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86  structures 4695  species 3  interactions 7826  sequences 15  architectures

Family: IMPDH (PF00478)

Summary: IMP dehydrogenase / GMP reductase domain

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This is the Wikipedia entry entitled "IMPDH/GMPR family". More...

IMPDH/GMPR family Edit Wikipedia article

IMP dehydrogenase / GMP reductase domain
PDB 1jcn EBI.jpg
binary complex of human type-i inosine monophosphate dehydrogenase with 6-cl-imp
Identifiers
Symbol IMPDH
Pfam PF00478
Pfam clan CL0036
InterPro IPR001093
PROSITE PDOC00391
SCOP 1ak5
SUPERFAMILY 1ak5

In molecular biology, the IMPDH/GMPR family of enzymes includes IMP dehydrogenase and GMP reductase. These enzymes are involved in purine metabolism. These enzymes adopt a TIM barrel structure.[1][2]

References[edit]

  1. ^ 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. 
  2. ^ 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. 

This article incorporates text from the public domain Pfam and InterPro IPR001093


This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

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 [2]. This family is a member of the common phosphate binding site TIM barrel family.

Literature references

  1. 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

  2. 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 IPR001093

Synonym(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]. Inosine 5-phosphate + NAD+ + H2O = xanthosine 5-phosphate + NADH IMP dehydrogenase is associated with cell proliferation and is a possible target for cancer chemotherapy. Mammalian and bacterial IMPDHs are tetramers of identical chains. There are two IMP dehydrogenase isozymes in humans [PUBMED:1969416]. IMP dehydrogenase nearly always contains a long insertion that has two CBS domains within it.

GMP reductase (EC) catalyses the irreversible and NADPH-dependent reductive deamination of GMP into IMP [PUBMED:2904262]. NADPH + guanosine 5-phosphate = NADP+ + inosine 5-phosphate + NH3 It converts nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and maintains intracellular balance of A and G nucleotides.

Gene Ontology

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Domain organisation

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Alignments

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

  Seed
(84)
Full
(7826)
Representative proteomes NCBI
(6840)
Meta
(6242)
RP15
(567)
RP35
(1087)
RP55
(1490)
RP75
(1800)
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Format an alignment

  Seed
(84)
Full
(7826)
Representative proteomes NCBI
(6840)
Meta
(6242)
RP15
(567)
RP35
(1087)
RP55
(1490)
RP75
(1800)
Alignment:
Format:
Order:
Sequence:
Gaps:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

  Seed
(84)
Full
(7826)
Representative proteomes NCBI
(6840)
Meta
(6242)
RP15
(567)
RP35
(1087)
RP55
(1490)
RP75
(1800)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

Pfam alignments:

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...

Trees

This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: Prosite
Previous IDs: none
Type: Domain
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 information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null --hand HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 24.0 24.0
Trusted cut-off 24.0 24.0
Noise cut-off 23.9 23.9
Model length: 352
Family (HMM) version: 20
Download: download the raw HMM for this family

Species distribution

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Interactions

There are 3 interactions for this family. More...

CBS IMPDH FMN_dh

Structures

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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