6-phospho-beta-glucosidase (P17411)

Identification
Name:6-phospho-beta-glucosidase
Synonyms:
  • Cellobiose-6-phosphate hydrolase
  • Phospho-chitobiase
Gene Name:chbF
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity, hydrolyzing O-glycosyl compounds
Specific Function:Hydrolyzes a wide variety of P-beta-glucosides including cellobiose-6P, salicin-6P, arbutin-6P, gentiobiose-6P, methyl- beta-glucoside-6P and p-nitrophenyl-beta-D-glucopyranoside-6P. Is also able to hydrolyze phospho-N,N'-diacetylchitobiose
Cellular Location:Cytoplasmic
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Arbutin 6-phosphate + 1.0Water ↔ 1.0Hydroquinone + 1.0beta-D-Glucose 6-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Cellobiose-6-phosphate + 1.0Water ↔ 1.0D-Glucose + 1.0Glucose 6-phosphate
ReactionCard
SMPDB Reactions:
1.0N'-monoacetylchitobiose-6'-phosphate+1.0Thumb → 1.0Thumb+1.0Glucosamine
1.0N'-monoacetylchitobiose-6'-phosphate + 1.0Water → 1.0N-Acetyl-D-Glucosamine 6-Phosphate + 1.0Glucosamine
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Diacetylchitobiose-6-phosphate + 1.0Water → 1.0N-Acetyl-D-glucosamine + 1.0N-Acetyl-D-Glucosamine 6-Phosphate
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Cellobiose-6-phosphate + 1.0Water → 1.0Glucose 6-phosphate + 1.0b-D-Glucose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB215046-Phospho-beta-D-glucosyl-(1,4)-D-glucoseMetaboCard
ECMDB20117Arbutin 6-phosphateMetaboCard
ECMDB00516b-D-GlucoseMetaboCard
ECMDB03498beta-D-Glucose 6-phosphateMetaboCard
ECMDB20267Cellobiose-6-phosphateMetaboCard
ECMDB00122D-GlucoseMetaboCard
ECMDB20547Diacetylchitobiose-6-phosphateMetaboCard
ECMDB01401Glucose 6-phosphateMetaboCard
ECMDB02434HydroquinoneMetaboCard
ECMDB00215N-Acetyl-D-glucosamineMetaboCard
ECMDB01062N-Acetyl-D-Glucosamine 6-PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing O-glycosyl compounds
Process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b1734
Gene OrientationCounterclockwise
Centisome Percentage:39.12
Left Sequence End1815172
Right Sequence End1816524
Gene Sequence:
>1353 bp
ATGCTGAGTTTTCTCTGGGATTTGGCTTCGTTCATCGTTGCACTGGGTGTACTTATCACC
GTGCATGAATTTGGTCATTTCTGGGTTGCCCGGCGTTGTGGTGTTCGCGTTGAGCGTTTC
TCAATAGGGTTTGGTAAGGCGCTCTGGCGGCGAACTGATAAGCTCGGCACCGAATATGTT
ATCGCCCTGATCCCGTTGGGCGGTTATGTCAAAATGCTGGATGAGCGCGCAGAACCGGTC
GTTCCGGAACTCCGCCACCATGCCTTCAATAATAAATCTGTCGGCCAACGAGCGGCGATT
ATTGCCGCAGGTCCGGTTGCAAACTTCATTTTTGCTATCTTTGCCTACTGGCTGGTTTTT
ATTATTGGTGTGCCTGGCGTACGTCCGGTGGTTGGCGAAATAGCAGCCAATTCGATAGCT
GCGGAAGCACAAATTGCACCAGGTACGGAACTAAAAGCCGTAGATGGTATCGAAACGCCT
GATTGGGATGCCGTGCGTTTGCAGTTGGTCGATAAAATTGGCGATGAAAGCACCACCATT
ACAGTAGCGCCATTTGGCAGCGACCAACGGCGGGATGTAAAGCTCGATTTACGTCACTGG
GCGTTTGAGCCTGATAAAGAAGATCCGGTATCTTCGCTGGGGATTCGTCCTCGTGGGCCG
CAAATTGAACCTGTACTGGAAAATGTGCAGCCAAACTCGGCGGCAAGCAAGGCAGGTTTG
CAAGCAGGCGACAGGATCGTTAAAGTCGATGGTCAGCCCTTAACGCAGTGGGTGACCTTT
GTGATGCTTGTCCGGGATAACCCGGGTAAATCCTTAGCGTTAGAAATCGAAAGGCAGGGG
AGTCCCTTGTCTTTGACATTAATCCCGGAGAGTAAACCGGGTAATGGTAAAGCGATTGGT
TTTGTCGGTATTGAGCCGAAAGTCATTCCTTTGCCAGATGAGTATAAAGTTGTACGCCAG
TATGGGCCGTTCAACGCCATCGTCGAAGCCACGGACAAAACGTGGCAGCTGATGAAGCTG
ACGGTCAGTATGCTGGGAAAATTGATCACCGGTGATGTGAAACTGAACAACCTCAGTGGG
CCGATCTCTATCGCCAAGGGGGCTGGGATGACAGCGGAACTCGGGGTTGTTTATTACCTG
CCGTTTCTTGCGCTTATTAGCGTGAACTTAGGGATAATTAACCTGTTTCCGTTGCCCGTA
CTTGACGGGGGGCATCTGCTGTTCCTTGCGATCGAAAAGATCAAGGGCGGACCGGTATCC
GAGCGGGTTCAAGACTTTTGTTATCGCATTGGCTCGATTCTGCTGGTGCTGTTAATGGGG
CTTGCACTTTTCAATGATTTCTCTCGGTTATGA
Protein Properties
Pfam Domain Function:
Protein Residues:450
Protein Molecular Weight:50512
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>6-phospho-beta-glucosidase
MSQKLKVVTIGGGSSYTPELLEGFIKRYHELPVSELWLVDVEGGKPKLDIIFDLCQRMID
NAGVPMKLYKTLDRREALKDADFVTTQLRVGQLPARELDERIPLSHGYLGQETNGAGGLF
KGLRTIPVIFDIVKDVEELCPNAWVINFTNPAGMVTEAVYRHTGFKRFIGVCNIPIGMKM
FIRDVLMLKDSDDLSIDLFGLNHMVFIKDVLINGKSRFAELLDGVASGQLKASSVKNIFD
LPFSEGLIRSLNLLPCSYLLYYFKQKEMLAIEMGEYYKGGARAQVVQKVEKQLFELYKNP
ELKVKPKELEQRGGAYYSDAACEVINAIYNDKQAEHYVNIPHHGQIDNIPADWAVEMTCK
LGRDGATPHPRITHFDDKVMGLIHTIKGFEIAASNAALSGEFNDVLLALNLSPLVHSDRD
AELLAREMILAHEKWLPNFADCIAELKKAH
References
External Links:
ResourceLink
Uniprot ID:P17411
Uniprot Name:CHBF_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902917
Ecogene ID:EG10144
Ecocyc:EG10144
ColiBase:b1734
Kegg Gene:b1734
EchoBASE ID:EB0142
CCDB:CHBF_ECOLI
BacMap:16129688
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Guzzo, A., DuBow, M. S. (1994). "A luxAB transcriptional fusion to the cryptic celF gene of Escherichia coli displays increased luminescence in the presence of nickel." Mol Gen Genet 242:455-460. Pubmed: 8121401
  • 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
  • Keyhani, N. O., Roseman, S. (1997). "Wild-type Escherichia coli grows on the chitin disaccharide, N,N'-diacetylchitobiose, by expressing the cel operon." Proc Natl Acad Sci U S A 94:14367-14371. Pubmed: 9405618
  • Keyhani, N. O., Wang, L. X., Lee, Y. C., Roseman, S. (2000). "The chitin disaccharide, N,N'-diacetylchitobiose, is catabolized by Escherichia coli and is transported/phosphorylated by the phosphoenolpyruvate:glycose phosphotransferase system." J Biol Chem 275:33084-33090. Pubmed: 10913117
  • Parker, L. L., Hall, B. G. (1990). "Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12." Genetics 124:455-471. Pubmed: 2179047
  • Thompson, J., Ruvinov, S. B., Freedberg, D. I., Hall, B. G. (1999). "Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases." J Bacteriol 181:7339-7345. Pubmed: 10572139