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InterPro: IPR003607 Metal-dependent phosphohydrolase, HD domain
Protein matches
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UniProtKB Matches: 16030 proteins |
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Accession
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IPR003607 Metal-dep_PHydrolase_HD_dom |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Children
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IPR002073 3'5'-cyclic nucleotide phosphodiesterase
IPR006674 Metal-dependent phosphohydrolase, HD subdomain
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Found in
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IPR005249 Conserved hypothetical protein CHP00488
IPR006261 Deoxyguanosinetriphosphate triphosphohydrolase
IPR010043 Protein-PII uridylyltransferase
IPR011119 Protein of unknown function, putative helicase/relaxase
IPR012006 tRNA nucleotidyltransferase, proteobacteria
IPR017670 Phosphonate degradation operon associated HDIG domain protein
IPR017705 2,3-cyclic-nucleotide 2-phosphodiesterase
IPR020779 Deoxyguanosinetriphosphate triphosphohydrolase, proteobacteria
IPR020873 3'-5' exoribonuclease YhaM
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GO Term annotation
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Function
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GO:0003824 catalytic activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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The HD domain is found in a superfamily of enzymes with a predicted or known phosphohydrolase activity. These enzymes appear to be involved in the nucleic acid metabolism, signal transduction and possibly other functions in bacteria, archaea and eukaryotes.
The fact that all the highly conserved residues in the HD superfamily are histidines or aspartates suggests that coordination of divalent cations is essential for the activity of these proteins [1]. This domain is also found in eukaryotic 3',5'-cGMP phosphodiesterase (EC:3.1.4.17) (PDE), which is located in photoreceptor outer segments [2] and it is light activated, playing a pivotal role in
signal transduction. This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).
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Structural links
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Additional Reading
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Liu S, Mansour MN, Dillman KS, Perez JR, Danley DE, Aeed PA, Simons SP, Lemotte PK, Menniti FS.
Structural basis for the catalytic mechanism of human phosphodiesterase 9.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 13309-14
[PubMed: 18757755]
http://dx.doi.org/10.1073/pnas.0708850105
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Chen G, Wang H, Robinson H, Cai J, Wan Y, Ke H.
An insight into the pharmacophores of phosphodiesterase-5 inhibitors from synthetic and crystal structural studies.
Biochem. Pharmacol. 75 2008 1717-28
[PubMed: 18346713]
http://dx.doi.org/10.1016/j.bcp.2008.01.019
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Wang H, Ye M, Robinson H, Francis SH, Ke H.
Conformational variations of both phosphodiesterase-5 and inhibitors provide the structural basis for the physiological effects of vardenafil and sildenafil.
Mol. Pharmacol. 73 2008 104-10
[PubMed: 17959709]
http://dx.doi.org/10.1124/mol.107.040212
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Oganesyan V, Adams PD, Jancarik J, Kim R, Kim SH.
Structure of O67745_AQUAE, a hypothetical protein from Aquifex aeolicus.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 2007 369-74
[PubMed: 17565173]
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Zimmerman MD, Proudfoot M, Yakunin A, Minor W.
Structural insight into the mechanism of substrate specificity and catalytic activity of an HD-domain phosphohydrolase: the 5'-deoxyribonucleotidase YfbR from Escherichia coli.
J. Mol. Biol. 378 2008 215-26
[PubMed: 18353368]
http://dx.doi.org/10.1016/j.jmb.2008.02.036
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InterPro 23.1
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