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Escherichia coli K-12 substr. MG1655 Enzyme: betaine aldehyde dehydrogenase



Gene: betB Accession Numbers: EG10110 (EcoCyc), b0312, ECK0310

Regulation Summary Diagram: ?

Subunit composition of betaine aldehyde dehydrogenase = [BetB]4

Summary:
Betaine aldehyde dehydrogenase (BADH) catalyzes the second step in the biosynthesis of the osmoprotectant glycine betaine from choline [Landfald86, Falkenberg90].

Expression of the bet operon is regulated by oxygen, choline, osmotic stress, and temperature [Eshoo88, Lamark96].

BetB: "betaine" [Andresen88]

Gene Citations: [Rkenes96]

Locations: cytosol, inner membrane

Map Position: [326,485 <- 327,957] (7.04 centisomes)
Length: 1473 bp / 490 aa

Molecular Weight of Polypeptide: 52.911 kD (from nucleotide sequence), 55.0 kD (experimental) [Falkenberg90 ]

Molecular Weight of Multimer: 240.0 kD (experimental) [Incharoensakdi00]

pI: 5.4

Unification Links: ASAP:ABE-0001072 , CGSC:17737 , DIP:DIP-9208N , EchoBASE:EB0108 , EcoGene:EG10110 , EcoliWiki:b0312 , ModBase:P17445 , OU-Microarray:b0312 , PortEco:betB , PR:PRO_000022208 , Pride:P17445 , Protein Model Portal:P17445 , RefSeq:NP_414846 , RegulonDB:EG10110 , SMR:P17445 , String:511145.b0312 , Swiss-Model:P17445 , UniProt:P17445

Relationship Links: InterPro:IN-FAMILY:IPR011264 , InterPro:IN-FAMILY:IPR015590 , InterPro:IN-FAMILY:IPR016160 , InterPro:IN-FAMILY:IPR016161 , InterPro:IN-FAMILY:IPR016162 , InterPro:IN-FAMILY:IPR016163 , Pfam:IN-FAMILY:PF00171 , Prosite:IN-FAMILY:PS00070 , Prosite:IN-FAMILY:PS00687

In Paralogous Gene Group: 95 (14 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006970 - response to osmotic stress Inferred from experiment [Landfald86, Andresen88]
GO:0019285 - glycine betaine biosynthetic process from choline Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA06, GOA01, Landfald86]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008802 - betaine-aldehyde dehydrogenase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Falkenberg90, Landfald86]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016620 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0005886 - plasma membrane

MultiFun Terms: cell processes adaptations osmotic pressure
metabolism central intermediary metabolism betaine biosynthesis

Essentiality data for betB 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]
Yes [Feist07, Comment 4]

Credits:
Last-Curated ? 07-Oct-2010 by Keseler I , SRI International


Enzymatic reaction of: betaine aldehyde dehydrogenase

Synonyms: BADH, betaine aldehyde:NAD+ oxidoreductase

EC Number: 1.2.1.8

betaine aldehyde + NAD+ + H2O <=> glycine betaine + NADH + 2 H+

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.

Alternative Substrates for betaine aldehyde [Comment 5 ]: 4-aminobutanal [Incharoensakdi00 ] , A-aminopropionaldehyde [Incharoensakdi00 ]

In Pathways: glycine betaine biosynthesis I (Gram-negative bacteria)

Inhibitors (Competitive): tetramethylammonium [Falkenberg90] , trimethylacetaldehyde [Falkenberg90] , 3-methylbutanal [Falkenberg90] , D-glyceraldehyde [Falkenberg90] , benzaldehyde [Falkenberg90] , acetaldehyde [Falkenberg90] , phenylacetaldehyde [Falkenberg90] , choline [Falkenberg90] , butyrylcholine [Falkenberg90] , N-dimethylethanolamine [Falkenberg90] , N-monomethylethanolamine [Falkenberg90]

Inhibitors (Unknown Mechanism): Zn2+ [Falkenberg90] , Hg2+ [Falkenberg90] , p-chloromercuribenzoate [Falkenberg90]

Kinetic Parameters:

Substrate
Km (μM)
Citations
betaine aldehyde
150.0
[Yilmaz, BRENDA14]
betaine aldehyde
160.0
[Falkenberg90, BRENDA14]
betaine aldehyde
1800.0, 6500.0
[Gruez04, BRENDA14]
betaine aldehyde
130.0
[Landfald86, BRENDA14]
betaine aldehyde
77.0, 77.0
[Incharoensakdi00]
NAD+
60.0
[Landfald86, BRENDA14]
NAD+
99.0
[Falkenberg90, BRENDA14]
NAD+
77.0, 77.0
[Incharoensakdi00]

pH(opt): 7.5 [BRENDA14, Falkenberg90], 8.5 [BRENDA14, Yilmaz], 7.5-9.5 [Landfald86]


Sequence Features

Feature Class Location Attached Group Citations Comment
Cleavage-of-Initial-Methionine 1  
[Lamark91, UniProt08, Lamark91]
UniProt: Removed;
Chain 2 -> 490  
[UniProt09]
UniProt: Betaine aldehyde dehydrogenase;
Metal-Binding-Site 26  
[UniProt14]
UniProt: Potassium 1; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 27  
[UniProt14]
UniProt: Potassium 1; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 93  
[UniProt14]
UniProt: Potassium 1; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 150 -> 153 NAD/NADP
[UniProt14]
UniProt: NAD/NADP; Non-Experimental Qualifier: by similarity.
Active-Site 162  
[UniProt14]
UniProt: Charge relay system; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 176 -> 179 NAD/NADP
[UniProt14]
UniProt: NAD/NADP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 180  
[UniProt14]
UniProt: Potassium 1; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 209  
[UniProt14]
UniProt: NAD/NADP; via amide nitrogen; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 229 -> 234  
[UniProt10a]
UniProt: NAD; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 232  
[Boyd91, UniProt10]
Alternate sequence: A → R; UniProt: (in Ref. 2; AAA23506/AAA23505);
Metal-Binding-Site 246  
[UniProt14]
UniProt: Potassium 2; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Amino-Acid-Site 248  
[UniProt14]
UniProt: Seems to be a necessary countercharge to the potassium cations; Sequence Annotation Type: site; Non-Experimental Qualifier: by similarity.
Active-Site 252  
[UniProt10a]
UniProt: Non-Experimental Qualifier: by similarity;
Cysteine-sulfenic-acid-Modification 286  
[UniProt14]
UniProt: Cysteine sulfenic acid (-SOH); Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 286  
[UniProt14]
UniProt: NAD/NADP; Non-Experimental Qualifier: by similarity.
Sequence-Conflict 312  
[Boyd91, UniProt10]
Alternate sequence: R → P; UniProt: (in Ref. 2; AAA23506/AAA23505);
Amino-Acid-Sites-That-Bind 387  
[UniProt14]
UniProt: NAD/NADP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 457  
[UniProt14]
UniProt: Potassium 2; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 460  
[UniProt14]
UniProt: Potassium 2; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Active-Site 464  
[UniProt14]
UniProt: Charge relay system; Non-Experimental Qualifier: by similarity.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0312 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10110; confirmed by SwissProt match.


References

Andresen88: Andresen PA, Kaasen I, Styrvold OB, Boulnois G, Strom AR (1988). "Molecular cloning, physical mapping and expression of the bet genes governing the osmoregulatory choline-glycine betaine pathway of Escherichia coli." J Gen Microbiol 1988;134 ( Pt 6);1737-46. PMID: 3065456

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

Boyd91: Boyd LA, Adam L, Pelcher LE, McHughen A, Hirji R, Selvaraj G (1991). "Characterization of an Escherichia coli gene encoding betaine aldehyde dehydrogenase (BADH): structural similarity to mammalian ALDHs and a plant BADH." Gene 103(1);45-52. PMID: 1879697

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

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

Eshoo88: Eshoo MW (1988). "lac fusion analysis of the bet genes of Escherichia coli: regulation by osmolarity, temperature, oxygen, choline, and glycine betaine." J Bacteriol 1988;170(11);5208-15. PMID: 3141381

Falkenberg90: Falkenberg P, Strom AR (1990). "Purification and characterization of osmoregulatory betaine aldehyde dehydrogenase of Escherichia coli." Biochim Biophys Acta 1990;1034(3);253-9. PMID: 2194570

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

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.

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

Gruez04: Gruez A, Roig-Zamboni V, Grisel S, Salomoni A, Valencia C, Campanacci V, Tegoni M, Cambillau C (2004). "Crystal structure and kinetics identify Escherichia coli YdcW gene product as a medium-chain aldehyde dehydrogenase." J Mol Biol 343(1);29-41. PMID: 15381418

Incharoensakdi00: Incharoensakdi A, Matsuda N, Hibino T, Meng YL, Ishikawa H, Hara A, Funaguma T, Takabe T (2000). "Overproduction of spinach betaine aldehyde dehydrogenase in Escherichia coli. Structural and functional properties of wild-type, mutants and E. coli enzymes." Eur J Biochem 267(24);7015-23. PMID: 11106411

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

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

Lamark91: Lamark T, Kaasen I, Eshoo MW, Falkenberg P, McDougall J, Strom AR (1991). "DNA sequence and analysis of the bet genes encoding the osmoregulatory choline-glycine betaine pathway of Escherichia coli." Mol Microbiol 1991;5(5);1049-64. PMID: 1956285

Lamark96: Lamark T, Rokenes TP, McDougall J, Strom AR (1996). "The complex bet promoters of Escherichia coli: regulation by oxygen (ArcA), choline (BetI), and osmotic stress." J Bacteriol 1996;178(6);1655-62. PMID: 8626294

Landfald86: Landfald B, Strom AR (1986). "Choline-glycine betaine pathway confers a high level of osmotic tolerance in Escherichia coli." J Bacteriol 1986;165(3);849-55. PMID: 3512525

Rkenes96: Rkenes TP, Lamark T, Strom AR (1996). "DNA-binding properties of the BetI repressor protein of Escherichia coli: the inducer choline stimulates BetI-DNA complex formation." J Bacteriol 1996;178(6);1663-70. PMID: 8626295

UniProt08: UniProt Consortium (2008). "UniProt version 14.6 released on 2008-12-16." Database.

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

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.

UniProt14: UniProt Consortium (2014). "UniProt version 2014-01 released on 2014-01-01 00:00:00." Database.

UniProtGOA11: 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."

Yilmaz: Yilmaz JL, Bulow L "Enhanced stress tolerance in Escherichia coli and Nicotiana tabacum expressing a betaine aldehyde dehydrogenase/choline dehydrogenase fusion protein." Biotechnol Prog 18(6);1176-82. PMID: 12467448

Other References Related to Gene Regulation

Lynch96: Lynch AS, Lin EC (1996). "Transcriptional control mediated by the ArcA two-component response regulator protein of Escherichia coli: characterization of DNA binding at target promoters." J Bacteriol 1996;178(21);6238-49. PMID: 8892825

Son11: Son YJ, Phue JN, Trinh LB, Lee SJ, Shiloach J (2011). "The role of Cra in regulating acetate excretion and osmotic tolerance in E. coli K-12 and E. coli B at high density growth." Microb Cell Fact 10;52. PMID: 21718532


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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 Sun Dec 21, 2014, biocyc14.