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Conserved domains on  [gi|491968179|ref|WP_005697457|]
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MULTISPECIES: thiaminase II [Haemophilus]

Protein Classification

TenA family protein( domain architecture ID 14443675)

TenA family protein such as Bacillus halodurans aminopyrimidine aminohydrolase, which catalyzes an amino-pyrimidine hydrolysis reaction at the C5' of the pyrimidine moiety of thiamine compounds, as part of the thiamine salvage pathway

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TenA_C_ScTHI20-like cd19367
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ...
 11-212 3.06e-99

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: 286.33  E-value: 3.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  11 PYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQLHLDYCRQW 90
Cdd:cd19367    1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAEW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  91 DISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENY-PKLPSNPYQAWIDAYSAPEYQQ 169
Cdd:cd19367   81 GISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASDEYQE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491968179 170 AAQETVDFLTALC-EPLNDSQLTNIQQIFTTATRMEIGFWQMGL 212
Cdd:cd19367  161 AVREGIELLEKLAaERPSPARLEELVKIFATATRLEIGFWDMGL 204
 
Name Accession Description Interval E-value
TenA_C_ScTHI20-like cd19367
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ...
 11-212 3.06e-99

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: 286.33  E-value: 3.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  11 PYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQLHLDYCRQW 90
Cdd:cd19367    1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAEW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  91 DISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENY-PKLPSNPYQAWIDAYSAPEYQQ 169
Cdd:cd19367   81 GISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASDEYQE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491968179 170 AAQETVDFLTALC-EPLNDSQLTNIQQIFTTATRMEIGFWQMGL 212
Cdd:cd19367  161 AVREGIELLEKLAaERPSPARLEELVKIFATATRLEIGFWDMGL 204
TenA COG0819
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ...
 4-215 3.01e-84

Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];


Pssm-ID: 440581 [Multi-domain]  Cd Length: 218  Bit Score: 249.03  E-value: 3.01e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLD-ILCQEIQL 82
Cdd:COG0819    6 RLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAgLLEVELAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENyPKLPSNPYQAWIDAY 162
Cdd:COG0819   86 HERYAAELGISEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAER-PLPPDHPYAEWIETY 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491968179 163 SAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLDLA 215
Cdd:COG0819  165 ASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAYRLE 217
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 6-213 1.20e-66

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: 204.13  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179    6 IQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEM-DMPRKTLDILCQEIQLHL 84
Cdd:pfam03070   1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   85 DYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWIDAYSA 164
Cdd:pfam03070  81 RLAEALGLSREDLSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTYAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 491968179  165 PEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLD 213
Cdd:pfam03070 161 EYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALD 209
salvage_TenA TIGR04306
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ...
 10-214 7.51e-45

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: 148.49  E-value: 7.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   10 QPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEM-DMPRKTLDILCQEIQLHLDYCR 88
Cdd:TIGR04306   2 KPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKACDEDMEkELVEQIQGGVETEMGQHKRLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   89 QWDISEQEIFQTPE-SAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENyPKLPSNP-YQAWIDAYSAPE 166
Cdd:TIGR04306  82 VLGISDEEYFQKIKpGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGK-HTAPEHSvYHKWIETYSSSW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491968179  167 YQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLDL 214
Cdd:TIGR04306 161 FREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY 208
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
4-215 8.26e-28

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 109.49  E-value: 8.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDM-PRKTLDILCQEIQL 82
Cdd:PRK14713 323 ALWQASGPIREAIEDLPFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAPDPAEQVFwAQSAQACLEVESEL 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYC--RQWDiseqeifqTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWID 160
Cdd:PRK14713 403 HRSWLgdRDAD--------TAPSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHARAGNPDDHPYAEWLQ 474

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491968179 161 AYSAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLDLA 215
Cdd:PRK14713 475 TYADPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQARRRA 529
 
Name Accession Description Interval E-value
TenA_C_ScTHI20-like cd19367
TenA_C family similar to the C-terminal TenA_C domain of Saccharomyces cerevisiae THI20 ...
 11-212 3.06e-99

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: 286.33  E-value: 3.06e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  11 PYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQLHLDYCRQW 90
Cdd:cd19367    1 PIWKAYTNHPFVRQLADGTLPLESFRHYLKQDYLYLIHYARAHALAAYKAPTLEDIRAAAAILLAILEEMELHVKYCAEW 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  91 DISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENY-PKLPSNPYQAWIDAYSAPEYQQ 169
Cdd:cd19367   81 GISEEELEATPESPATLAYTRYVLDVGLSGDLLDLLVALAPCLLGYGEIGLRLAADPaTKLEGNPYWSWIETYASDEYQE 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491968179 170 AAQETVDFLTALC-EPLNDSQLTNIQQIFTTATRMEIGFWQMGL 212
Cdd:cd19367  161 AVREGIELLEKLAaERPSPARLEELVKIFATATRLEIGFWDMGL 204
TenA COG0819
Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and ...
 4-215 3.01e-84

Aminopyrimidine aminohydrolase TenA (thiamine salvage pathway) [Coenzyme transport and metabolism];


Pssm-ID: 440581 [Multi-domain]  Cd Length: 218  Bit Score: 249.03  E-value: 3.01e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLD-ILCQEIQL 82
Cdd:COG0819    6 RLREAAAPIWEAILEHPFVQGLADGTLPREAFRHYLVQDYLYLEHFARALALAAAKAPDLEDMRFLAGLAAgLLEVELAL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENyPKLPSNPYQAWIDAY 162
Cdd:COG0819   86 HERYAAELGISEEELEATPPSPTTRAYTSYLLAAAASGDYAELLAALLPCEWGYAEIGKRLAER-PLPPDHPYAEWIETY 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491968179 163 SAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLDLA 215
Cdd:COG0819  165 ASEEFQELVEWLIALLDRLAATASEAERERLEEAFRTASRLEYAFWDMAYRLE 217
TENA_THI-4 pfam03070
TENA/THI-4/PQQC family; Members of this family are found in all the three major phyla of life: ...
 6-213 1.20e-66

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: 204.13  E-value: 1.20e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179    6 IQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEM-DMPRKTLDILCQEIQLHL 84
Cdd:pfam03070   1 HPQLRPIWKFYINHPFVQALAKGTLPREQFQGYVIQDYLYLVNFARVLAIIASKSPDLEVRrEWENRIVDHDGNEIELHL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   85 DYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWIDAYSA 164
Cdd:pfam03070  81 RLAEALGLSREDLSAYKPLPATRAYVRYLLDFARRGSWLEAVAALLPCLFVYQEIASRLGEKIRALEGPEYYEWVKTYAS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 491968179  165 PEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLD 213
Cdd:pfam03070 161 EYFRAAVEEAKRLLDRLLAYVSDEQLEELQEIFLKALEFEYSFWTMALD 209
TenA_C_BhTenA-like cd19366
TenA_C proteins similar to Bacillus halodurans TenA; This family of TenA proteins belongs to ...
 4-210 1.29e-65

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: 201.25  E-value: 1.29e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLD-ILCQEIQL 82
Cdd:cd19366    4 RLREKAKPIWEAGLEHPFVQGLGDGTLDKEKFKFYLKQDYLYLIDYARVFALGAAKADDLETMGRFAELLHgTLNTEMDL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWIDAY 162
Cdd:cd19366   84 HRQYAAEFGITEEELEATEPSPTTLAYTSYMLRTAQTGTLAELLAALLPCAWGYAEIGKRLAEQGGALEHNPYREWIEMY 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491968179 163 SAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQM 210
Cdd:cd19366  164 SSDEFTELADWLIDLLDELAEGKSEAELERLEEIFLTSSRYEYMFWDM 211
TenA_C_HP1287-like cd19361
TenA_C proteins similar to Helicobacter pylori TenA (HP1287; This family of TenA proteins ...
 5-210 2.62e-61

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: 190.48  E-value: 2.62e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   5 LIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLD-ILCQEIQLH 83
Cdd:cd19361    5 LYEAVEDIWDSYYEHPFVQGIADGTLDIEKFRFYMIQDYLYLLDYAKVFALGVAKAKDEEVMRFFADLINaILNEEMDIH 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  84 LDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNP-YQAWIDAY 162
Cdd:cd19361   85 RGYMKRLGITEEEIENTKPALDNLSYTSYMLSVAYEGGIAEILAAILSCSWSYEYIAKKLVERYPAALEHEfYGEWVKGY 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491968179 163 SAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQM 210
Cdd:cd19361  165 SSEEYAEANQELIDLLDRLTEDISEEQIEKLEEIFVNCSRYELKFWDM 212
TenA_C-like cd19369
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ...
 11-210 4.22e-56

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: 176.65  E-value: 4.22e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  11 PYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQ-EIQLHLDYCRQ 89
Cdd:cd19369    1 PIWEQYLEHPFIKELGEGTLDKEKFKNYLIQDSLYLKEYAKVFAMGIYKSRTMKEMQFFYSSLSFVNEdETATRIKYLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  90 WDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENY-PKLPSNPYQAWIDAYSAPEYQ 168
Cdd:cd19369   81 FGLTDEDIEKIEPLPENKAYTDYMLGIAKTGDVKEILMAVLPCMLSYYYIFKELVKKYkDNLESNPYKDWIEDYASEEYA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 491968179 169 QAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQM 210
Cdd:cd19369  161 EYCKEWIDFADRLCENLSEEEKEKLKEIFRKASLYELKFWDM 202
TenA_C-like cd19365
uncharacterized TenA_C proteins; This family of TenA proteins belongs to the TenA_C class as ...
 4-208 2.15e-46

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: 152.28  E-value: 2.15e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRK-TLDILCQEIQL 82
Cdd:cd19365    3 ALWEAIAPIYAAILAHPFIRELADGTLPREKFRFYLAQDALYLRDYARALALLAARAPDPEEQVFFARfAAGAIEVEREL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEqeifQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENypKLPSNPYQAWIDAY 162
Cdd:cd19365   83 HRSFLGEFGIDA----AAEPSPVTLAYTSFLLATAATGPYAVAVAAVLPCFWIYAEVGKRLAAA--ASPNHPYQDWIDTY 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 491968179 163 SAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFW 208
Cdd:cd19365  157 SDEEFAEAVRRAIAIVDRLAAEASPEERARMLEAFLRASRLEWMFW 202
TenA_PqqC-like cd16099
TenA-like proteins including TenA_C and TenA_E proteins, as well as pyrroloquinoline quinone ...
 13-210 3.32e-46

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: 151.35  E-value: 3.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  13 WKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQLHLDYCRQWDI 92
Cdd:cd16099    2 WDAILNHPFVQELAAGTLPREKFRYYLAQDYYYLKDFARALALAAAKAPDLELRTFLAELINVLDDELELHEKLLAELGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  93 SEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPklPSNPYQAWIDAYSAPEYQQAAQ 172
Cdd:cd16099   82 SEEDLSEAEPNPATLAYTNHLLRVAARGTPAEGLAALLPCYWSYGEIGRRLAASLP--EHPPYRFWIDFYASDEYQELVE 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491968179 173 ETVDFLTALCEPlNDSQLTNIQQIFTTATRMEIGFWQM 210
Cdd:cd16099  160 ELLQLLDQLAAA-GEEEKEELKEIFLTSLRYELMFWDA 196
salvage_TenA TIGR04306
thiaminase II; The TenA protein of Bacillus subtilis and Staphylococcus aurues, and the ...
 10-214 7.51e-45

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: 148.49  E-value: 7.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   10 QPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEM-DMPRKTLDILCQEIQLHLDYCR 88
Cdd:TIGR04306   2 KPIWDDYINHPFVQKIGDGTLERDKFRFYIEQDYAYLVEYAKVHALGGSKACDEDMEkELVEQIQGGVETEMGQHKRLAE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   89 QWDISEQEIFQTPE-SAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENyPKLPSNP-YQAWIDAYSAPE 166
Cdd:TIGR04306  82 VLGISDEEYFQKIKpGPALRSYTSYMYDVSRRGNWQELVAALLPCLWGYGEAATKLKGK-HTAPEHSvYHKWIETYSSSW 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 491968179  167 YQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLDL 214
Cdd:TIGR04306 161 FREAVNEGENLLNHLAETSSPEELEKLKTIFAESCEYEYNFWTMAYEY 208
TenA_C_BsTenA-like cd19364
TenA_C proteins similar to Bacillus subtilis TenA; This family of TenA proteins belongs to the ...
 4-213 3.62e-40

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: 136.55  E-value: 3.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQ-EIQL 82
Cdd:cd19364    4 ELREAADPLWQKSFEHPFIQGLADGTLPLETFRYYLIQDAYYLKHFAKLHALAAAKADDPAIKALLLEGAQGLAEgELAL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITEnypKLPSNP-YQAWIDA 161
Cdd:cd19364   84 RETFFKELGITEEEIAQTPPAPTAYHYVSHMYRQLNEGSVAEAVAALLPCYWLYQEIGERLAD---AGSPVPlYQRWIDT 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491968179 162 YSAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLD 213
Cdd:cd19364  161 YASDEFTESVQQQIDLVDRLAEEASEEEREKMKQAFLISSYYELQFWEMAYT 212
TenA_C_AtTH2-like cd19368
TenA_C family similar to the N-terminal TenA_C domain of Arabidopsis thaliana thiamine ...
 19-207 1.87e-39

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: 134.68  E-value: 1.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  19 HEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQLHLDYCRQWDISEQEIF 98
Cdd:cd19368   19 HPFVVGLAAGNLPLDSFRHYISQDAHFLEAFARAYELAEAKADDDEDKKAIRELRKGVLEELKLHDSYAEEWGVDLPKEV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  99 QTpeSAACISYTRYLLDCGMTG--GLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWIDAYSAPEYQQAAQETVD 176
Cdd:cd19368   99 TP--DPATRKYTDFLLATASGKvkVAAYTLAAMAPCMRLYAFLGQELARALDDTEDHPYKKWIDTYSSQEFEALALQLED 176

                        170       180       190
                 ....*....|....*....|....*....|.
gi 491968179 177 FLTALCEPLNDSQLTNIQQIFTTATRMEIGF 207
Cdd:cd19368  177 LLDKLSASLTGEELEALEKLYRRAMKLEVEF 207
TenA_C_SaTenA-like cd19360
TenA_C proteins similar to Staphylococcus aureus TenA (SaTenA); This family of TenA proteins ...
 4-210 1.39e-37

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: 129.63  E-value: 1.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLD-ILCQEIQL 82
Cdd:cd19360    4 ELREEAQPILEAIYAHPFVQGIAAGELPKEALIHYVQQDYEYLNAFLKVYALAIAKSDTREDMRFFLEQIGfILNGESHA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWIDAY 162
Cdd:cd19360   84 HQNLCEVAGVDYEELQGAPWAPTADHYIKHMYYAARTGDLGDILAALLPCPWTYVELAKRLIEEGKPTPDNPFYEWIDFY 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491968179 163 SAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQM 210
Cdd:cd19360  164 ADDEMDGLTDQLFARLDRLAEKASEEERERAKQAFLKSCQLEWRFWEM 211
PRK14713 PRK14713
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
4-215 8.26e-28

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 237797 [Multi-domain]  Cd Length: 530  Bit Score: 109.49  E-value: 8.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDM-PRKTLDILCQEIQL 82
Cdd:PRK14713 323 ALWQASGPIREAIEDLPFVRALADGTLPEEAFEFYLAQDALYLNGYSRALARLAALAPDPAEQVFwAQSAQACLEVESEL 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYC--RQWDiseqeifqTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWID 160
Cdd:PRK14713 403 HRSWLgdRDAD--------TAPSPVTLAYTDFLLARAAGGSYAVGAAAVLPCFWLYAEVGAELHARAGNPDDHPYAEWLQ 474

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491968179 161 AYSAPEYQQAAQETVDFLTALCEPLNDSQLTNIQQIFTTATRMEIGFWQMGLDLA 215
Cdd:PRK14713 475 TYADPEFAAATRRAIAFVDRAFRAASPAERAAMARAFLTACRYELEFFDQARRRA 529
TenA_C_PH1161-like cd19363
uncharacterized TenA_C proteins similar to Pyrococcus horikoshii PH1161; This family of TenA ...
 3-210 9.34e-26

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: 98.94  E-value: 9.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   3 NQLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMdmpRKTLDILCQEIQL 82
Cdd:cd19363    3 GKLRRDADDIWKKILNHPFVVELYSGTLPMEKFKFYLLQDYNYLVGSTKNLSILASKAESLDLM---RELLELAYGEATT 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HL-DYCR---QWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAW 158
Cdd:cd19363   80 EFaNYEElldELGLSLEDAIKVEPFPTNVAYMNFLLSTSSLGSFYEGLAALLPCFWSYLEIAEYHKDKLSENPNDIYRDW 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 491968179 159 IDAYSAPEYQQAAQETVDFLTALCEPLNDSQLTniqQIFTTATRMEIGFWQM 210
Cdd:cd19363  160 ASVYLSKEYKELVERLRRIVDKYGEGEPFEKLK---RIFKTASKYEYMFWDA 208
TenA_C_SsTenA-1-like cd19362
uncharacterized TenA_C proteins similar to Sulfolobus solfataricus TenA-1 (Sso2206); This ...
 13-212 6.13e-25

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: 96.74  E-value: 6.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  13 WKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAfalgVFKARNFAEMDMPRKTLDILCQE----IQLHLDYCR 88
Cdd:cd19362   12 WNKYVRHEFVERMRDGTLPLDNFRYYLIQDSKYVEEMLRA----LLRASSKAPLDKAIKILNSVFSGrdkgMEVHKFLYS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  89 QWDISEQEIFQTPESAACISYTRYLLDCGmTGGLPELYAAVTPCALGYAQVARYITENypklPSNPYQAWIDAYSAPEYQ 168
Cdd:cd19362   88 ELGITEDEIRRTGYNLVNYAYTRHLYYYS-TLGWPQFLAAWAPCMWGYSEIGKYVLNS----PNELYKTWASFYASKDYK 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 491968179 169 qaaqetvDFLTALCEPLNDSQLT-NIQQIFTTATRMEIGFWQMGL 212
Cdd:cd19362  163 -------KRVEAILEALDSIEDTeDIKNIFRNSVNFEIMFWDAAL 200
TenA_C_Bt3146-like cd19359
uncharacterized TenA_C proteins similar to Bacteroides thetaiotaomicron Bt3146; This family of ...
 2-208 9.02e-25

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: 96.26  E-value: 9.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   2 INQLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQ 81
Cdd:cd19359    1 IDKLWNDNEDLWDKALNNPFCQGMADGTLDLDGFGYYMVQDYYYCINYVRFKALRAAKAPDPDLLAFLAAKIKSYLDYAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  82 LHLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENYPKLPSNPYQAWIDA 161
Cdd:cd19359   81 DFLKTCHIKLGIPDVVDGVKPSPALKAYVDFERSVAESEDWFYLLVAMIPCIYLWYWLANQLNEDPSDKNTNFYKTWIEP 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 491968179 162 YSApeYQQAAQETVDFLTAlCEPLNDSQLTNIQQIFTTATRMEIGFW 208
Cdd:cd19359  161 NLP--DPSSAKQLEFFLNA-NAAWSKIDREKANEIFRQAMQLEINFF 204
PTZ00347 PTZ00347
phosphomethylpyrimidine kinase; Provisional
 4-208 5.62e-23

phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 240375 [Multi-domain]  Cd Length: 504  Bit Score: 95.80  E-value: 5.62e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILCQEIQ-L 82
Cdd:PTZ00347  16 ALWKENQDLAMMSLHLPFVQGLGDGTLDQNAFRTYIAQDTLYLNGYIRILSYCITKSDVTATGGGLLELLKGVLEELKnC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEifqtpesAACISYTRYLLDCGMTGGLPEL--YAAVTPCALGYAQVARYITENYPKLPSNPYQAWID 160
Cdd:PTZ00347  96 HHHYIDNPDAAGPE-------AACRKYVDFLLASGNADTLGPSvvIAAVIPCARLYAWVGQELTNEVELTESHPFRRWLL 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491968179 161 AYSAPEYQQAAQETVDFLTALCEPLNDSQltnIQQIFTTATRMEIGFW 208
Cdd:PTZ00347 169 SYSDEPINTSVEQLESLLDKYIRPGEFSE---VAQAYRRAMELEYDFF 213
TenA_E_Spr0628-like cd19358
TenA_E proteins similar to Streptococcus pneumoniae Spr0628 and Saccharomyces cerevisiae S288C ...
 4-210 4.68e-19

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: 81.46  E-value: 4.68e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   4 QLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFAEMDMPRKTLDILC-QEIQL 82
Cdd:cd19358    4 RLRAANAEDWDAAVTHRFVRELCAGTLPDAVLARYLVQDYQFVETFLRLLGKAVAKAPDLEAKLRLARFLGFLAnDENDY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  83 HLDYCRQWDISEQEIFQTPESAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITEnypKLPSNP-YQAWIDA 161
Cdd:cd19358   84 FERAFAALGVSEADREAPPLLPATRAFIDLMLEAARSGSYAEILTVLLVAEWLYLDWASRAAA---AAPLRFkHQEWIDL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491968179 162 YSAPEYQQAaqetVDFLTALCE--PLNDSQLTNIQQIFTTATRMEIGFWQM 210
Cdd:cd19358  161 HSGPEFEAW----VDFLRDEVDrvGPTEEERERLEAVFARAVELEIAFFDA 207
PRK09517 PRK09517
multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; ...
 21-208 1.61e-18

multifunctional thiamine-phosphate pyrophosphorylase/synthase/phosphomethylpyrimidine kinase; Provisional


Pssm-ID: 169939 [Multi-domain]  Cd Length: 755  Bit Score: 83.48  E-value: 1.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  21 FVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFA-LGVFKARNFAEMDMPRKTLDILCQEIQLHldycRQWdISEQEIFQ 99
Cdd:PRK09517 566 FIRMLGDGTLRRPEFDFYIDQDAQYLRQYSRALArLSSIAPDSHAQVEWAQSAAECIVVEAELH----RSY-LSGKEAPS 640

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179 100 TPeSAACISYTRYLLDCGMTGGLPELYAAVTPCALGYAQVARYITENypKLPSNPYQAWIDAYSAPEYQQAAQETVDFLT 179
Cdd:PRK09517 641 AP-SPVTMAYTDFLIARTYTEDYVVGVAAVLPCYWLYAEIGLMLAEQ--NHDEHPYKDWLNTYSGEEFIAGTRAAIARVE 717

                        170       180
                 ....*....|....*....|....*....
gi 491968179 180 ALCEPLNDSQLTNIQQIFTTATRMEIGFW 208
Cdd:PRK09517 718 KALENAGPEQRVDAARAFLSASVHEREFF 746
TenA_E_At3g16990-like cd19357
TenA_E proteins similar to Arabidopsis thaliana At3g16990; This family of TenA proteins ...
 2-210 1.26e-17

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: 77.74  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179   2 INQLIQQTQPYWKQYVEHEFVQQLAQGTLPKACFQHYLKQDYIYLFHYSRAFALGVFKARNFaEMDMPRKTLDILC---- 77
Cdd:cd19357    1 TSHLLSLHPALYTAATQHPFLRAAADGTLPKEALSRWLAQDRLYVQAYIRFLGSLLARAPLP-SSSLNQRLLDVLLgala 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491968179  78 ---QEIQLHLDYCRQWDISEQEiFQTPESAACISYTRYLLDCGmTGGLPELYAAVtpcALG-----YAQVARYITENYPK 149
Cdd:cd19357   80 nlrRELAFFEETAAEYGLDLPG-LGVPPSPATRAYVDFLASLA-SEGVSYLEGLV---VLWatekvYLDAWSYARSFLPS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491968179 150 LP--SNPYQAWIDAYSAPEYQQaaqeTVDFLTALCEPLNDSQLTNIQQ----IFTTATRMEIGFWQM 210
Cdd:cd19357  155 DAdgGALYREFIPNWTSPEFAA----FVDRLGDLVDEALEQAGEEVLEraeeVWRRVLELEEAFWPM 217
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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