Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: cytoplasmic trehalase



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

Regulation Summary Diagram: ?

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]

Gene Citations: [Maciag11]

Locations: cytosol

Map Position: [3,667,615 -> 3,669,264] (79.05 centisomes)
Length: 1650 bp / 549 aa

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

pI: 4.8 [Sofia94]

Isozyme Sequence Similarity:
periplasmic trehalase: YES

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, GOA01a, Horlacher96]
GO:0071474 - cellular hyperosmotic response Inferred from experiment Inferred by computational analysis [GOA01a, Weber06]
GO:0005991 - trehalose metabolic process Inferred by computational analysis [GOA06, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0004555 - alpha,alpha-trehalase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Horlacher96]
GO:0003824 - catalytic 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:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, GOA01a]
GO:0005829 - cytosol

MultiFun Terms: metabolism carbon utilization carbon compounds

Essentiality data for treF knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

Credits:
Last-Curated ? 24-Mar-2010 by Keseler I , 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)

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.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

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

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

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

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

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

Maciag11: Maciag A, Peano C, Pietrelli A, Egli T, De Bellis G, Landini P (2011). "In vitro transcription profiling of the {sigma}S subunit of bacterial RNA polymerase: re-definition of the {sigma}S regulon and identification of {sigma}S-specific promoter sequence elements." Nucleic Acids Res 39(13);5338-55. PMID: 21398637

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 manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms 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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc14.