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Escherichia coli K-12 substr. MG1655 Enzyme: thiamin monophosphate kinase



Gene: thiL Accession Numbers: G6234 (EcoCyc), b0417, ECK0411

Synonyms: thiJ, ATP:thiamine-phosphate phosphotransferase

Regulation Summary Diagram: ?

Summary:
Thiamin phosphate kinase (ThiL) is involved in the final step of thiamin biosynthesis. ThiL catalyzes the phosphorylation of thiamin monophosphate to yield thiamin diphosphate in the presence of ATP and Mg2+[Nishino72, Nakayama72, Imamura82].

Mutations in thiL resulted in a requirement for thiamin pyrophosphate for growth [Begley99]. In Salmonella typhimurium, altered ThiL activity resulted in decreased repression of transcription of thiamin pyrophosphate-regulated genes [Webb97].

The ThiL structure with substrate and product complexes in Aquifex aeolicus was determined [McCulloch08].

Gene Citations: [Nonaka06, Torrents07]

Locations: cytosol

Map Position: [434,858 -> 435,835] (9.37 centisomes)
Length: 978 bp / 325 aa

Molecular Weight of Polypeptide: 35.071 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0001452 , EchoBASE:EB4149 , EcoGene:EG20227 , EcoliWiki:b0417 , ModBase:P0AGG0 , OU-Microarray:b0417 , PortEco:thiL , PR:PRO_000024061 , Pride:P0AGG0 , Protein Model Portal:P0AGG0 , RefSeq:NP_414951 , RegulonDB:G6234 , SMR:P0AGG0 , String:511145.b0417 , UniProt:P0AGG0

Relationship Links: InterPro:IN-FAMILY:IPR000728 , InterPro:IN-FAMILY:IPR006283 , InterPro:IN-FAMILY:IPR010918 , InterPro:IN-FAMILY:IPR016188 , Panther:IN-FAMILY:PTHR30270 , Pfam:IN-FAMILY:PF00586 , Pfam:IN-FAMILY:PF02769

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009228 - thiamine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Nishino72]
GO:0009229 - thiamine diphosphate biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, GOA06, Nishino72]
GO:0016310 - phosphorylation Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0000287 - magnesium ion binding Inferred from experiment Inferred by computational analysis [GOA06, Nishino72]
GO:0005524 - ATP binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA06, Nishino72]
GO:0009030 - thiamine-phosphate kinase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Nishino72]
GO:0046872 - metal ion binding Inferred from experiment Inferred by computational analysis [UniProtGOA11, Nishino72]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01]
GO:0016301 - kinase activity Inferred by computational analysis [UniProtGOA11]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks cofactors, small molecule carriers thiamin

Essentiality data for thiL knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Credits:
Curated 19-Sep-2006 by Shearer A , SRI International
Last-Curated ? 06-Aug-2013 by Kubo A , SRI International


Enzymatic reaction of: thiamin monophosphate kinase

EC Number: 2.7.4.16

thiamin phosphate + ATP <=> thiamin diphosphate + ADP

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: superpathway of thiamin diphosphate biosynthesis I , thiamin diphosphate biosynthesis I (E. coli) , thiamin salvage II

Cofactors or Prosthetic Groups: Mg2+ [Comment 2, Nishino72]

Activators (Allosteric): Rb+ [Nishino72]

Activators (Unknown Mechanism): K+ [Nishino72, Comment 3] , ammonium [Nishino72]

Inhibitors (Competitive): pyrithiamine phosphate [Nishino72]

Inhibitors (Noncompetitive): AMP

Inhibitors (Unknown Mechanism): ADP [Nishino72, Comment 4] , p-chloromercuribenzoate [Nishino72] , N-ethylmaleimide [Nishino72] , diphosphate [Nishino72] , EDTA [Nishino72]

Primary Physiological Regulators of Enzyme Activity: ADP

Kinetic Parameters:

Substrate
Km (μM)
Citations
thiamin phosphate
11.0
[Nishino72]
ATP
270.0
[Nishino72]

pH(opt): 8 [Nishino72]


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 30
[UniProt12b]
UniProt: Magnesium 3; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 45
[UniProt12b]
UniProt: Magnesium 4; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 46
[UniProt12b]
UniProt: Magnesium 1; via carbonyl oxygen; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 47
[UniProt12b]
UniProt: Magnesium 1; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 54
[UniProt12b]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 75
[UniProt12b]
UniProt: Magnesium 2; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 121 -> 122
[UniProt12b]
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 122
[UniProt12b]
UniProt: Magnesium 1; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 146
[UniProt12b]
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 212
[UniProt12b]
UniProt: Magnesium 3; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 214
[UniProt12b]
UniProt: ATP; Non-Experimental Qualifier: by similarity.
Metal-Binding-Site 215
[UniProt12b]
UniProt: Magnesium 5; Non-Experimental Qualifier: by similarity.
Sequence-Conflict 254
[Iida97, UniProt10a]
Alternate sequence: A → E; UniProt: (in Ref. 1; BAA21778);
Amino-Acid-Sites-That-Bind 263
[UniProt12b]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 319
[UniProt12b]
UniProt: Substrate; Non-Experimental Qualifier: by similarity.


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
3/2/1998 (pkarp) Merged genes G200/EG20227 and G6234/thiL
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

Begley99: Begley TP, Downs DM, Ealick SE, McLafferty FW, Van Loon AP, Taylor S, Campobasso N, Chiu HJ, Kinsland C, Reddick JJ, Xi J (1999). "Thiamin biosynthesis in prokaryotes." Arch Microbiol 1999;171(5);293-300. PMID: 10382260

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

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."

Iida97: Iida A., Hayashi M., Fujio T., Teshiba S. (1997). "Molecular cloning, mapping, and sequencing of the thiL gene encoding thiamine-monophosphate kinase in Escherichia coli K-12." Data submission to EMBL/GenBank/DDBJ databases on 1997-08.

Imamura82: Imamura N, Nakayama H (1982). "thiK and thiL loci of Escherichia coli." J Bacteriol 151(2);708-17. PMID: 6284709

McCulloch08: McCulloch KM, Kinsland C, Begley TP, Ealick SE (2008). "Structural studies of thiamin monophosphate kinase in complex with substrates and products." Biochemistry 47(12);3810-21. PMID: 18311927

Nakayama72: Nakayama H, Hayashi R (1972). "Biosynthesis of thiamine pyrophosphate in Escherichia coli." J Bacteriol 109(2);936-8. PMID: 4550824

Nishino72: Nishino H (1972). "Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase." J Biochem (Tokyo) 1972;72(5);1093-100. PMID: 4567662

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Torrents07: Torrents E, Grinberg I, Gorovitz-Harris B, Lundstrom H, Borovok I, Aharonowitz Y, Sjoberg BM, Cohen G (2007). "NrdR controls differential expression of the Escherichia coli ribonucleotide reductase genes." J Bacteriol 189(14);5012-21. PMID: 17496099

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt12b: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 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."

Webb97: Webb E, Downs D (1997). "Characterization of thiL, encoding thiamin-monophosphate kinase, in Salmonella typhimurium." J Biol Chem 272(25);15702-7. PMID: 9188462


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, biocyc13.