Sugar phosphatase supH (P75792)

Identification
Name:Sugar phosphatase supH
Synonyms:Not Available
Gene Name:supH
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of fructose-1-P most efficiently, but it remains uncertain if this is the real substrate in vivo
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:Not Available
KEGG Reactions:
1.0Sugar phosphate+1.0Thumb+1.0Thumb ↔ 1.0Sugar+1.0Thumb+1.0Sugar
1.0Sugar phosphate + 1.0Water + 1.0Sugar phosphate ↔ 1.0Sugar + 1.0Phosphate + 1.0Sugar
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0a sugar phosphate → 1.0a sugar+1.0Thumb
1.0Water + 1.0a sugar phosphate → 1.0a sugar + 1.0Phosphate
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Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Fructose 6-phosphate + 1.0Water → 1.0D-Fructose + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glycerol 3-phosphate + 1.0Water → 1.0Glycerol + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Mannose 6-phosphate → 1.0D-Mannose + 1.0Phosphate
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0D-Ribose-5-phosphate → 1.0Phosphate + 1.0Ribose
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1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glucose 6-phosphate + 1.0Water → 1.0D-Glucose + 1.0Phosphate
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1.0Sugar phosphate+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Sugar phosphate + 1.0Water → 1.0Sucrose + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00660D-FructoseMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB00169D-MannoseMetaboCard
ECMDB02033D-Ribose-5-phosphateMetaboCard
ECMDB00124Fructose 6-phosphateMetaboCard
ECMDB01401Glucose 6-phosphateMetaboCard
ECMDB00131GlycerolMetaboCard
ECMDB00126Glycerol 3-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01078Mannose 6-phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00283RiboseMetaboCard
ECMDB00258SucroseMetaboCard
ECMDB23867Sugar phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
Process
metabolic process
Gene Properties
Blattner:b0822
Gene OrientationCounterclockwise
Centisome Percentage:18.50
Left Sequence End858436
Right Sequence End859251
Gene Sequence:
>816 bp
ATGCAGTATTGGGGAAAAATCATTGGCGTGGCCGTGGCCTTACTGATGGGCGGCGGCTTT
TGGGGCGTAGTGTTAGGCCTGTTAATTGGCCATATGTTTGATAAAGCCCGTAGCCGTAAA
ATGGCGTGGTTCGCCAACCAGCGTGAGCGTCAGGCGCTGTTTTTTGCCACCACTTTTGAA
GTGATGGGGCATTTAACCAAATCCAAAGGTCGCGTCACGGAGGCTGATATTCATATCGCC
AGCCAGTTGATGGACCGAATGAATCTTCATGGCGCTTCCCGTACTGCGGCGCAAAATGCG
TTCCGGGTGGGAAAATCAGACAATTACCCGCTGCGCGAAAAGATGCGCCAGTTTCGCAGT
GTCTGCTTTGGTCGTTTTGACTTAATTCGTATGTTTCTGGAGATCCAGATTCAGGCGGCG
TTTGCTGATGGTTCACTGCACCCGAATGAACGGGCGGTGCTGTATGTCATTGCAGAAGAA
TTAGGGATCTCCCGCGCTCAGTTTGACCAGTTTTTGCGCATGATGCAGGGCGGTGCACAG
TTTGGCGGCGGTTATCAGCAGCAAACTGGCGGTGGTAACTGGCAGCAAGCGCAGCGTGGC
CCAACGCTGGAAGATGCCTGTAATGTGCTGGGCGTGAAGCCGACGGATGATGCGACCACC
ATCAAACGTGCCTACCGTAAGCTGATGAGTGAACACCATCCCGATAAGCTGGTGGCGAAA
GGTTTGCCGCCTGAGATGATGGAGATGGCGAAGCAGAAAGCGCAGGAAATTCAGCAGGCA
TATGAGCTGATAAAGCAGCAGAAAGGGTTTAAATGA
Protein Properties
Pfam Domain Function:
Protein Residues:271
Protein Molecular Weight:30413
Protein Theoretical pI:6
PDB File:1RLT
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Sugar phosphatase supH
MSVKVIVTDMDGTFLNDAKTYNQPRFMAQYQELKKRGIKFVVASGNQYYQLISFFPELKD
EISFVAENGALVYEHGKQLFHGELTRHESRIVIGELLKDKQLNFVACGLQSAYVSENAPE
AFVALMAKHYHRLKPVKDYQEIDDVLFKFSLNLPDEQIPLVIDKLHVALDGIMKPVTSGF
GFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIK
QIARYATDDNNHEGALNVIQAVLDNTSPFNS
References
External Links:
ResourceLink
Uniprot ID:P75792
Uniprot Name:SUPH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321936
PDB ID:1RLT
Ecogene ID:EG13327
Ecocyc:EG13327
ColiBase:b0822
Kegg Gene:b0822
EchoBASE ID:EB3111
CCDB:SUPH_ECOLI
BacMap:16128790
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
  • 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
  • Kuznetsova, E., Proudfoot, M., Sanders, S. A., Reinking, J., Savchenko, A., Arrowsmith, C. H., Edwards, A. M., Yakunin, A. F. (2005). "Enzyme genomics: Application of general enzymatic screens to discover new enzymes." FEMS Microbiol Rev 29:263-279. Pubmed: 15808744
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Roberts, A., Lee, S. Y., McCullagh, E., Silversmith, R. E., Wemmer, D. E. (2005). "YbiV from Escherichia coli K12 is a HAD phosphatase." Proteins 58:790-801. Pubmed: 15657928