Phosphatase ybhA (P21829)

Identification
Name:Phosphatase ybhA
Synonyms:Not Available
Gene Name:ybhA
Enzyme Class:Not Available
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Catalyzes the dephosphorylation of the artificial chromogenic substrate p-nitrophenyl phosphate (pNPP) and of the natural substrates pyridoxalphosphate and erythrose 4-phosphate
Cellular Location:Cytoplasmic
SMPDB Pathways:
  • Gluconeogenesis from L-malic acid PW000819
  • glycerol metabolism PW000914
  • glycerol metabolism II PW000915
  • glycerol metabolism III (sn-glycero-3-phosphoethanolamine) PW000916
  • glycerol metabolism IV (glycerophosphoglycerol) PW000917
  • glycerol metabolism V (glycerophosphoserine) PW000918
  • glycolysis and pyruvate dehydrogenase PW000785
KEGG Pathways:Not Available
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water ↔ 1.0Fructose 6-phosphate + 1.0Phosphate
ReactionCard
SMPDB Reactions:
1.0Fructose 6-phosphate+1.0Thumb+1.0Thumb → 1.0Fructose 1,6-bisphosphate+1.0Thumb+1.0Thumb
1.0Fructose 6-phosphate + 1.0Phosphate + 1.0Fructose 6-phosphate → 1.0Fructose 1,6-bisphosphate + 1.0Water + 1.0Fructose 1,6-bisphosphate
ReactionCard
1.0Fructose 1,6-bisphosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water + 1.0Fructose 1,6-bisphosphate → 1.0Phosphate + 1.0D-tagatofuranose 6-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Pyridoxal 5'-phosphate → 1.0Phosphate + 1.0Pyridoxal
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water ↔ 1.0Fructose 6-phosphate + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Fructose 1,6-bisphosphate + 1.0Water → 1.0Fructose 6-phosphate + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Water + 1.0Pyridoxine 5'-phosphate → 1.0Phosphate + 1.0Pyridoxine
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Pyridoxal 5'-phosphate + 1.0Water → 1.0Pyridoxal + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24205D-tagatofuranose 6-phosphateMetaboCard
ECMDB01058Fructose 1,6-bisphosphateMetaboCard
ECMDB00124Fructose 6-phosphateMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB01545PyridoxalMetaboCard
ECMDB01491Pyridoxal 5'-phosphateMetaboCard
ECMDB00239PyridoxineMetaboCard
ECMDB01319Pyridoxine 5'-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
cell part
membrane
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
ATPase activity, coupled to transmembrane movement of ions
ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
binding
catalytic activity
hydrolase activity
ion transmembrane transporter activity
nucleoside binding
purine nucleoside binding
substrate-specific transmembrane transporter activity
transmembrane transporter activity
transporter activity
Process
ATP biosynthetic process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside phosphate metabolic process
nucleotide metabolic process
purine nucleoside triphosphate biosynthetic process
purine nucleotide biosynthetic process
purine nucleotide metabolic process
purine ribonucleoside triphosphate biosynthetic process
Gene Properties
Blattner:b0766
Gene OrientationCounterclockwise
Centisome Percentage:17.17
Left Sequence End796836
Right Sequence End797654
Gene Sequence:
>819 bp
ATGGCTCGTCTGGCAGCATTTGATATGGATGGCACTTTATTGATGCCCGACCATCATTTA
GGTGAGAAAACCCTCTCTACTTTGGCGCGACTGCGTGAACGCGACATTACCCTCACTTTT
GCCACGGGGCGTCATGCGCTGGAGATGCAGCATATTCTCGGGGCGCTATCGCTGGATGCG
TATTTGATTACCGGCAACGGAACGCGCGTGCATTCTCTGGAAGGTGAACTTTTACATCGT
GATGATTTACCTGCGGATGTCGCGGAGCTGGTGCTGTATCAGCAATGGGATACCCGAGCC
AGCATGCATATCTTCAATGACGACGGTTGGTTTACCGGGAAAGAGATCCCTGCGTTGTTG
CAGGCATTTGTCTATAGCGGTTTTCGTTATCAGATAATCGATGTCAAAAAAATGCCACTC
GGCAGCGTCACCAAGATCTGCTTCTGTGGCGATCACGACGATCTTACACGCTTGCAGATC
CAGCTATACGAAGCATTAGGCGAGCGTGCACATTTGTGTTTTTCCGCCACGGATTGCCTC
GAAGTGCTGCCGGTGGGCTGCAATAAAGGCGCTGCATTGACGGTGCTGACCCAACATTTA
GGTTTATCGTTGCGCGATTGCATGGCCTTTGGTGATGCGATGAACGATCGCGAAATGTTA
GTCAGCGTCGGTAGCGGATTTATTATGGGCAATGCGATGCCGCAACTGCGCGCGGAGCTC
CCGCATTTACCGGTGATTGGACATTGCCGAAATCAGGCTGTCTCTCACTATTTGACGCAC
TGGCTGGACTATCCACATCTACCTTATTCCCCCGAATAA
Protein Properties
Pfam Domain Function:
Protein Residues:272
Protein Molecular Weight:30201
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Phosphatase ybhA
MTTRVIALDLDGTLLTPKKTLLPSSIEALARAREAGYQLIIVTGRHHVAIHPFYQALALD
TPAICCNGTYLYDYHAKTVLEADPMPVIKALQLIEMLNEHHIHGLMYVDDAMVYEHPTGH
VIRTSNWAQTLPPEQRPTFTQVASLAETAQQVNAVWKFALTHDDLPQLQHFGKHVEHELG
LECEWSWHDQVDIARGGNSKGKRLTKWVEAQGWSMENVVAFGDNFNDISMLEAAGTGVAM
GNADDAVKARANIVIGDNTTDSIAQFIYSHLI
References
External Links:
ResourceLink
Uniprot ID:P21829
Uniprot Name:YBHA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674586
Ecogene ID:EG11239
Ecocyc:EG11239
ColiBase:b0766
Kegg Gene:b0766
EchoBASE ID:EB1221
CCDB:YBHA_ECOLI
BacMap:16128734
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
  • Maupin-Furlow, J. A., Rosentel, J. K., Lee, J. H., Deppenmeier, U., Gunsalus, R. P., Shanmugam, K. T. (1995). "Genetic analysis of the modABCD (molybdate transport) operon of Escherichia coli." J Bacteriol 177:4851-4856. Pubmed: 7665460
  • 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
  • Walkenhorst, H. M., Hemschemeier, S. K., Eichenlaub, R. (1995). "Molecular analysis of the molybdate uptake operon, modABCD, of Escherichia coli and modR, a regulatory gene." Microbiol Res 150:347-361. Pubmed: 8564363