol enters bacterial cells via facilitated diffusion, an energy-independent transport process catalysed by the glycerol transport facilitator GlpF, an integral membrane protein of the aquaporin family. Intracellular glycerol is usually converted to glycerol-3-P in an ATP-requiring phosphorylation reaction catalysed by glycerol kinase (GlpK). Glycerol-3-P, the inducer of the glpFK operon, is not a substrate for GlpF and hence remains entrapped in the cell where it is metabolized further. In some bacterial species, for example Bacillus firmus, glycerol-3-P activates the antiterminator GlpP [PUBMED:1809833]. In B. subtilis, glpF and glpK are organised in an operon followed by the glycerol-3-P dehydrogenase-encoding glpD gene and preceded by glpP coding for an antiterminator regulating the expression of glpFK, glpD and glpTQ. Their induction requires the inducer glycerol-3-P, which activates the antiterminator GlpP by allowing it to bind to the leader region of glpD and presumably also of glpFK and glpTQ mRNAs.
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|Biological process||regulation of transcription, DNA-dependent (GO:0006355)|
|response to biotic stimulus (GO:0009607)|
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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
|Author:||Waterfield DI, Finn RD|
|Number in seed:||8|
|Number in full:||1079|
|Average length of the domain:||171.60 aa|
|Average identity of full alignment:||41 %|
|Average coverage of the sequence by the domain:||93.62 %|
|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:||7|
|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 G3P_antiterm 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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