Thiamine-phosphate pyrophosphorylase (P30137)

Identification
Name:Thiamine-phosphate pyrophosphorylase
Synonyms:
  • TMP pyrophosphorylase
  • TMP-PPase
  • Thiamine-phosphate synthase
Gene Name:thiE
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP)
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 1.04-Methyl-5-(2-phosphoethyl)-thiazole + 1.0Hydrogen ion ↔ 1.0Pyrophosphate + 1.0Thiamine monophosphate
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1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 1.04-Methyl-5-(2-phosphoethyl)-thiazole ↔ 1.0Pyrophosphate + 1.0Thiamine monophosphate
ReactionCard
SMPDB Reactions:
1.04-amino-2-methyl-5-diphosphomethylpyrimidine+1.0Thumb+2.0Thumb+1.0Thumb → 1.0Thiamine monophosphate+1.0Thumb+1.0diphosphate+1.0Thumb+1.0Thumb
1.04-amino-2-methyl-5-diphosphomethylpyrimidine + 1.02-((2R,5Z)-2-Carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate + 2.0Hydrogen ion + 1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate → 1.0Thiamine monophosphate + 1.0Carbon dioxide + 1.0diphosphate + 1.0Thiamine monophosphate + 1.0Pyrophosphate
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1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Pyrophosphate+1.0Thumb
1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 1.02-((2R,5Z)-2-Carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate + 1.0Hydrogen ion → 1.0Carbon dioxide + 1.0Pyrophosphate + 1.0Thiamine monophosphate
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EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 1.04-Methyl-5-(2-phosphoethyl)-thiazole + 1.0Hydrogen ion ↔ 1.0Pyrophosphate + 1.0Thiamine monophosphate
ReactionCard
1.02-[(2R,5Z)-(2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.02-[(2R,5Z)-(2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + 1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 1.0Hydrogen ion → 1.0Thiamine monophosphate + 1.0Carbon dioxide + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Hydrogen ion + 1.04-Methyl-5-(2-phosphoethyl)-thiazole + 1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate → 1.0Thiamine monophosphate + 1.0Pyrophosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 1.04-Methyl-5-(2-phosphoethyl)-thiazole → 1.0Pyrophosphate + 1.0Thiamine monophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB230532-((2R,5Z)-2-Carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphateMetaboCard
ECMDB200462-Methyl-4-amino-5-hydroxymethylpyrimidine diphosphateMetaboCard
ECMDB200944-Methyl-5-(2-phosphoethyl)-thiazoleMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
ECMDB02666Thiamine monophosphateMetaboCard
GO Classification:
Function
catalytic activity
thiamin-phosphate diphosphorylase activity
transferase activity
transferase activity, transferring alkyl or aryl (other than methyl) groups
Process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
thiamin and derivative metabolic process
thiamin biosynthetic process
thiamin metabolic process
Gene Properties
Blattner:b3993
Gene OrientationCounterclockwise
Centisome Percentage:90.34
Left Sequence End4191592
Right Sequence End4192227
Gene Sequence:
>636 bp
ATGAATAAAGCAAAACGCCTGGAGATCCTCACTCGCCTGCGTGAGAACAATCCTCATCCC
ACCACCGAGCTTAATTTCAGTTCGCCTTTTGAATTGCTGATTGCCGTACTGCTTTCCGCT
CAGGCGACCGATGTCAGTGTTAATAAGGCGACGGCGAAACTCTACCCGGTGGCGAATACG
CCTGCAGCGATGCTTGAACTGGGCGTTGAAGGGGTGAAAACCTATATCAAAACGATTGGG
CTTTATAACAGCAAAGCAGAAAATATCATCAAAACCTGCCGTATCTTGCTGGAGCAGCAT
AATGGCGAGGTTCCGGAAGATCGTGCTGCGCTTGAAGCCCTGCCCGGCGTAGGTCGTAAA
ACAGCCAACGTCGTATTAAACACTGCATTCGGCTGGCCGACTATTGCTGTCGACACGCAC
ATTTTCCGCGTTTGTAATCGTACTCAATTTGCGCCGGGGAAAAACGTCGAACAGGTAGAA
GAAAAGCTACTGAAAGTGGTTCCAGCAGAGTTTAAAGTCGACTGCCACCATTGGTTGATC
CTGCACGGGCGTTATACCTGCATTGCCCGCAAGCCCCGCTGTGGCTCTTGTATTATTGAA
GATCTTTGTGAATACAAAGAGAAAGTTGACATCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:211
Protein Molecular Weight:23015
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Thiamine-phosphate pyrophosphorylase
MYQPDFPPVPFRSGLYPVVDSVQWIERLLDAGVRTLQLRIKDRRDEEVEADVVAAIALGR
RYNARLFINDYWRLAIKHQAYGVHLGQEDLQATDLNAIRAAGLRLGVSTHDDMEIDVALA
ARPSYIALGHVFPTQTKQMPSAPQGLEQLARHVERLADYPTVAIGGISLARAPAVIATGV
GSIAVVSAITQAADWRLATAQLLEIAGVGDE
References
External Links:
ResourceLink
Uniprot ID:P30137
Uniprot Name:THIE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:1742691
Ecogene ID:EG11586
Ecocyc:EG11586
ColiBase:b3993
Kegg Gene:b3993
EchoBASE ID:EB1545
CCDB:THIE_ECOLI
BacMap:16131823
General Reference:
  • Blattner, F. R., Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L. (1993). "Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Nucleic Acids Res 21:5408-5417. Pubmed: 8265357
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kelleher, N. L., Taylor, S. V., Grannis, D., Kinsland, C., Chiu, H. J., Begley, T. P., McLafferty, F. W. (1998). "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry." Protein Sci 7:1796-1801. Pubmed: 10082377
  • Vander Horn, P. B., Backstrom, A. D., Stewart, V., Begley, T. P. (1993). "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12." J Bacteriol 175:982-992. Pubmed: 8432721