Trehalose-6-phosphate hydrolase (P28904)

Identification
Name:Trehalose-6-phosphate hydrolase
Synonyms:
  • Alpha,alpha-phosphotrehalase
Gene Name:treC
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Alpha,alpha-trehalose 6-phosphate + H(2)O = D- glucose + D-glucose 6-phosphate
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Trehalose 6-phosphate + 1.0Water ↔ 1.0D-Glucose + 1.0Glucose 6-phosphate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0β-D-glucose 6-phosphate+1.0Beta-D-Glucopyranuronic acid
1.0alpha,alpha-Trehalose 6-phosphate + 1.0Water → 1.0β-D-glucose 6-phosphate + 1.0Beta-D-Glucopyranuronic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Trehalose 6-phosphate + 1.0Water → 1.0Glucose 6-phosphate + 1.0b-D-Glucose
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Trehalose 6-phosphate → 1.0Glucose 6-phosphate + 1.0D-Glucose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB04010alpha,alpha-Trehalose 6-phosphateMetaboCard
ECMDB00516b-D-GlucoseMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB01401Glucose 6-phosphateMetaboCard
ECMDB01124Trehalose 6-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
alpha,alpha-phosphotrehalase activity
binding
catalytic activity
cation binding
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
ion binding
trehalase activity
Process
carbohydrate metabolic process
disaccharide metabolic process
metabolic process
oligosaccharide metabolic process
primary metabolic process
trehalose catabolic process
trehalose metabolic process
Gene Properties
Blattner:b4239
Gene OrientationCounterclockwise
Centisome Percentage:96.15
Left Sequence End4461077
Right Sequence End4462732
Gene Sequence:
>1656 bp
ATGGAATTTTCGTTTTCACCCAAACGTCTTGTTGTTGCTGTCGCCGCCGCTCTTCCTCTC
ATGGCCAGCGCAGCAGATACCCCGTCAACTGCCACCGCACGCAAAGGCTTTGCCGGATAC
GATCACCCAAACCAGTATCTGGTTAAACCGGCGACCACTATTGCCGACAATATGATGCCA
GTAATGCAGCATCCGGCGCAGGATAAAGAAACCCAGCAGAAGCTGGCAGAACTTGAGAAA
AAAACCGGTAAGAAACCGAATGTGGTTGTTTTCTTGCTGGACGATGTGGGCTGGATGGAC
GTCGGTTTTAACGGTGGCGGCGTGGCGGTGGGTAACCCTACACCAGATATCGACGCCGTT
GCCAGCCAGGGGCTGATTTTAACTTCGGCGTATTCTCAACCAAGCTCTTCCCCAACCCGC
GCCACCATTCTCACCGGACAATACTCCATCCACCACGGCATTCTGATGCCGCCAATGTAC
GGGCAACCGGGCGGGCTGCAAGGGTTAACCACGCTGCCGCAGTTGCTGCACGATCAGGGC
TACGTCACTCAGGCCATCGGAAAATGGCATATGGGGGAAAACAAAGAGTCGCAGCCGCAG
AACGTTGGCTTTGATGATTTCCGTGGCTTTAACTCGGTGTCTGATATGTACACCGAATGG
CGCGACGTTCACGTCAATCCGGAAGTGGCCCTGAGTCCGGACCGTTCTGAATACATCAAG
CAATTACCGTTCAGCAAAGATGACGTTCATGCGGTGCGCGGCGGCGAACAACAGGCCATT
GCCGACATTACGCCGAAATATATGGAAGATCTGGATCAACGCTGGATGGACTATGGCGTT
AAGTTCCTCGACAAGATGGCGAAGAGCGATAAACCATTCTTCCTCTACTACGGCACTCGT
GGCTGCCACTTCGATAACTACCCAAATGCGAAATATGCGGGTAGCTCTCCGGCACGCACC
TCGTATGGCGACTGCATGGTGGAGATGAACGATGTGTTCGCTAATCTGTATAAAACACTG
GAGAAAAACGGTCAGCTTGATAACACGCTGATCGTCTTTACCTCCGATAACGGACCGGAA
GCCGAAGTACCGCCGCACGGACGCACCCCGTTCCGTGGTGCGAAAGGTTCGACCTGGGAA
GGCGGCGTTCGCGTACCGACTTTCGTTTACTGGAAAGGGATGATCCAACCGCGTAAATCT
GACGGTATTGTCGATCTGGCAGATCTCTTCCCTACCGCGCTGGATCTGGCAGGGCATCCT
GGAGCGAAAGTGGCGAATTTAGTGCCGAAAACCACCTTTATCGATGGTGTGGACCAGACA
TCCTTCTTCCTGGGAACAAATGGTCAGTCTAACCGTAAGGCCGAGCACTACTTCCTCAAC
GGTAAACTCGCTGCTGTGCGTATGGATGAGTTCAAGTATCACGTCCTGATTCAGCAACCT
TACGCTTATACCCAGAGCGGATATCAGGGTGGATTCACCGGCACAGTAATGCAAACGGCG
GGATCGTCGGTGTTTAACCTCTACACCGATCCGCAGGAAAGCGACTCCATCGGCGTGCGC
CATATTCCGATGGGTGTACCGCTACAGACCGAAATGCACGCGTATATGGAGATCCTGAAA
AAATATCCACCACGCGCGCAGATTAAATCTGACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:551
Protein Molecular Weight:63837
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Trehalose-6-phosphate hydrolase
MTHLPHWWQNGVIYQIYPKSFQDTTGSGTGDLRGVIQHLDYLHKLGVDAIWLTPFYVSPQ
VDNGYDVANYTAIDPTYGTLDDFDELVTQAKSRGIRIILDMVFNHTSTQHAWFREALNKE
SPYRQFYIWRDGEPETPPNNWRSKFGGSAWRWHAESEQYYLHLFAPEQADLNWENPAVRA
ELKKVCEFWADRGVDGLRLDVVNLISKDPRFPEDLDGDGRRFYTDGPRAHEFLHEMNRDV
FTPRGLMTVGEMSSTSLEHCQRYAALTGSELSMTFNFHHLKVDYPGGEKWTLAKPDFVAL
KTLFRHWQQGMHNVAWNALFWCNHDQPRIVSRFGDEGEYRVPAAKMLAMVLHGMQGTPYI
YQGEEIGMTNPHFTRITDYRDVESLNMFAELRNDGRDADELLAILASKSRDNSRTPMQWS
NGDNAGFTAGEPWIGLGDNYQQINVEAALADDSSVFYTYQKLIALRKQEAILTWGNYQDL
LPNSPVLWCYRREWKGQTLLVIANLSREIQPWQAGQMRGNWQLVMHNYEEASPQPCAMNL
RPFEAVWWLQK
References
External Links:
ResourceLink
Uniprot ID:P28904
Uniprot Name:TREC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676250
Ecogene ID:EG11402
Ecocyc:EG11402
ColiBase:b4239
Kegg Gene:b4239
EchoBASE ID:EB1374
CCDB:TREC_ECOLI
BacMap:16132061
General Reference:
  • 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
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • 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
  • Rimmele, M., Boos, W. (1994). "Trehalose-6-phosphate hydrolase of Escherichia coli." J Bacteriol 176:5654-5664. Pubmed: 8083158
  • Sun, X., Harder, J., Krook, M., Jornvall, H., Sjoberg, B. M., Reichard, P. (1993). "A possible glycine radical in anaerobic ribonucleotide reductase from Escherichia coli: nucleotide sequence of the cloned nrdD gene." Proc Natl Acad Sci U S A 90:577-581. Pubmed: 8421692