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Conserved domains on  [gi|2462613686|ref|XP_054213869|]
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thiamine pyrophosphokinase 1 isoform X3 [Homo sapiens]

Protein Classification

thiamin pyrophosphokinase( domain architecture ID 1006276)

thiamine pyrophosphokinase (TPK) is an enzyme that converts thiamine into thiamine pyrophosphate (TPP), the active form of vitamin B1

CATH:  2.60.120.320|3.40.50.10240
EC:  2.7.6.2
Gene Ontology:  GO:0006772|GO:0004788|GO:0030975|GO:0005524
SCOP:  4003288|4003310

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02714 super family cl29325
thiamin pyrophosphokinase
 58-187 2.66e-42

thiamin pyrophosphokinase


The actual alignment was detected with superfamily member PLN02714:

Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 141.31  E-value: 2.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  58 FLPEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFTKCLKMLQKKIEEKD-----------LKGK---------- 115
Cdd:PLN02714   53 YKPDVIKGDMDSIRPEVLDFYSNLGTKIVDeSHDQDTTDLHKCIAYIRDSTPDLDksnlcilvlgaLGGRfdheagninv 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 116 --------------------------HRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDg 169
Cdd:PLN02714  133 lyrfpdlrivllsddclirllpathrHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIVK- 211

                         170
                  ....*....|....*...
gi 2462613686 170 SGVVTVETDHPLLWTMAI 187
Cdd:PLN02714  212 EDKVTVESDSDLLWTISI 229
 
Name Accession Description Interval E-value
PLN02714 PLN02714
thiamin pyrophosphokinase
 58-187 2.66e-42

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 141.31  E-value: 2.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  58 FLPEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFTKCLKMLQKKIEEKD-----------LKGK---------- 115
Cdd:PLN02714   53 YKPDVIKGDMDSIRPEVLDFYSNLGTKIVDeSHDQDTTDLHKCIAYIRDSTPDLDksnlcilvlgaLGGRfdheagninv 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 116 --------------------------HRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDg 169
Cdd:PLN02714  133 lyrfpdlrivllsddclirllpathrHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIVK- 211

                         170
                  ....*....|....*...
gi 2462613686 170 SGVVTVETDHPLLWTMAI 187
Cdd:PLN02714  212 EDKVTVESDSDLLWTISI 229
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 58-185 3.40e-34

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: 119.96  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  58 FLPEFINGDFDSIRPEVREYYATKGCELISTPD-QDHTDFTKCLKMLQKK------------------------------ 106
Cdd:cd07995    40 IVPDLIIGDFDSISPEVLEYYKSKGVEIIHFPDeKDFTDFEKALKLALERgadeivilgatggrldhtlanlnlllkyak 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 107 -------IEEKD-----LKGKHRLHVDTgmEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTYDG-SGVV 173
Cdd:cd07995   120 dgikivlIDEQNeifllLPGSHTLELEE--EGKYVSLIPLGEVT-GLTLKGLKYPLDNATLSFGSSLGTSNEFTGeKATV 196

                         170
                  ....*....|..
gi 2462613686 174 TVETDhPLLWTM 185
Cdd:cd07995   197 SVESG-LLLVIL 207
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 19-185 4.72e-26

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: 98.90  E-value: 4.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  19 NLKLSSRPPATSHLIRTPKDTHYCGASKGlGNSFIGNeSFLPEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFT 97
Cdd:TIGR01378   1 LILAGGGPDSELPLRLLKEHDLVIAADGG-ANHLLKL-GLTPDLIVGDFDSIDEEELDFYKETGVKIIVfPPEKDTTDLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  98 KCLKMLQKK-------------------------------------IEEKD-----LKGKHrlHVDTGMEGDWCGLIPVG 135
Cdd:TIGR01378  79 LALKYALERgadeitilgatggrldhtlanlnllleyakrgievrlIDEQNvirllLPGKY--QIFKEPKGTYISLLPFG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462613686 136 QPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLLWTM 185
Cdd:TIGR01378 157 GDVHGLTTKGLKYPLNNADLKFGGTRGISNEFIGN-KATVSVDSGILLVI 205
TPK_catalytic pfam04263
Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). ...
 55-110 1.28e-21

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: 84.86  E-value: 1.28e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613686  55 NESFLPEFINGDFDSIRPEVREYYATKGCELISTP-DQDHTDFTKCLKMLQKKIEEK 110
Cdd:pfam04263  23 RLGIKPDVIVGDFDSIRPEVREYYKSKGVEIIKTPaDQDTTDLEKAIELALEKGVDE 79
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 60-177 5.84e-20

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: 82.92  E-value: 5.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  60 PEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFTKCLKMLQKK-------------------------------- 106
Cdd:COG1564    44 PDLIIGDFDSISEEELEQYKEKGVEIIIfPPEKDETDTELALRYALERgadeililgatggrldhtlanlsllaryaekg 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 107 -----IEEKD-----LKGKHRLHvdtGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSN-TYDGSGVVTV 175
Cdd:COG1564   124 irivlIDENNeifllPPGSLTLE---GPPGTYVSLIPLSDPVTGLTLEGLKYPLDNATLTFGSSLGISNeAIGDEATISV 200


                  ..
gi 2462613686 176 ET 177
Cdd:COG1564   201 ES 202
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 114-181 8.35e-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: 73.37  E-value: 8.35e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613686  114 GKHrlHVDTGMEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTY-DGSGVVTVETDHPL 181
Cdd:smart00983   1 GKH--EILKLPDGKYCSLIPLGDVA-GLTTKGLKYPLENADLSFGSSLSTSNEFiGEPVTVSVESGKLL 66
 
Name Accession Description Interval E-value
PLN02714 PLN02714
thiamin pyrophosphokinase
 58-187 2.66e-42

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 141.31  E-value: 2.66e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  58 FLPEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFTKCLKMLQKKIEEKD-----------LKGK---------- 115
Cdd:PLN02714   53 YKPDVIKGDMDSIRPEVLDFYSNLGTKIVDeSHDQDTTDLHKCIAYIRDSTPDLDksnlcilvlgaLGGRfdheagninv 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 116 --------------------------HRLHVDTGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDg 169
Cdd:PLN02714  133 lyrfpdlrivllsddclirllpathrHEIHIDSSVEGPHCGLIPIGGPSASTTTTGLQWNLDNTEMRFGGLISTSNIVK- 211

                         170
                  ....*....|....*...
gi 2462613686 170 SGVVTVETDHPLLWTMAI 187
Cdd:PLN02714  212 EDKVTVESDSDLLWTISI 229
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 58-185 3.40e-34

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: 119.96  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  58 FLPEFINGDFDSIRPEVREYYATKGCELISTPD-QDHTDFTKCLKMLQKK------------------------------ 106
Cdd:cd07995    40 IVPDLIIGDFDSISPEVLEYYKSKGVEIIHFPDeKDFTDFEKALKLALERgadeivilgatggrldhtlanlnlllkyak 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 107 -------IEEKD-----LKGKHRLHVDTgmEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTYDG-SGVV 173
Cdd:cd07995   120 dgikivlIDEQNeifllLPGSHTLELEE--EGKYVSLIPLGEVT-GLTLKGLKYPLDNATLSFGSSLGTSNEFTGeKATV 196

                         170
                  ....*....|..
gi 2462613686 174 TVETDhPLLWTM 185
Cdd:cd07995   197 SVESG-LLLVIL 207
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 19-185 4.72e-26

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: 98.90  E-value: 4.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  19 NLKLSSRPPATSHLIRTPKDTHYCGASKGlGNSFIGNeSFLPEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFT 97
Cdd:TIGR01378   1 LILAGGGPDSELPLRLLKEHDLVIAADGG-ANHLLKL-GLTPDLIVGDFDSIDEEELDFYKETGVKIIVfPPEKDTTDLE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  98 KCLKMLQKK-------------------------------------IEEKD-----LKGKHrlHVDTGMEGDWCGLIPVG 135
Cdd:TIGR01378  79 LALKYALERgadeitilgatggrldhtlanlnllleyakrgievrlIDEQNvirllLPGKY--QIFKEPKGTYISLLPFG 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462613686 136 QPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLLWTM 185
Cdd:TIGR01378 157 GDVHGLTTKGLKYPLNNADLKFGGTRGISNEFIGN-KATVSVDSGILLVI 205
TPK_catalytic pfam04263
Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). ...
 55-110 1.28e-21

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: 84.86  E-value: 1.28e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2462613686  55 NESFLPEFINGDFDSIRPEVREYYATKGCELISTP-DQDHTDFTKCLKMLQKKIEEK 110
Cdd:pfam04263  23 RLGIKPDVIVGDFDSIRPEVREYYKSKGVEIIKTPaDQDTTDLEKAIELALEKGVDE 79
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 60-177 5.84e-20

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: 82.92  E-value: 5.84e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686  60 PEFINGDFDSIRPEVREYYATKGCELIS-TPDQDHTDFTKCLKMLQKK-------------------------------- 106
Cdd:COG1564    44 PDLIIGDFDSISEEELEQYKEKGVEIIIfPPEKDETDTELALRYALERgadeililgatggrldhtlanlsllaryaekg 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462613686 107 -----IEEKD-----LKGKHRLHvdtGMEGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSN-TYDGSGVVTV 175
Cdd:COG1564   124 irivlIDENNeifllPPGSLTLE---GPPGTYVSLIPLSDPVTGLTLEGLKYPLDNATLTFGSSLGISNeAIGDEATISV 200


                  ..
gi 2462613686 176 ET 177
Cdd:COG1564   201 ES 202
TPK_B1_binding pfam04265
Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC: ...
 115-182 2.33e-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: 2.33e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462613686 115 KHRLHVDTGMeGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLL 182
Cdd:pfam04265   1 EHTIKKEEGF-GKYCSLIPLGGPVTGLTLKGLKYPLTNATLSFGGSLSTSNEFVEE-EATISFDSGIL 66
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 114-181 8.35e-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: 73.37  E-value: 8.35e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462613686  114 GKHrlHVDTGMEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTY-DGSGVVTVETDHPL 181
Cdd:smart00983   1 GKH--EILKLPDGKYCSLIPLGDVA-GLTTKGLKYPLENADLSFGSSLSTSNEFiGEPVTVSVESGKLL 66
 
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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