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Conserved domains on  [gi|1034654945|ref|XP_016867469|]
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thiamin pyrophosphokinase 1 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02714 super family cl29325
thiamin pyrophosphokinase
 6-161 1.71e-48

thiamin pyrophosphokinase


The actual alignment was detected with superfamily member PLN02714:

Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 156.33  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   6 RGCELIS-TPDQDHTDFTKCLKMLQKKIEEKDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHITpfpIIIIQEESLIYL 84
Cdd:PLN02714   76 LGTKIVDeSHDQDTTDLHKCIAYIRDSTPDLDKSNLCILVLGALGGRFDHEAGNINVLYRFPDLR---IVLLSDDCLIRL 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654945  85 L-QPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDgSGVVTVETDHPLLWTMAI 161
Cdd:PLN02714  153 LpATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIVK-EDKVTVESDSDLLWTISI 229
 
Name Accession Description Interval E-value
PLN02714 PLN02714
thiamin pyrophosphokinase
 6-161 1.71e-48

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 156.33  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   6 RGCELIS-TPDQDHTDFTKCLKMLQKKIEEKDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHITpfpIIIIQEESLIYL 84
Cdd:PLN02714   76 LGTKIVDeSHDQDTTDLHKCIAYIRDSTPDLDKSNLCILVLGALGGRFDHEAGNINVLYRFPDLR---IVLLSDDCLIRL 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654945  85 L-QPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDgSGVVTVETDHPLLWTMAI 161
Cdd:PLN02714  153 LpATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIVK-EDKVTVESDSDLLWTISI 229
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 2-159 1.19e-40

Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 153431 [Multi-domain]  Cd Length: 208  Bit Score: 135.75  E-value: 1.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   2 RLAERGCELISTPD-QDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATHITPfPIIIIQEES 80
Cdd:cd07995    59 YYKSKGVEIIHFPDeKDFTDFEKALKLALER------GADEIVILGATGGRLDHTLANLNLLLKYAKDGI-KIVLIDEQN 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945  81 LIYLLQPGKHRLHVDTgmEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTYDG-SGVVTVETDhPLLWTM 159
Cdd:cd07995   132 EIFLLLPGSHTLELEE--EGKYVSLIPLGEVT-GLTLKGLKYPLDNATLSFGSSLGTSNEFTGeKATVSVESG-LLLVIL 207
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 14-159 2.15e-32

thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273588 [Multi-domain]  Cd Length: 205  Bit Score: 114.30  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945  14 PDQDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATHiTPFPIIIIQEESLIYLLQPGKHrlH 93
Cdd:TIGR01378  70 PEKDTTDLELALKYALER------GADEITILGATGGRLDHTLANLNLLLEYAK-RGIEVRLIDEQNVIRLLLPGKY--Q 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654945  94 VDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLLWTM 159
Cdd:TIGR01378 141 IFKEPKGTYISLLPFGGDVHGLTTKGLKYPLNNADLKFGGTRGISNEFIGN-KATVSVDSGILLVI 205
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 2-151 1.80e-25

Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441172 [Multi-domain]  Cd Length: 209  Bit Score: 96.40  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   2 RLAERGCELIS-TPDQDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATHItPFPIIIIQEES 80
Cdd:COG1564    61 QYKEKGVEIIIfPPEKDETDTELALRYALER------GADEILILGATGGRLDHTLANLSLLARYAEK-GIRIVLIDENN 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654945  81 LIYLLQPGKHRLHvdtGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSN-TYDGSGVVTVET 151
Cdd:COG1564   134 EIFLLPPGSLTLE---GPPGTYVSLIPLSDPVTGLTLEGLKYPLDNATLTFGSSLGISNeAIGDEATISVES 202
TPK_B1_binding pfam04265
Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC: ...
 89-156 1.22e-19

Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 461244 [Multi-domain]  Cd Length: 66  Bit Score: 77.49  E-value: 1.22e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654945  89 KHRLHVDTGMeGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLL 156
Cdd:pfam04265   1 EHTIKKEEGF-GKYCSLIPLGGPVTGLTLKGLKYPLTNATLSFGGSLSTSNEFVEE-EATISFDSGIL 66
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 88-155 2.47e-18

Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 214953 [Multi-domain]  Cd Length: 66  Bit Score: 74.14  E-value: 2.47e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654945   88 GKHrlHVDTGMEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTY-DGSGVVTVETDHPL 155
Cdd:smart00983   1 GKH--EILKLPDGKYCSLIPLGDVA-GLTTKGLKYPLENADLSFGSSLSTSNEFiGEPVTVSVESGKLL 66
 
Name Accession Description Interval E-value
PLN02714 PLN02714
thiamin pyrophosphokinase
 6-161 1.71e-48

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 156.33  E-value: 1.71e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   6 RGCELIS-TPDQDHTDFTKCLKMLQKKIEEKDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHITpfpIIIIQEESLIYL 84
Cdd:PLN02714   76 LGTKIVDeSHDQDTTDLHKCIAYIRDSTPDLDKSNLCILVLGALGGRFDHEAGNINVLYRFPDLR---IVLLSDDCLIRL 152

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654945  85 L-QPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDgSGVVTVETDHPLLWTMAI 161
Cdd:PLN02714  153 LpATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIVK-EDKVTVESDSDLLWTISI 229
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 2-159 1.19e-40

Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin pyrophosphokinase) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamine) to form the coenzyme thiamine pyrophosphate (TPP). TPP is required for central metabolic functions, and thiamine deficiency is associated with potentially fatal human diseases. The structure of thiamine pyrophosphokinase suggests that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 153431 [Multi-domain]  Cd Length: 208  Bit Score: 135.75  E-value: 1.19e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   2 RLAERGCELISTPD-QDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATHITPfPIIIIQEES 80
Cdd:cd07995    59 YYKSKGVEIIHFPDeKDFTDFEKALKLALER------GADEIVILGATGGRLDHTLANLNLLLKYAKDGI-KIVLIDEQN 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945  81 LIYLLQPGKHRLHVDTgmEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTYDG-SGVVTVETDhPLLWTM 159
Cdd:cd07995   132 EIFLLLPGSHTLELEE--EGKYVSLIPLGEVT-GLTLKGLKYPLDNATLSFGSSLGTSNEFTGeKATVSVESG-LLLVIL 207
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 14-159 2.15e-32

thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly eukaryotic thiamine pyrophosphokinase. However, it is now expanded to include also homologous enzymes, apparently functionally equivalent, from species that rely on thiamine pyrophosphokinase rather than thiamine-monophosphate kinase (TIGR01379) to produce the active TPP cofactor. This includes the thiamine pyrophosphokinase from Bacillus subtilis, previously designated YloS. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 273588 [Multi-domain]  Cd Length: 205  Bit Score: 114.30  E-value: 2.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945  14 PDQDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATHiTPFPIIIIQEESLIYLLQPGKHrlH 93
Cdd:TIGR01378  70 PEKDTTDLELALKYALER------GADEITILGATGGRLDHTLANLNLLLEYAK-RGIEVRLIDEQNVIRLLLPGKY--Q 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654945  94 VDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLLWTM 159
Cdd:TIGR01378 141 IFKEPKGTYISLLPFGGDVHGLTTKGLKYPLNNADLKFGGTRGISNEFIGN-KATVSVDSGILLVI 205
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 2-151 1.80e-25

Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 441172 [Multi-domain]  Cd Length: 209  Bit Score: 96.40  E-value: 1.80e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654945   2 RLAERGCELIS-TPDQDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATHItPFPIIIIQEES 80
Cdd:COG1564    61 QYKEKGVEIIIfPPEKDETDTELALRYALER------GADEILILGATGGRLDHTLANLSLLARYAEK-GIRIVLIDENN 133

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654945  81 LIYLLQPGKHRLHvdtGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSN-TYDGSGVVTVET 151
Cdd:COG1564   134 EIFLLPPGSLTLE---GPPGTYVSLIPLSDPVTGLTLEGLKYPLDNATLTFGSSLGISNeAIGDEATISVES 202
TPK_B1_binding pfam04265
Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC: ...
 89-156 1.22e-19

Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 461244 [Multi-domain]  Cd Length: 66  Bit Score: 77.49  E-value: 1.22e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654945  89 KHRLHVDTGMeGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLL 156
Cdd:pfam04265   1 EHTIKKEEGF-GKYCSLIPLGGPVTGLTLKGLKYPLTNATLSFGGSLSTSNEFVEE-EATISFDSGIL 66
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 88-155 2.47e-18

Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 214953 [Multi-domain]  Cd Length: 66  Bit Score: 74.14  E-value: 2.47e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654945   88 GKHrlHVDTGMEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTY-DGSGVVTVETDHPL 155
Cdd:smart00983   1 GKH--EILKLPDGKYCSLIPLGDVA-GLTTKGLKYPLENADLSFGSSLSTSNEFiGEPVTVSVESGKLL 66
TPK_catalytic pfam04263
Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). ...
 2-67 2.13e-17

Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). Thiamin pyrophosphokinase (TPK) catalyzes the transfer of a pyrophosphate group from ATP to vitamin B1 (thiamin) to form the coenzyme thiamin pyrophosphate (TPP). Thus, TPK is important for the formation of a coenzyme required for central metabolic functions. The structure of thiamin pyrophosphokinase suggest that the enzyme may operate by a mechanism of pyrophosphoryl transfer similar to those described for pyrophosphokinases functioning in nucleotide biosynthesis.


Pssm-ID: 461242  Cd Length: 112  Bit Score: 72.92  E-value: 2.13e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654945   2 RLAERGCELISTP-DQDHTDFTKCLKMLQKKieekdlKVDVIVTLGGLAGRFDQIMASVNTLFQATH 67
Cdd:pfam04263  45 YYKSKGVEIIKTPaDQDTTDLEKAIELALEK------GVDEIVVLGALGGRFDHTLANINLLYKLLK 105
 
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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