Summary: IMP dehydrogenase / GMP reductase domain
This is the Wikipedia entry entitled "IMPDH/GMPR family". More...
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IMPDH/GMPR family Edit Wikipedia article
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|IMP dehydrogenase / GMP reductase domain|
binary complex of human type-i inosine monophosphate dehydrogenase with 6-cl-imp
- Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD et al. (1997). "Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex.". Biochemistry 36 (35): 10666–74. doi:10.1021/bi9708850. PMID 9271497.
- Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E et al. (1999). "Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase.". Biochemistry 38 (15): 4691–700. doi:10.1021/bi982858v. PMID 10200156.
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IMP dehydrogenase / GMP reductase domain Provide feedback
This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains PF00571 are inserted in the TIM barrel . This family is a member of the common phosphate binding site TIM barrel family.
Whitby FG, Luecke H, Kuhn P, Somoza JR, Huete-Perez JA, Phillips JD, Hill CP, Fletterick RJ, Wang CC; , Biochemistry 1997;36:10666-10674.: Crystal structure of Tritrichomonas foetus inosine-5'-monophosphate dehydrogenase and the enzyme-product complex. PUBMED:9271497 EPMC:9271497
Zhang R, Evans G, Rotella FJ, Westbrook EM, Beno D, Huberman E, Joachimiak A, Collart FR; , Biochemistry 1999;38:4691-4700.: Characteristics and crystal structure of bacterial inosine-5'-monophosphate dehydrogenase. PUBMED:10200156 EPMC:10200156
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001093Synonym(s): Inosine-5'-monophosphate dehydrogenase, Inosinic acid dehydrogenase; Synonym(s): Guanosine 5'-monophosphate oxidoreductase
This entry contains two related enzymes: IMP dehydrogenase and GMP reductase. These enzymes adopt a TIM barrel structure.
IMP dehydrogenase (EC) (IMPDH) catalyses the rate-limiting reaction of de novo GTP biosynthesis, the NAD-dependent reduction of IMP into XMP [PUBMED:2902093].
GMP reductase (EC) catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [PUBMED:2904262].
|Molecular function||catalytic activity (GO:0003824)|
|Biological process||oxidation-reduction process (GO:0055114)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
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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
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
|Author:||Finn RD, Bateman A|
|Number in seed:||84|
|Number in full:||7826|
|Average length of the domain:||406.30 aa|
|Average identity of full alignment:||38 %|
|Average coverage of the sequence by the domain:||94.26 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null --hand HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||20|
|Download:||download the raw HMM for this family|
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The tree shows the occurrence of this domain across different species. More...
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There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 IMPDH domain has been found. There are 86 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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