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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: cytoplasmic trehalase

Gene: treF Accession Numbers: EG12245 (MetaCyc), b3519, ECK3504

Species: Escherichia coli K-12 substr. MG1655

Summary:
E. coli contains two trehalases: the cytoplasmic TreF (discussed here) and the periplasmic TreA. Both enzymes catalyze the hydrolysis of trehalose into two molecules of D-glucose.

Transcription of treF is only weakly induced by high osmolarity and partially dependent on the stationary-phase alternative sigma factor RpoS [Horlacher96]. Under aerobic conditions, TreF protein is induced more than 20-fold by high osmolarity [Weber06].

Citations: [Uhland00]

Locations: cytosol

Map Position: [3,667,615 -> 3,669,264]

Molecular Weight of Polypeptide: 63.697 kD (from nucleotide sequence), 64.0 kD (experimental) [Horlacher96 ]

pI: 4.8 [Sofia94]

Unification Links: ASAP:ABE-0011497 , CGSC:35861 , EchoBASE:EB2156 , EcoGene:EG12245 , EcoliWiki:b3519 , EcoO157Cyc:TREF-MONOMER , OU-Microarray:b3519 , PortEco:treF , PR:PRO_000024109 , Pride:P62601 , Protein Model Portal:P62601 , RefSeq:NP_417976 , RegulonDB:EG12245 , SMR:P62601 , String:511145.b3519 , UniProt:P62601

Relationship Links: InterPro:IN-FAMILY:IPR001661 , InterPro:IN-FAMILY:IPR008928 , InterPro:IN-FAMILY:IPR018232 , InterPro:IN-FAMILY:IPR023715 , Panther:IN-FAMILY:PTHR23403 , Pfam:IN-FAMILY:PF01204 , Prints:IN-FAMILY:PR00744 , Prosite:IN-FAMILY:PS00927 , Prosite:IN-FAMILY:PS00928

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0005993 - trehalose catabolic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA01, Horlacher96]
GO:0071474 - cellular hyperosmotic response Inferred from experiment Inferred by computational analysis [GOA01, Weber06]
GO:0005991 - trehalose metabolic process Inferred by computational analysis [GOA06, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0004555 - alpha,alpha-trehalase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Horlacher96]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016798 - hydrolase activity, acting on glycosyl bonds Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01]
GO:0005829 - cytosol

MultiFun Terms: metabolism carbon utilization carbon compounds

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: trehalase

Synonyms: α,α-trehalase, α,α-trehalose glucohydrolase, cytoplasmic trehalase

EC Number: 3.2.1.28

α,α-trehalose + H2O <=> β-D-glucose + α-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.

In Pathways: trehalose degradation II (trehalase)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
The enzyme does not hydrolyze lactose, maltose or sucrose. Its activity decreases with increasing salt concentration [Horlacher96].

Kinetic Parameters:

Substrate
Km (μM)
Citations
α,α-trehalose
160.0, 310.0, 1500.0
[Uhland00, BRENDA14]
α,α-trehalose
1900.0
[Horlacher96]

pH(opt): 6.0 [BRENDA14, Horlacher96]


Sequence Features

Feature Class Location Citations Comment
Amino-Acid-Sites-That-Bind 168
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Protein-Segment 175 -> 176
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 212
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Protein-Segment 221 -> 223
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Protein-Segment 292 -> 294
[UniProt13]
UniProt: Substrate binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 324
[UniProt13]
UniProt: Substrate; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Active-Site 326
[UniProt13]
UniProt: Proton donor/acceptor; Non-Experimental Qualifier: by similarity.
Active-Site 509
[UniProt13]
UniProt: Proton donor/acceptor; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 525
[UniProt13]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.

History:
10/20/97 Gene b3519 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG12245; confirmed by SwissProt match.


References

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

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.

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Horlacher96: Horlacher R, Uhland K, Klein W, Ehrmann M, Boos W (1996). "Characterization of a cytoplasmic trehalase of Escherichia coli." J Bacteriol 178(21);6250-7. PMID: 8892826

Sofia94: Sofia HJ, Burland V, Daniels DL, Plunkett G, Blattner FR (1994). "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Nucleic Acids Res 1994;22(13);2576-86. PMID: 8041620

Uhland00: Uhland K, Mondigler M, Spiess C, Prinz W, Ehrmann M (2000). "Determinants of translocation and folding of TreF, a trehalase of Escherichia coli." J Biol Chem 275(31);23439-45. PMID: 10816581

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Weber06: Weber A, Kogl SA, Jung K (2006). "Time-dependent proteome alterations under osmotic stress during aerobic and anaerobic growth in Escherichia coli." J Bacteriol 188(20);7165-75. PMID: 17015655


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Fri Dec 19, 2014, biocyc14.