NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767947427|ref|XP_011514350|]
View 

thiamin pyrophosphokinase 1 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PLN02714 super family cl29325
thiamin pyrophosphokinase
 16-135 7.90e-43

thiamin pyrophosphokinase


The actual alignment was detected with superfamily member PLN02714:

Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 140.92  E-value: 7.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427  16 IVTLGGLAGRFDQIMASVNTLFQATHITpfpIIIIQEESLIYLL-QPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGL 94
Cdd:PLN02714 113 ILVLGALGGRFDHEAGNINVLYRFPDLR---IVLLSDDCLIRLLpATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGL 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767947427  95 KWNLTNDVLAFGTLVSTSNTYDgSGVVTVETDHPLLWTMAI 135
Cdd:PLN02714 190 QWNLDNTEMRFGGLISTSNIVK-EDKVTVESDSDLLWTISI 229
 
Name Accession Description Interval E-value
PLN02714 PLN02714
thiamin pyrophosphokinase
 16-135 7.90e-43

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 140.92  E-value: 7.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427  16 IVTLGGLAGRFDQIMASVNTLFQATHITpfpIIIIQEESLIYLL-QPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGL 94
Cdd:PLN02714 113 ILVLGALGGRFDHEAGNINVLYRFPDLR---IVLLSDDCLIRLLpATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGL 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767947427  95 KWNLTNDVLAFGTLVSTSNTYDgSGVVTVETDHPLLWTMAI 135
Cdd:PLN02714 190 QWNLDNTEMRFGGLISTSNIVK-EDKVTVESDSDLLWTISI 229
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 9-133 3.59e-32

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: 112.64  E-value: 3.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427   9 KDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHITPfPIIIIQEESLIYLLQPGKHRLHVDTgmEGDWCGLIPVGQPCmQ 88
Cdd:cd07995   87 LERGADEIVILGATGGRLDHTLANLNLLLKYAKDGI-KIVLIDEQNEIFLLLPGSHTLELEE--EGKYVSLIPLGEVT-G 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767947427  89 VTTTGLKWNLTNDVLAFGTLVSTSNTYDG-SGVVTVETDhPLLWTM 133
Cdd:cd07995  163 LTLKGLKYPLDNATLSFGSSLGTSNEFTGeKATVSVESG-LLLVIL 207
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 14-133 3.61e-25

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: 94.66  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427   14 DVIVTLGGLAGRFDQIMASVNTLFQATHiTPFPIIIIQEESLIYLLQPGKHrlHVDTGMEGDWCGLIPVGQPCMQVTTTG 93
Cdd:TIGR01378  90 DEITILGATGGRLDHTLANLNLLLEYAK-RGIEVRLIDEQNVIRLLLPGKY--QIFKEPKGTYISLLPFGGDVHGLTTKG 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767947427   94 LKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLLWTM 133
Cdd:TIGR01378 167 LKYPLNNADLKFGGTRGISNEFIGN-KATVSVDSGILLVI 205
TPK_B1_binding pfam04265
Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC: ...
 63-130 1.20e-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: 76.72  E-value: 1.20e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767947427   63 KHRLHVDTGMeGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLL 130
Cdd:pfam04265   1 EHTIKKEEGF-GKYCSLIPLGGPVTGLTLKGLKYPLTNATLSFGGSLSTSNEFVEE-EATISFDSGIL 66
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 9-125 9.06e-19

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: 78.30  E-value: 9.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427   9 KDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHItPFPIIIIQEESLIYLLQPGKHRLHvdtGMEGDWCGLIPVGQPCMQ 88
Cdd:COG1564   89 LERGADEILILGATGGRLDHTLANLSLLARYAEK-GIRIVLIDENNEIFLLPPGSLTLE---GPPGTYVSLIPLSDPVTG 164

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767947427  89 VTTTGLKWNLTNDVLAFGTLVSTSN-TYDGSGVVTVET 125
Cdd:COG1564  165 LTLEGLKYPLDNATLTFGSSLGISNeAIGDEATISVES 202
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 62-129 4.35e-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: 72.60  E-value: 4.35e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767947427    62 GKHrlHVDTGMEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTY-DGSGVVTVETDHPL 129
Cdd:smart00983   1 GKH--EILKLPDGKYCSLIPLGDVA-GLTTKGLKYPLENADLSFGSSLSTSNEFiGEPVTVSVESGKLL 66
 
Name Accession Description Interval E-value
PLN02714 PLN02714
thiamin pyrophosphokinase
 16-135 7.90e-43

thiamin pyrophosphokinase


Pssm-ID: 178316 [Multi-domain]  Cd Length: 229  Bit Score: 140.92  E-value: 7.90e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427  16 IVTLGGLAGRFDQIMASVNTLFQATHITpfpIIIIQEESLIYLL-QPGKHRLHVDTGMEGDWCGLIPVGQPCMQVTTTGL 94
Cdd:PLN02714 113 ILVLGALGGRFDHEAGNINVLYRFPDLR---IVLLSDDCLIRLLpATHRHEIHIDSSVEGPHCGLIPIGGPSASTTTTGL 189

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 767947427  95 KWNLTNDVLAFGTLVSTSNTYDgSGVVTVETDHPLLWTMAI 135
Cdd:PLN02714 190 QWNLDNTEMRFGGLISTSNIVK-EDKVTVESDSDLLWTISI 229
TPK cd07995
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 9-133 3.59e-32

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: 112.64  E-value: 3.59e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427   9 KDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHITPfPIIIIQEESLIYLLQPGKHRLHVDTgmEGDWCGLIPVGQPCmQ 88
Cdd:cd07995   87 LERGADEIVILGATGGRLDHTLANLNLLLKYAKDGI-KIVLIDEQNEIFLLLPGSHTLELEE--EGKYVSLIPLGEVT-G 162

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767947427  89 VTTTGLKWNLTNDVLAFGTLVSTSNTYDG-SGVVTVETDhPLLWTM 133
Cdd:cd07995  163 LTLKGLKYPLDNATLSFGSSLGTSNEFTGeKATVSVESG-LLLVIL 207
thi_PPkinase TIGR01378
thiamine pyrophosphokinase; This model has been revised. Originally, it described strictly ...
 14-133 3.61e-25

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: 94.66  E-value: 3.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427   14 DVIVTLGGLAGRFDQIMASVNTLFQATHiTPFPIIIIQEESLIYLLQPGKHrlHVDTGMEGDWCGLIPVGQPCMQVTTTG 93
Cdd:TIGR01378  90 DEITILGATGGRLDHTLANLNLLLEYAK-RGIEVRLIDEQNVIRLLLPGKY--QIFKEPKGTYISLLPFGGDVHGLTTKG 166

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767947427   94 LKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLLWTM 133
Cdd:TIGR01378 167 LKYPLNNADLKFGGTRGISNEFIGN-KATVSVDSGILLVI 205
TPK_B1_binding pfam04265
Thiamin pyrophosphokinase, vitamin B1 binding domain; Family of thiamin pyrophosphokinase (EC: ...
 63-130 1.20e-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: 76.72  E-value: 1.20e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767947427   63 KHRLHVDTGMeGDWCGLIPVGQPCMQVTTTGLKWNLTNDVLAFGTLVSTSNTYDGSgVVTVETDHPLL 130
Cdd:pfam04265   1 EHTIKKEEGF-GKYCSLIPLGGPVTGLTLKGLKYPLTNATLSFGGSLSTSNEFVEE-EATISFDSGIL 66
ThiN COG1564
Thiamine pyrophosphokinase [Coenzyme transport and metabolism]; Thiamine pyrophosphokinase is ...
 9-125 9.06e-19

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: 78.30  E-value: 9.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767947427   9 KDLKVDVIVTLGGLAGRFDQIMASVNTLFQATHItPFPIIIIQEESLIYLLQPGKHRLHvdtGMEGDWCGLIPVGQPCMQ 88
Cdd:COG1564   89 LERGADEILILGATGGRLDHTLANLSLLARYAEK-GIRIVLIDENNEIFLLPPGSLTLE---GPPGTYVSLIPLSDPVTG 164

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 767947427  89 VTTTGLKWNLTNDVLAFGTLVSTSN-TYDGSGVVTVET 125
Cdd:COG1564  165 LTLEGLKYPLDNATLTFGSSLGISNeAIGDEATISVES 202
TPK_B1_binding smart00983
Thiamin pyrophosphokinase, vitamin B1 binding domain; Thiamin pyrophosphokinase (TPK) ...
 62-129 4.35e-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: 72.60  E-value: 4.35e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767947427    62 GKHrlHVDTGMEGDWCGLIPVGQPCmQVTTTGLKWNLTNDVLAFGTLVSTSNTY-DGSGVVTVETDHPL 129
Cdd:smart00983   1 GKH--EILKLPDGKYCSLIPLGDVA-GLTTKGLKYPLENADLSFGSSLSTSNEFiGEPVTVSVESGKLL 66
TPK_catalytic pfam04263
Thiamin pyrophosphokinase, catalytic domain; Family of thiamin pyrophosphokinase (EC:2.7.6.2). ...
 2-41 1.42e-07

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: 46.73  E-value: 1.42e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 767947427    2 LQKKIEE-KDLKVDVIVTLGGLAGRFDQIMASVNTLFQATH 41
Cdd:pfam04263  65 LEKAIELaLEKGVDEIVVLGALGGRFDHTLANINLLYKLLK 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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH