MULTISPECIES: thiaminase II [Staphylococcus]
Protein Classification
heme oxygenase-like domain-containing protein( domain architecture ID 60957)
heme oxygenase-like domain-containing protein such as pyrroloquinoline-quinone synthase that catalyzes the ring cyclization and eight-electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| HemeO-like super family | cl15243 | heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the ... |
11-218 | 7.19e-108 | ||||
heme oxygenase; Heme oxygenase (HO, EC 1.14.14.18) catalyzes the rate limiting step in the degradation of heme to biliverdin in a multi-step reaction. HO is essential for recycling iron from heme which is used as a substrate and cofactor for its own degradation to biliverdin, iron, and carbon monoxide. This family serves a variety of specific needs in different branches of life: in vertebrates, HO plays a role in heme homeostasis and oxidative stress response, and cellular signaling in mammals that include isoforms HO-1 and HO-2; in photosynthetic organisms including cyanobacteria, algae, and higher plants, biliverdin is used for photosynthetic pigment formation or light-sensing; and, in pathogenic bacteria, HO is part of a pathway for iron acquisition from host heme and heme products. HO shares tertiary structure similarity to methane monooxygenase (EC 1.14.13.25), ribonucleotide reductase (EC 1.17.4.1) and thiaminase II (EC 3.5.99.2), but shares little sequence homology. The actual alignment was detected with superfamily member TIGR04306: Pssm-ID: 449518 [Multi-domain] Cd Length: 208 Bit Score: 309.12 E-value: 7.19e-108
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| salvage_TenA | TIGR04306 | thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
11-218 | 7.19e-108 | ||||
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the C-terminal region of trifunctional protein Thi20p from Saccharomyces cerevisiae, perform cleavages on thiamine and related compounds to produce 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), a substrate a salvage pathway for thiamine biosynthesis. The gene symbol tenA, for Transcription ENhancement A, reflects a misleading early characterization as a regulatory protein. This family is related to PqqC from the PQQ biosynthesis system (see TIGR02111), heme oxygenase (pfam01126), and CADD (Chlamydia protein Associating with Death Domains), a putative folate metabolism enzyme (see TIGR04305). Pssm-ID: 213919 [Multi-domain] Cd Length: 208 Bit Score: 309.12 E-value: 7.19e-108
|
||||||||
| TenA_C_SaTenA-like | cd19360 | TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ... |
3-214 | 2.39e-92 | ||||
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. This family includes Staphylococcus aureus TenA (SaTenA) which plays two essential roles in thiamin metabolism: in the deamination of aminopyrimidine to HMP, and in hydrolyzing thiamin into HMP and 5-(2-hydroxyethyl)4-methylthiazole (THZ). 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. SaTenA is then also a putative transcriptional regulator controlling the secretion of extracellular proteases such as subtilisin-type proteases in bacteria. This family includes mostly uncharacterized TenA like proteins. Pssm-ID: 381695 [Multi-domain] Cd Length: 211 Bit Score: 269.84 E-value: 2.39e-92
|
||||||||
| TenA | COG0819 | Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
1-220 | 2.83e-54 | ||||
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism]; Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 173.15 E-value: 2.83e-54
|
||||||||
| PTZ00347 | PTZ00347 | phosphomethylpyrimidine kinase; Provisional |
23-221 | 5.00e-11 | ||||
phosphomethylpyrimidine kinase; Provisional Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 61.52 E-value: 5.00e-11
|
||||||||
| TENA_THI-4 | pfam03070 | TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
8-217 | 1.14e-10 | ||||
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: 58.91 E-value: 1.14e-10
|
||||||||
| Name | Accession | Description | Interval | E-value | ||||
| salvage_TenA | TIGR04306 | thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ... |
11-218 | 7.19e-108 | ||||
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the C-terminal region of trifunctional protein Thi20p from Saccharomyces cerevisiae, perform cleavages on thiamine and related compounds to produce 4-amino-5-hydroxymethyl-2-methylpyrimidine (HMP), a substrate a salvage pathway for thiamine biosynthesis. The gene symbol tenA, for Transcription ENhancement A, reflects a misleading early characterization as a regulatory protein. This family is related to PqqC from the PQQ biosynthesis system (see TIGR02111), heme oxygenase (pfam01126), and CADD (Chlamydia protein Associating with Death Domains), a putative folate metabolism enzyme (see TIGR04305). Pssm-ID: 213919 [Multi-domain] Cd Length: 208 Bit Score: 309.12 E-value: 7.19e-108
|
||||||||
| TenA_C_SaTenA-like | cd19360 | TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ... |
3-214 | 2.39e-92 | ||||
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. This family includes Staphylococcus aureus TenA (SaTenA) which plays two essential roles in thiamin metabolism: in the deamination of aminopyrimidine to HMP, and in hydrolyzing thiamin into HMP and 5-(2-hydroxyethyl)4-methylthiazole (THZ). 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. SaTenA is then also a putative transcriptional regulator controlling the secretion of extracellular proteases such as subtilisin-type proteases in bacteria. This family includes mostly uncharacterized TenA like proteins. Pssm-ID: 381695 [Multi-domain] Cd Length: 211 Bit Score: 269.84 E-value: 2.39e-92
|
||||||||
| TenA | COG0819 | Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ... |
1-220 | 2.83e-54 | ||||
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism]; Pssm-ID: 440581 [Multi-domain] Cd Length: 218 Bit Score: 173.15 E-value: 2.83e-54
|
||||||||
| TenA_C_BsTenA-like | cd19364 | TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ... |
3-217 | 6.09e-37 | ||||
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. This family includes Bacillus subtilis TenA which has been shown to be a thiaminase II, catalyzing the hydrolysis of thiamine into HMP and 5-(2-hydroxyethyl)-4-methylthiazole (THZ), within thiamine metabolism. 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: 381699 [Multi-domain] Cd Length: 212 Bit Score: 128.46 E-value: 6.09e-37
|
||||||||
| TenA_PqqC-like | cd16099 | TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ... |
14-214 | 1.01e-34 | ||||
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: 122.46 E-value: 1.01e-34
|
||||||||
| TenA_C-like | cd19365 | uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
4-215 | 1.13e-24 | ||||
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. 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. This family includes mostly uncharacterized TenA_C- like proteins. Pssm-ID: 381700 [Multi-domain] Cd Length: 205 Bit Score: 96.43 E-value: 1.13e-24
|
||||||||
| TenA_C_BhTenA-like | cd19366 | TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ... |
3-215 | 1.75e-20 | ||||
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. This family includes Bacillus halodurans TenA which 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. 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: 381701 [Multi-domain] Cd Length: 213 Bit Score: 85.69 E-value: 1.75e-20
|
||||||||
| TenA_C_HP1287-like | cd19361 | TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ... |
3-214 | 9.10e-19 | ||||
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. This family includes Helicobacter pylori TenA (HP1287) protein which is thought to catalyze a salvage reaction in thiamin metabolism, however its 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. HP1287 may contribute to stomach colonization and persistence. Pssm-ID: 381696 [Multi-domain] Cd Length: 212 Bit Score: 81.09 E-value: 9.10e-19
|
||||||||
| TenA_C-like | cd19369 | uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ... |
13-214 | 2.98e-16 | ||||
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. 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. This family includes mostly uncharacterized TenA_C- like proteins. Pssm-ID: 381704 [Multi-domain] Cd Length: 202 Bit Score: 74.19 E-value: 2.98e-16
|
||||||||
| TenA_C_AtTH2-like | cd19368 | TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine ... |
3-213 | 1.01e-15 | ||||
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine requiring 2; This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. Arabidopsis thaliana TH2 is an orphan enzyme thiamin monophosphate phosphatase which has a haloacid dehalogenase (HAD) family domain fused to its TenA_C domain, it's TenA_C domain has thiamin salvage hydrolase activity against amino-HMP. This family includes mostly uncharacterized single-domain TenA_C- like proteins; some however have additional domains such as a HAD family domain or a kinase domain 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: 381703 [Multi-domain] Cd Length: 210 Bit Score: 73.04 E-value: 1.01e-15
|
||||||||
| TenA_C_ScTHI20-like | cd19367 | TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ... |
22-216 | 2.27e-11 | ||||
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 protein; This TenA family belongs to the TenA_C class as it has a conserved active site Cys residue; the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. Saccharomyces cerevisiae THI20 includes a C-terminal tetrameric TenA-like domain fused to an N-terminal HMP kinase/HMP-P kinase (ThiD-like) domain, and participates in thiamin biosynthesis, degradation and salvage; the TenA-like domain catalyzes the production of HMP from thiamin degradation products (salvage). A majority of this family are single-domain TenA_C- like proteins; some however have additional domains such as a ThiD domain. 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: 381702 [Multi-domain] Cd Length: 204 Bit Score: 60.99 E-value: 2.27e-11
|
||||||||
| TenA_C_PH1161-like | cd19363 | uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ... |
4-215 | 4.16e-11 | ||||
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. 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. This family includes functionally uncharacterized TenA like proteins such as Pyrococcus horikoshii PH1161 protein. Pssm-ID: 381698 [Multi-domain] Cd Length: 210 Bit Score: 60.42 E-value: 4.16e-11
|
||||||||
| PTZ00347 | PTZ00347 | phosphomethylpyrimidine kinase; Provisional |
23-221 | 5.00e-11 | ||||
phosphomethylpyrimidine kinase; Provisional Pssm-ID: 240375 [Multi-domain] Cd Length: 504 Bit Score: 61.52 E-value: 5.00e-11
|
||||||||
| TENA_THI-4 | pfam03070 | TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ... |
8-217 | 1.14e-10 | ||||
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: 58.91 E-value: 1.14e-10
|
||||||||
| PRK14713 | PRK14713 | bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
3-215 | 6.61e-10 | ||||
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; Pssm-ID: 237797 [Multi-domain] Cd Length: 530 Bit Score: 58.26 E-value: 6.61e-10
|
||||||||
| PRK09517 | PRK09517 | multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ... |
3-215 | 1.92e-09 | ||||
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional Pssm-ID: 169939 [Multi-domain] Cd Length: 755 Bit Score: 56.91 E-value: 1.92e-09
|
||||||||
| TenA_C_Bt3146-like | cd19359 | uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of ... |
5-213 | 6.92e-09 | ||||
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. 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. This family includes mostly uncharacterized TenA-like proteins such as Bacteroides thetaiotaomicron Bt3146. Pssm-ID: 381694 [Multi-domain] Cd Length: 206 Bit Score: 53.89 E-value: 6.92e-09
|
||||||||
| TenA_E_Spr0628-like | cd19358 | TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ... |
3-215 | 4.39e-05 | ||||
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C PET18; 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. Arabidopsis thaliana TenA_E (not belonging to this family) hydrolyzes amino-HMP to AMP, and the N-formyl derivative of amino-HMP to amino-HMP. Members of this family include the putative thiaminase Streptococcus pneumoniae Spr0628, and Saccharomyces cerevisiae S288C PET18, a protein of unknown function whose expression is induced in the absence of thiamin. 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. Many proteins in this family have yet to be characterized. Pssm-ID: 381693 [Multi-domain] Cd Length: 209 Bit Score: 42.94 E-value: 4.39e-05
|
||||||||
| TenA_C_SsTenA-1-like | cd19362 | uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This ... |
22-216 | 1.50e-03 | ||||
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This family of TenA proteins belongs to the TenA_C class as it has a conserved active site Cys residue; only one of the double Glu residues identified in the active site of TenA_E from the archaeon Pyrococcus furiosus is conserved in this family. TenA_C proteins (EC 3.5.99.2) 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. 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. This family includes mostly uncharacterized TenA like proteins such as Sulfolobus solfataricus putative TenA-like thiaminase (Tena-1, Sso2206). Pssm-ID: 381697 [Multi-domain] Cd Length: 200 Bit Score: 38.58 E-value: 1.50e-03
|
||||||||
| Blast search parameters | ||||
|
