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Escherichia coli K-12 substr. MG1655 Enzyme: 6-phospho-β-glucosidase; cryptic



Gene: ascB Accession Numbers: EG10085 (EcoCyc), b2716, ECK2711

Synonyms: sac

Regulation Summary Diagram: ?

Summary:
ascB is thought to encode phospho-β-glucosidase as part of the cryptic asc operon [Hall92].

sac: "salicin-arbutin-cellobiose" [Parker88]

Locations: cytosol

Map Position: [2,839,012 -> 2,840,436] (61.19 centisomes)
Length: 1425 bp / 474 aa

Molecular Weight of Polypeptide: 53.935 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0008928 , CGSC:33236 , EchoBASE:EB0083 , EcoGene:EG10085 , EcoliWiki:b2716 , ModBase:P24240 , OU-Microarray:b2716 , PortEco:ascB , PR:PRO_000022161 , Pride:P24240 , Protein Model Portal:P24240 , RefSeq:NP_417196 , RegulonDB:EG10085 , SMR:P24240 , String:511145.b2716 , UniProt:P24240

Relationship Links: CAZy:IN-FAMILY:GH1 , InterPro:IN-FAMILY:IPR001360 , InterPro:IN-FAMILY:IPR013781 , InterPro:IN-FAMILY:IPR017853 , InterPro:IN-FAMILY:IPR018120 , Panther:IN-FAMILY:PTHR10353 , Pfam:IN-FAMILY:PF00232 , Prints:IN-FAMILY:PR00131 , Prosite:IN-FAMILY:PS00572 , Prosite:IN-FAMILY:PS00653

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004553 - hydrolase activity, hydrolyzing O-glycosyl compounds Inferred by computational analysis [GOA01]
GO:0008706 - 6-phospho-beta-glucosidase activity Inferred by computational analysis [GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016798 - hydrolase activity, acting on glycosyl bonds Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for ascB 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]

Enzymatic reaction of: arbutin-6-phosphate glucohydrolase (6-phospho-β-glucosidase; cryptic)

EC Number: 3.2.1.86

arbutin-6-phosphate + H2O <=> β-D-glucose 6-phosphate + benzene-1,4-diol

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 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.


Enzymatic reaction of: 6-phospho-β-D-glucosyl-(1,4)-D-glucose glucohydrolase (6-phospho-β-glucosidase; cryptic)

Synonyms: 6-phospho-b-glucosidase, 6-phospho-b-D-glucosyl-(1,4)-D-glucose glucohydrolase, phospho-b-glucosidase A, phospho-b-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.


Sequence Features

Feature Class Location Citations Comment
Active-Site 180
[UniProt10a]
UniProt: Proton donor; Non-Experimental Qualifier: potential;
Active-Site 372
[UniProt10a]
UniProt: Nucleophile; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 405 -> 406
[Hall92, UniProt10]
Alternate sequence: EA → GT; UniProt: (in Ref. 1; AAA16430);
Sequence-Conflict 428
[Hall92, UniProt10]
Alternate sequence: S → C; UniProt: (in Ref. 1; AAA16430);
Sequence-Conflict 455 -> 456
[Hall92, UniProt10]
Alternate sequence: RK → HR; UniProt: (in Ref. 1; AAA16430);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2716 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10085; 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.

Hall92: Hall BG, Xu L (1992). "Nucleotide sequence, function, activation, and evolution of the cryptic asc operon of Escherichia coli K12." Mol Biol Evol 9(4);688-706. PMID: 1630307

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

Parker88: Parker LL, Hall BG (1988). "A fourth Escherichia coli gene system with the potential to evolve beta-glucoside utilization." Genetics 119(3);485-90. PMID: 3042507

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

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

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

Other References Related to Gene Regulation

Beisel12: Beisel CL, Updegrove TB, Janson BJ, Storz G (2012). "Multiple factors dictate target selection by Hfq-binding small RNAs." EMBO J 31(8);1961-74. PMID: 22388518

Ishida09: Ishida Y, Kori A, Ishihama A (2009). "Participation of regulator AscG of the beta-glucoside utilization operon in regulation of the propionate catabolism operon." J Bacteriol 191(19);6136-44. PMID: 19633077


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 Mon Nov 24, 2014, BIOCYC14B.