Inositol-1-monophosphatase (P0ADG4)

Identification
Name:Inositol-1-monophosphatase
Synonyms:
  • I-1-Pase
  • IMPase
  • Inositol-1-phosphatase
Gene Name:suhB
Enzyme Class:
Biological Properties
General Function:Involved in phosphatidylinositol phosphorylation
Specific Function:Myo-inositol phosphate + H(2)O = myo-inositol + phosphate
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Myo-inositol 1-phosphate → 1.0Inositol + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Myo-inositol 1-phosphate + 1.0Water ↔ 1.0Inositol + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Myo-inositol 4-phosphate + 1.0Water ↔ 1.0Inositol + 1.0Phosphate
ReactionCard
1.0myo-Inositol phosphate+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0myo-Inositol phosphate + 1.0Water ↔ 1.0Inositol + 1.0Phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0D-Myo-inositol (1)-monophosphate → 1.0Phosphate + 1.0Inositol
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glycerol 2-phosphate + 1.0Water → 1.0Glycerol + 1.0Phosphate
ReactionCard
1.0Myo-inositol phosphate+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Myo-inositol phosphate + 1.0Water → 1.0Myoinositol + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20543D-Myo-inositol (1)-monophosphateMetaboCard
ECMDB01313D-Myo-inositol 4-phosphateMetaboCard
ECMDB00131GlycerolMetaboCard
ECMDB21222Glycerol 2-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00160InositolMetaboCard
ECMDB00213Myo-inositol 1-phosphateMetaboCard
ECMDB04087MyoinositolMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on ester bonds
inositol or phosphatidylinositol phosphatase activity
inositol-1(or 4)-monophosphatase activity
phosphatase activity
phosphoric ester hydrolase activity
Gene Properties
Blattner:b2533
Gene OrientationClockwise
Centisome Percentage:57.36
Left Sequence End2661464
Right Sequence End2662267
Gene Sequence:
>804 bp
ATGGCTATCCCTGCATTTGGTTTAGGTACTTTCCGTCTGAAAGACGACGTTGTTATTTCA
TCTGTGATAACGGCGCTTGAACTTGGTTATCGCGCAATTGATACCGCACAAATCTATGAT
AACGAAGCCGCAGTAGGTCAGGCGATTGCAGAAAGTGGCGTGCCACGTCATGAACTCTAC
ATCACCACTAAAATCTGGATTGAAAATCTCAGCAAAGACAAATTGATCCCAAGTCTGAAA
GAGAGCCTGCAAAAATTGCGTACCGATTATGTTGATCTGACGCTAATCCACTGGCCGTCA
CCAAACGATGAAGTCTCTGTTGAAGAGTTTATGCAGGCGCTGCTGGAAGCCAAAAAACAA
GGGCTGACGCGTGAGATCGGTATTTCCAACTTCACGATCCCGTTGATGGAAAAAGCGATT
GCTGCTGTTGGTGCTGAAAACATCGCTACTAACCAGATTGAACTCTCTCCTTATCTGCAA
AACCGTAAAGTGGTTGCCTGGGCTAAACAGCACGGCATCCATATTACTTCCTATATGACG
CTGGCGTATGGTAAGGCCCTGAAAGATGAGGTTATTGCTCGTATCGCAGCTAAACACAAT
GCGACTCCGGCACAAGTGATTCTGGCGTGGGCTATGGGGGAAGGTTACTCAGTAATTCCT
TCTTCTACTAAACGTAAAAACCTGGAAAGTAATCTTAAGGCACAAAATTTACAGCTTGAT
GCCGAAGATAAAAAAGCGATCGCCGCACTGGATTGCAACGACCGCCTGGTTAGCCCGGAA
GGTCTGGCTCCTGAATGGGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:267
Protein Molecular Weight:29172
Protein Theoretical pI:7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Inositol-1-monophosphatase
MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYP
QHTIITEESGELEGTDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPM
RNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQYATTYINIVGKLFNECA
DFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMLTG
NIVAGNPRVVKAMLANMRDELSDALKR
References
External Links:
ResourceLink
Uniprot ID:P0ADG4
Uniprot Name:SUHB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674382
Ecogene ID:EG10983
Ecocyc:EG10983
ColiBase:b2533
Kegg Gene:b2533
EchoBASE ID:EB0976
CCDB:SUHB_ECOLI
BacMap:16130458
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
  • Chen, L., Roberts, M. F. (2000). "Overexpression, purification, and analysis of complementation behavior of E. coli SuhB protein: comparison with bacterial and archaeal inositol monophosphatases." Biochemistry 39:4145-4153. Pubmed: 10747806
  • 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
  • Matsuhisa, A., Suzuki, N., Noda, T., Shiba, K. (1995). "Inositol monophosphatase activity from the Escherichia coli suhB gene product." J Bacteriol 177:200-205. Pubmed: 8002619
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Yano, R., Nagai, H., Shiba, K., Yura, T. (1990). "A mutation that enhances synthesis of sigma 32 and suppresses temperature-sensitive growth of the rpoH15 mutant of Escherichia coli." J Bacteriol 172:2124-2130. Pubmed: 2138605