Sugar phosphatase YbiV
Details
- Name
- Sugar phosphatase YbiV
- Synonyms
- 3.1.3.23
- supH
- Gene Name
- ybiV
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0011184|Sugar phosphatase YbiV MSVKVIVTDMDGTFLNDAKTYNQPRFMAQYQELKKRGIKFVVASGNQYYQLISFFPELKD EISFVAENGALVYEHGKQLFHGELTRHESRIVIGELLKDKQLNFVACGLQSAYVSENAPE AFVALMAKHYHRLKPVKDYQEIDDVLFKFSLNLPDEQIPLVIDKLHVALDGIMKPVTSGF GFIDLIIPGLHKANGISRLLKRWDLSPQNVVAIGDSGNDAEMLKMARYSFAMGNAAENIK QIARYATDDNNHEGALNVIQAVLDNTSPFNS
- Number of residues
- 271
- Molecular Weight
- 30412.59
- Theoretical pI
- 6.31
- GO Classification
- Functionsmagnesium ion binding / sugar-phosphatase activityProcessesdephosphorylation
- General Function
- Sugar-phosphatase activity
- Specific Function
- Catalyzes the hydrolysis of sugar phosphate to sugar and inorganic phosphate. Has a wide substrate specificity catalyzing the hydrolysis of ribose-5-phosphate, glucose-6-phosphate, fructose-1-phosphate, acetyl-phosphate, glycerol-1-phosphate, glycerol-2-phosphate, 2-deoxy-glucose-6-phosphate, mannose-6-phosphate and fructose-6-phosphate. Appears to have a low level of phosphotransferase activity using monophosphates as the phosphate donor.
- Pfam Domain Function
- Hydrolase_3 (PF08282)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0011185|Sugar phosphatase YbiV (ybiV) ATGAGCGTAAAAGTTATCGTCACAGACATGGACGGTACTTTTCTTAACGACGCCAAAACG TACAACCAACCACGTTTTATGGCGCAATATCAGGAACTGAAAAAGCGCGGCATTAAGTTC GTTGTTGCCAGCGGTAATCAGTATTACCAGCTTATTTCATTCTTTCCTGAGCTAAAGGAT GAGATCTCTTTTGTCGCGGAAAACGGCGCACTGGTTTACGAACATGGCAAGCAGTTGTTC CACGGCGAACTGACCCGACATGAATCGCGGATTGTTATTGGCGAGTTGCTAAAAGATAAG CAACTCAATTTTGTCGCCTGCGGTCTGCAAAGTGCATATGTCAGCGAAAATGCCCCCGAA GCATTTGTCGCACTGATGGCAAAACACTACCATCGCCTGAAACCTGTAAAAGATTATCAG GAGATTGACGACGTACTGTTCAAGTTTTCGCTCAACCTGCCGGATGAACAAATCCCGTTA GTGATCGACAAACTGCACGTAGCGCTCGATGGCATTATGAAACCCGTTACCAGTGGTTTT GGCTTTATCGACCTGATTATTCCCGGTCTACATAAAGCAAACGGTATTTCGCGGTTACTG AAACGCTGGGATCTGTCACCGCAAAATGTGGTAGCGATTGGCGACAGCGGTAACGATGCG GAGATGCTGAAAATGGCGCGTTATTCCTTTGCGATGGGCAATGCTGCGGAAAACATTAAA CAAATCGCCCGTTACGCTACCGATGATAATAATCATGAAGGCGCGCTGAATGTGATTCAG GCGGTGCTGGATAACACATCCCCTTTTAACAGCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P75792 UniProtKB Entry Name SUPH_ECOLI GenBank Protein ID 1787043 GenBank Gene ID U00096 - General References
- 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 al.: 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. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Kuznetsova E, Proudfoot M, Sanders SA, Reinking J, Savchenko A, Arrowsmith CH, Edwards AM, Yakunin AF: Enzyme genomics: Application of general enzymatic screens to discover new enzymes. FEMS Microbiol Rev. 2005 Apr;29(2):263-79. [Article]
- Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF: Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J Biol Chem. 2006 Nov 24;281(47):36149-61. Epub 2006 Sep 21. [Article]
- Roberts A, Lee SY, McCullagh E, Silversmith RE, Wemmer DE: YbiV from Escherichia coli K12 is a HAD phosphatase. Proteins. 2005 Mar 1;58(4):790-801. [Article]