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InterPro: IPR014036 HTH transcriptional regulator, DeoR

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UniProtKB
Matches:
4601 proteins
AccessionHelp IPR014036 HTH_DeoR
SecondaryHelp IPR001034
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InterPro annotation
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AbstractHelp

The deoR-type HTH domain is a DNA-binding, helix-turn-helix (HTH) domain of about 50-60 amino acids present in transcription regulators of the deoR family, involved in sugar catabolism. This family of prokaryotic regulators is named after Escherichia coli deoR, a repressor of the deo operon, which encodes nucleotide and deoxyribonucleotide catabolic enzymes. DeoR also negatively regulates the expression of nupG and tsx, a nucleoside-specific transport protein and a channel-forming protein, respectively.

DeoR-like transcription repressors occur in diverse bacteria as regulators of sugar and nucleoside metabolic systems. The effector molecules for deoR-like regulators are generally phosphorylated intermediates of the relevant metabolic pathway. The DNA-binding deoR-type HTH domain occurs usually in the N-terminal part. The C-terminal part can contain an effector-binding domain and/or an oligomerization domain. DeoR occurs as an octamer, whilst glpR and agaR are tetramers. Several operators may be bound simultaneously, which could facilitate DNA looping [1, 2].

Structural linksHelp
SCOP: c.124.1.4
CATH: 3.40.50.1360
Database linksHelp Pfam Clan: CL0246.4

Taxonomic coverageHelp

Example proteinsHelp
A2C4N6 Ribose-5-phosphate isomerase A

O50083 Ribose-5-phosphate isomerase A

Q6G3V6 Ribose-5-phosphate isomerase A

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Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR014036 HTH transcriptional regulator, DeoR
IPR004788 Ribose 5-phosphate isomerase
IPR020672 Ribose-5-phosphate isomerase, subgroup
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Beck von Bodman S, Hayman GT, Farrand SK.
Opine catabolism and conjugal transfer of the nopaline Ti plasmid pTiC58 are coordinately regulated by a single repressor.
Proc. Natl. Acad. Sci. U.S.A. 89 643-7 1992 [PubMed: 1731335]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1731335&action=stream&blobtype=pdf
2. Ray WK, Larson TJ.
Application of AgaR repressor and dominant repressor variants for verification of a gene cluster involved in N-acetylgalactosamine metabolism in Escherichia coli K-12.
Mol. Microbiol. 51 813-26 2004 [PubMed: 14731281]
http://dx.doi.org/10.1046/j.1365-2958.2003.03868.x

Additional ReadingHelp
Ishikawa K, Matsui I, Payan F, Cambillau C, Ishida H, Kawarabayasi Y, Kikuchi H, Roussel A.
A hyperthermostable D-ribose-5-phosphate isomerase from Pyrococcus horikoshii characterization and three-dimensional structure.
Structure 10 2002 877-86 [PubMed: 12057201]
http://dx.doi.org/10.1016/S0969-2126(02)00779-7
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InterPro 23.1