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Escherichia coli K-12 substr. MG1655 Enzyme: monoacetylchitobiose-6-phosphate hydrolase



Gene: chbF Accession Numbers: EG10144 (EcoCyc), b1734, ECK1732

Synonyms: ydjD, celF

Regulation Summary Diagram: ?

Subunit composition of monoacetylchitobiose-6-phosphate hydrolase = [ChbF]4
         monoacetylchitobiose-6-phosphate hydrolase = ChbF

Summary:
ChbF appears to be a monoacetylchitobiose-6-phosphate hydrolase responsible for converting monoacetylchitobiose-6-phosphate to D-glucosamine and N-acetyl-D-glucosamine-6-phosphate [Keyhani97, Verma12]. ChbF belongs to family 4 of the glycosylhydrolase superfamily [Thompson99].

Substrate specificity of the enzyme was investigated by [Thompson99]; unfortunately, chitobiose derivatives were not among the tested substrates.

ChbF: "N,N'-diacetylchitobiose F" [Keyhani97]

Citations: [Plumbridge04]

Gene Citations: [Reizer90]

Locations: cytosol

Map Position: [1,815,172 <- 1,816,524] (39.12 centisomes)
Length: 1353 bp / 450 aa

Molecular Weight of Polypeptide: 50.512 kD (from nucleotide sequence), 50.0 kD (experimental) [Thompson99 ]

Molecular Weight of Multimer: 210.0 kD (experimental) [Thompson99]

Unification Links: ASAP:ABE-0005785 , CGSC:17734 , DIP:DIP-9267N , EchoBASE:EB0142 , EcoGene:EG10144 , EcoliWiki:b1734 , ModBase:P17411 , OU-Microarray:b1734 , PortEco:chbF , PR:PRO_000022275 , Pride:P17411 , Protein Model Portal:P17411 , RefSeq:NP_416248 , RegulonDB:EG10144 , SMR:P17411 , String:511145.b1734 , Swiss-Model:P17411 , UniProt:P17411

Relationship Links: CAZy:IN-FAMILY:GH4 , InterPro:IN-FAMILY:IPR001088 , InterPro:IN-FAMILY:IPR015955 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR019802 , InterPro:IN-FAMILY:IPR022616 , Pfam:IN-FAMILY:PF02056 , Pfam:IN-FAMILY:PF11975 , Prints:IN-FAMILY:PR00732 , Prosite:IN-FAMILY:PS01324

In Paralogous Gene Group: 342 (3 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0052777 - diacetylchitobiose catabolic process Inferred from experiment [Keyhani97]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [GOA01]
Molecular Function: GO:0008706 - 6-phospho-beta-glucosidase activity Inferred from experiment Inferred by computational analysis [GOA01a, Thompson99]
GO:0042802 - identical protein binding Inferred from experiment [Thompson99]
GO:0004553 - hydrolase activity, hydrolyzing O-glycosyl compounds Inferred by computational analysis [GOA01]
GO:0016616 - oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016798 - hydrolase activity, acting on glycosyl bonds Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005737 - cytoplasm
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for chbF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enriched Yes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]

Credits:
Created 09-Aug-2012 by Keseler I , SRI International
Last-Curated ? 09-Aug-2012 by Keseler I , SRI International


Enzymatic reaction of: monoacetylchitobiose-6-phosphate hydrolase

EC Number: 3.2.1.86

N-monoacetylchitobiose 6'-phosphate + H2O <=> N-acetyl-D-glucosamine 6-phosphate + D-glucosamine

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: chitobiose degradation

Cofactors or Prosthetic Groups: Mn2+ [Thompson99], NAD+ [Thompson99]


Enzymatic reaction of: 6-phospho-β-D-glucosyl-(1,4)-D-glucose glucohydrolase (monoacetylchitobiose-6-phosphate hydrolase)

Synonyms: 6-phospho-β-glucosidase, phospho-β-glucosidase, phosphocellobiase

EC Number: 3.2.1.86

β-D-cellobiose 6'-phosphate + H2O <=> β-D-glucose 6-phosphate + β-D-glucose

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Note: The enzyme may catalyze this reaction in vitro, but this reaction is not considered to be physiologically relevant.

Cofactors or Prosthetic Groups: Mn2+ [Thompson99], NAD+ [Thompson99]

Kinetic Parameters:

Substrate
Km (μM)
Citations
β-D-cellobiose 6'-phosphate
1300.0
[Thompson99]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Thompson99, UniProt11, Thompson99]
UniProt: Removed.
Chain 2 -> 450
[UniProt09]
UniProt: 6-phospho-beta-glucosidase;
Nucleotide-Phosphate-Binding-Region 5 -> 73
[UniProt10a]
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 96
[UniProt10a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Amino-Acid-Site 112
[UniProt10a]
UniProt: Increases basicity of active site Tyr; Sequence Annotation Type: site; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 150
[UniProt10a]
UniProt: Substrate; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 172
[UniProt10a]
UniProt: Manganese; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 203
[UniProt10a]
UniProt: Manganese; Non-Experimental Qualifier: by similarity;
Active-Site 258
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1734 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10144; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Keyhani97: Keyhani NO, 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 1997;94(26);14367-71. PMID: 9405618

Plumbridge04: Plumbridge J, Pellegrini O (2004). "Expression of the chitobiose operon of Escherichia coli is regulated by three transcription factors: NagC, ChbR and CAP." Mol Microbiol 52(2);437-49. PMID: 15066032

Reizer90: Reizer J, Reizer A, Saier MH (1990). "The cellobiose permease of Escherichia coli consists of three proteins and is homologous to the lactose permease of Staphylococcus aureus." Res Microbiol 1990;141(9);1061-7. PMID: 2092358

Thompson99: Thompson J, Ruvinov SB, Freedberg DI, Hall BG (1999). "Cellobiose-6-phosphate hydrolase (CelF) of Escherichia coli: characterization and assignment to the unusual family 4 of glycosylhydrolases." J Bacteriol 181(23);7339-45. PMID: 10572139

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Verma12: Verma SC, Mahadevan S (2012). "The chbG Gene of the Chitobiose (chb) Operon of Escherichia coli Encodes a Chitooligosaccharide Deacetylase." J Bacteriol 194(18);4959-71. PMID: 22797760

Other References Related to Gene Regulation

Kachroo07: Kachroo AH, Kancherla AK, Singh NS, Varshney U, Mahadevan S (2007). "Mutations that alter the regulation of the chb operon of Escherichia coli allow utilization of cellobiose." Mol Microbiol 66(6);1382-95. PMID: 18028317

Oberto10: Oberto J (2010). "FITBAR: a web tool for the robust prediction of prokaryotic regulons." BMC Bioinformatics 11;554. PMID: 21070640

Overgaard09: Overgaard M, Johansen J, Moller-Jensen J, Valentin-Hansen P (2009). "Switching off small RNA regulation with trap-mRNA." Mol Microbiol 73(5);790-800. PMID: 19682266

Parker90: Parker LL, Hall BG (1990). "Characterization and nucleotide sequence of the cryptic cel operon of Escherichia coli K12." Genetics 124(3);455-71. PMID: 2179047

Plumbridge14: Plumbridge J, Bossi L, Oberto J, Wade JT, Figueroa-Bossi N (2014). "Interplay of transcriptional and small RNA-dependent control mechanisms regulates chitosugar uptake in Escherichia coli and Salmonella." Mol Microbiol. PMID: 24593230

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, BIOCYC14B.