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Conserved domains on  [gi|1933719646|gb|QPE96818|]
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norphogenetic protein (plasmid) [Escherichia coli O152:H23]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TPK super family cl21552
Thiamine pyrophosphokinase; Thiamine pyrophosphokinase (TPK, EC:2.7.6.2, also spelled thiamin ...
 4-59 8.94e-03

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.


The actual alignment was detected with superfamily member pfam01973:

Pssm-ID: 473909  Cd Length: 171  Bit Score: 35.68  E-value: 8.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933719646   4 KNKFRGSDRVIIVGSGPS-----------AANFVaprgvpIIAVNGAIDWLNRA----SYFFTLDPSPDNM 59
Cdd:pfam01973  19 LNKFKGNKPAIIVGAGPSldknlpllkenRDKAV------IIAADRALKALLKEgikpDIVVSLDPQEASY 83
 
Name Accession Description Interval E-value
MptE-like pfam01973
6-hydroxymethylpterin diphosphokinase MptE-like; This domain can be found in a group of ...
 4-59 8.94e-03

6-hydroxymethylpterin diphosphokinase MptE-like; This domain can be found in a group of proteins, including archaeal 6-hydroxymethylpterin diphosphokinase (6-HMDPK), known as MptE, which catalyzes the formation of 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP) from 6-HMD and ATP. 6-HMDP is the precursor of the pterin containing moiety of the essential C1-carriers tetrahydrofolate and tetrahydromethanopterin. This entry also includes a number of uncharacterized proteins from bacteria.


Pssm-ID: 426539  Cd Length: 171  Bit Score: 35.68  E-value: 8.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933719646   4 KNKFRGSDRVIIVGSGPS-----------AANFVaprgvpIIAVNGAIDWLNRA----SYFFTLDPSPDNM 59
Cdd:pfam01973  19 LNKFKGNKPAIIVGAGPSldknlpllkenRDKAV------IIAADRALKALLKEgikpDIVVSLDPQEASY 83
 
Name Accession Description Interval E-value
MptE-like pfam01973
6-hydroxymethylpterin diphosphokinase MptE-like; This domain can be found in a group of ...
 4-59 8.94e-03

6-hydroxymethylpterin diphosphokinase MptE-like; This domain can be found in a group of proteins, including archaeal 6-hydroxymethylpterin diphosphokinase (6-HMDPK), known as MptE, which catalyzes the formation of 6-hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP) from 6-HMD and ATP. 6-HMDP is the precursor of the pterin containing moiety of the essential C1-carriers tetrahydrofolate and tetrahydromethanopterin. This entry also includes a number of uncharacterized proteins from bacteria.


Pssm-ID: 426539  Cd Length: 171  Bit Score: 35.68  E-value: 8.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1933719646   4 KNKFRGSDRVIIVGSGPS-----------AANFVaprgvpIIAVNGAIDWLNRA----SYFFTLDPSPDNM 59
Cdd:pfam01973  19 LNKFKGNKPAIIVGAGPSldknlpllkenRDKAV------IIAADRALKALLKEgikpDIVVSLDPQEASY 83
 
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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