MULTISPECIES: TenA family transcriptional regulator [Acinetobacter]
TenA family transcriptional regulator( domain architecture ID 10009274)
TenA family transcriptional regulator similar to Chlamydia trachomatis Chlamydia protein associating with death domains (CADD), a Chlamydia specific toxin that associates with death domains of tumor necrosis factor family (TNF) receptors and induces apoptosis in mammalian cell lines through a Caspase-dependent mechanism
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
PqqC | COG5424 | Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; |
14-242 | 1.81e-41 | ||||
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; : Pssm-ID: 444176 Cd Length: 228 Bit Score: 141.57 E-value: 1.81e-41
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Name | Accession | Description | Interval | E-value | ||||
PqqC | COG5424 | Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; |
14-242 | 1.81e-41 | ||||
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; Pssm-ID: 444176 Cd Length: 228 Bit Score: 141.57 E-value: 1.81e-41
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Haem_oxygenas_2 | pfam14518 | Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ... |
57-235 | 1.28e-15 | ||||
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase. Pssm-ID: 434009 Cd Length: 178 Bit Score: 72.42 E-value: 1.28e-15
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TenA_PqqC-like | cd16099 | TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
36-237 | 1.66e-06 | ||||
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone (PQQ) synthesis protein C; TenA proteins participate in thiamin metabolism and can be classified into two classes: TenA_C which has an active site Cys, and TenA_E which does not; TenA_E proteins often have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product amino-HMP (4-amino-5-amino-methyl-2-methylpyrimidine) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin. Bacillus subtilis TenA_C can hydrolyze amino-HMP to AMP and can catalyze the hydrolysis of thiamin. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal ThiD domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). Bacillus halodurans TenA_C participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. Helicobacter pylori TenA_C is also thought to catalyze a salvage reaction but the pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect; Pyrococcus furiosus TenA_E lacks appropriate surface charges for DNA interactions. This family also includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C (PQQC), an oxidase involved in the final step of PQQ biosynthesis, and CADD, a Chlamydia protein that interacts with death receptors. Pssm-ID: 381691 [Multi-domain] Cd Length: 196 Bit Score: 47.34 E-value: 1.66e-06
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Name | Accession | Description | Interval | E-value | ||||
PqqC | COG5424 | Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; |
14-242 | 1.81e-41 | ||||
Pyrroloquinoline quinone (PQQ) biosynthesis protein C [Coenzyme transport and metabolism]; Pssm-ID: 444176 Cd Length: 228 Bit Score: 141.57 E-value: 1.81e-41
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Haem_oxygenas_2 | pfam14518 | Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, ... |
57-235 | 1.28e-15 | ||||
Iron-containing redox enzyme; The CADD, Chlamydia protein associating with death domains, crystal structure reveals a dimer of seven-helical bundles. Each bundle contains a di-iron centre adjacent to an internal cavity that forms an active site similar to that of methane mono-oxygenase hydrolase. Pssm-ID: 434009 Cd Length: 178 Bit Score: 72.42 E-value: 1.28e-15
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TENA_THI-4 | pfam03070 | TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
24-160 | 3.57e-09 | ||||
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase. The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4. This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain. Pssm-ID: 397272 [Multi-domain] Cd Length: 210 Bit Score: 55.05 E-value: 3.57e-09
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TenA | COG0819 | Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
19-164 | 1.17e-07 | ||||
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism]; Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 50.65 E-value: 1.17e-07
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TenA_PqqC-like | cd16099 | TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
36-237 | 1.66e-06 | ||||
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone (PQQ) synthesis protein C; TenA proteins participate in thiamin metabolism and can be classified into two classes: TenA_C which has an active site Cys, and TenA_E which does not; TenA_E proteins often have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2) catalyze the hydrolysis of the thiamin breakdown product amino-HMP (4-amino-5-amino-methyl-2-methylpyrimidine) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin. Bacillus subtilis TenA_C can hydrolyze amino-HMP to AMP and can catalyze the hydrolysis of thiamin. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal ThiD domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). Bacillus halodurans TenA_C participates in a salvage pathway where the thiamine degradation product 2-methyl-4-formylamino-5-aminomethylpyrimidine (formylamino-HMP) is hydrolyzed first to amino-HMP by the YlmB protein, and the amino-HMP is then hydrolyzed by TenA to produce HMP. Helicobacter pylori TenA_C is also thought to catalyze a salvage reaction but the pyrimidine substrate has not yet been identified. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect; Pyrococcus furiosus TenA_E lacks appropriate surface charges for DNA interactions. This family also includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C (PQQC), an oxidase involved in the final step of PQQ biosynthesis, and CADD, a Chlamydia protein that interacts with death receptors. Pssm-ID: 381691 [Multi-domain] Cd Length: 196 Bit Score: 47.34 E-value: 1.66e-06
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TenA_PqqC | cd19370 | TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to ... |
37-228 | 8.36e-04 | ||||
TenA_like proteins, including PqqC and CADD; This family contains proteins with similarity to TenA, and includes bacterial coenzyme pyrroloquinoline quinone (PQQ) synthesis protein C or PQQC proteins. PQQ is the prosthetic group of several bacterial enzymes, including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria. PQQC catalyzes the last step of PQQ biogenesis which involves a ring closure and an eight-electron oxidation of the substrate [3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic acid (AHQQ)]. The exact molecular function of members of this family is unclear. Also belonging to this family is Chlamydia protein CADD (Chlamydia protein Associating with Death Domains), a redox protein toxin unique to Chlamydia species, which modulates host cell apoptosis; its redox activity and death domain binding ability may be required for this biological activity. CADD may have a role in folate metabolism. Pssm-ID: 381705 Cd Length: 219 Bit Score: 39.50 E-value: 8.36e-04
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TenA_E_At3g16990-like | cd19357 | TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ... |
37-122 | 3.85e-03 | ||||
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins belongs to the TenA_E class, and lacks the conserved active site Cys residue of the TenA_C class; most have a pair of structurally conserved Glu residues in the active site. TenA_C proteins (EC 3.5.99.2; aminopyrimidine aminohydrolase, also known as thiaminase II) catalyze the hydrolysis of the thiamin breakdown product 4-amino-5-amino-methyl-2-methylpyrimidine (amino-HMP) to 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP) in a thiamin salvage pathway; the role of TenA_E proteins is less clear. Members of this family include Arabidopsis thaliana At3g16990, Zea mays GRMZM2G080501, and Pyrococcus furiosus PF1337, among others. Arabidopsis thaliana TenA_E hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP, but does not hydrolyze thiamin; nor does it have activity with other thiamine degradation products such as thiamine mono- or diphosphate, oxythiamine, oxothiamine, thiamine disulfide, desthiothiamine or thiochrome as substrates. Structural studies of P. furiosus PF1337 strongly support its enzymatic function in thiamine biosynthesis. It has also been suggested that TenA proteins act as transcriptional regulators based on changes in gene-expression patterns when TenA is overexpressed in Bacillus subtilis, however this effect may be indirect. Pssm-ID: 381692 [Multi-domain] Cd Length: 217 Bit Score: 37.30 E-value: 3.85e-03
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Blast search parameters | ||||
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