Summary: Taurine catabolism dioxygenase TauD, TfdA family
This is the Wikipedia entry entitled "TauD protein domain". More...
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TauD protein domain Edit Wikipedia article
ensemble refinement of the protein crystal structure of gene product from arabidopsis thaliana at3g21360
In molecular biology, TauD refers to a protein domain that in many enteric bacteria is used to break down taurine (2-aminoethanesulphonic acid) as a source of sulphur under stress conditions. In essence, they are domains found in enzymes that provide bacteria with an important nutrient.
This protein family consists of TauD/TfdA taurine catabolism dioxygenases. The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulphonic acid) as a sulphur source and is expressed only under conditions of sulphate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulphite from taurine. The 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. (strain RASC) also belongs to this family. TfdA from Ralstonia eutropha (Alcaligenes eutrophus) is a 2,4-D monooxygenase.
- Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T (September 1997). "Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli". J. Biol. Chem. 272 (37): 23031–6. doi:10.1074/jbc.272.37.23031. PMID 9287300.
- Suwa Y, Wright AD, Fukimori F, Nummy KA, Hausinger RP, Holben WE, Forney LJ (July 1996). "Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC". Appl. Environ. Microbiol. 62 (7): 2464–9. PMC 168028. PMID 8779585.
- Streber WR, Timmis KN, Zenk MH (July 1987). "Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134". J. Bacteriol. 169 (7): 2950–5. PMC 212332. PMID 3036764.
Taurine catabolism dioxygenase TauD, TfdA family Provide feedback
This family consists of taurine catabolism dioxygenases of the TauD, TfdA family. TauD from E. coli P37610 is a alpha-ketoglutarate-dependent taurine dioxygenase . This enzyme catalyses the oxygenolytic release of sulfite from taurine . TfdA from Burkholderia sp. Q45423 is a 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase . TfdA from Alcaligenes eutrophus JMP134 P10088 is a 2,4-dichlorophenoxyacetate monooxygenase . Also included are gamma-Butyrobetaine hydroxylase enzymes EC:184.108.40.206 .
Eichhorn E, van der Ploeg JR, Kertesz MA, Leisinger T; , J Biol Chem 1997;272:23031-23036.: Characterization of alpha-ketoglutarate-dependent taurine dioxygenase from Escherichia coli. PUBMED:9287300 EPMC:9287300
Suwa Y, Wright AD, Fukimori F, Nummy KA, Hausinger RP, Holben WE, Forney LJ; , Appl Environ Microbiol 1996;62:2464-2469.: Characterization of a chromosomally encoded 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. strain RASC. PUBMED:8779585 EPMC:8779585
Streber WR, Timmis KN, Zenk MH; , J Bacteriol 1987;169:2950-2955.: Analysis, cloning, and high-level expression of 2,4-dichlorophenoxyacetate monooxygenase gene tfdA of Alcaligenes eutrophus JMP134. PUBMED:3036764 EPMC:3036764
Ruetschi U, Nordin I, Odelhog B, Jornvall H, Lindstedt S; , Eur J Biochem 1993;213:1075-1080.: gamma-Butyrobetaine hydroxylase. Structural characterization of the Pseudomonas enzyme. PUBMED:8504802 EPMC:8504802
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR003819This family consists of TauD/TfdA taurine catabolism dioxygenases. The Escherichia coli tauD gene is required for the utilization of taurine (2-aminoethanesulphonic acid) as a sulphur source and is expressed only under conditions of sulphate starvation. TauD is an alpha-ketoglutarate-dependent dioxygenase catalyzing the oxygenolytic release of sulphite from taurine [PUBMED:9287300]. The 2,4-dichlorophenoxyacetic acid/alpha-ketoglutarate dioxygenase from Burkholderia sp. (strain RASC) also belongs to this family [PUBMED:8779585]. TfdA from Ralstonia eutropha (Alcaligenes eutrophus) is a 2,4-D monooxygenase [PUBMED:3036764].
|Molecular function||oxidoreductase activity (GO:0016491)|
|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
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This clan represents the conserved barrel domain of the 'cupin' superfamily  ('cupa' is the Latin term for a small barrel). The cupin fold is found in a wide variety of enzymes, but notably contains the non-enzymatic seed storage proteins also.
The clan contains the following 53 members:2OG-Fe_Oxy_2 2OG-FeII_Oxy 2OG-FeII_Oxy_2 2OG-FeII_Oxy_3 2OG-FeII_Oxy_4 2OG-FeII_Oxy_5 3-HAO AraC_binding AraC_binding_2 AraC_N ARD Asp_Arg_Hydrox Auxin_BP CDO_I CENP-C_C CsiD Cupin_1 Cupin_2 Cupin_3 Cupin_4 Cupin_5 Cupin_6 Cupin_7 Cupin_8 dTDP_sugar_isom DUF1255 DUF1479 DUF1498 DUF1637 DUF1971 DUF386 DUF4437 Ectoine_synth EutQ FdtA FTO_NTD GPI HgmA HutD JmjC KduI MannoseP_isomer Ofd1_CTDD Oxygenase-NA PhyH Pirin Pirin_C PMI_typeI Pox_C4_C10 TauD Tet_JBP VIT VIT_2
We make a range of alignments for each Pfam-A family:
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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:||Bashton M, Bateman A, Mifsud W|
|Number in seed:||123|
|Number in full:||5659|
|Average length of the domain:||240.80 aa|
|Average identity of full alignment:||19 %|
|Average coverage of the sequence by the domain:||77.33 %|
|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:||11|
|Download:||download the raw HMM for this family|
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There is 1 interaction 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 TauD domain has been found. There are 78 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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