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discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
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discounted EARLY registration ends Dec 31, 2014
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MetaCyc Enzyme: ThiG

Gene: thiG Accession Numbers: EG11589 (MetaCyc), b3991, ECK3982

Synonyms: thiB

Species: Escherichia coli K-12 substr. MG1655

Component of:
thiazole synthase (summary available)
thiazole synthase (summary available)

Summary:
ThiG is involved in the synthesis of the thiazole moiety of thiamin. Thiazole synthase is a heterodimer of ThiG and ThiH, which catalyzes the conversion of 1-deoxy-D-xylulose 5-phosphate to a thiazole. [Leonardi03] ThiG and ThiH complex is required for the synthesis of 4-methyl-5-(beta-hydroxylethyl) thiazole phosphate, which is the rate-limiting step in thiamine synthesis. The formation of 4-methyl-5-(-hydroxyethyl)thiazole phosphate requires the precursor 1-deoxyxyulose 5-phosphate, a sulfur atom from cysteine which is transferred via ThiS, and dehydroglycine. [Vander93, Leonardi04, Dorrestein04]

ThiG and ThiH copurify as a large multimeric non-covalent complex. ThiG catalyzes the thiazole cyclization reaction and ThiH is a tyrosine lyase that cleaves tyrosine to form dehydroglycine. The activity of thiazole phosphate forming reaction using purified protein components required four proteins isolated as heterodimers, ThiGH and ThiFS. Experimental evidence indicated a presence of an iron-sulfur cluster within this complex and that the S-adenosylmethionine (AdoMet) bound this cluster. [Kriek07, Leonardi03]

Locations: cytosol

Map Position: [4,189,888 <- 4,190,658]

Molecular Weight of Polypeptide: 26.896 kD (from nucleotide sequence), 26.9 kD (experimental) [Kelleher98 ]

pI: 8.59

Unification Links: ASAP:ABE-0013050 , CGSC:34295 , DIP:DIP-6868N , EchoBASE:EB1547 , EcoGene:EG11589 , EcoliWiki:b3991 , Mint:MINT-1289283 , ModBase:P30139 , OU-Microarray:b3991 , PortEco:thiG , PR:PRO_000024056 , Protein Model Portal:P30139 , RefSeq:NP_418418 , RegulonDB:EG11589 , SMR:P30139 , String:511145.b3991 , Swiss-Model:P30139 , UniProt:P30139

Relationship Links: InterPro:IN-FAMILY:IPR008867 , InterPro:IN-FAMILY:IPR013785 , Pfam:IN-FAMILY:PF05690

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009228 - thiamine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Vander93]
GO:0009229 - thiamine diphosphate biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Leonardi03]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0016740 - transferase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016783 - sulfurtransferase activity Inferred by computational analysis [GOA06]
GO:0036355 - 2-iminoacetate synthase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

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

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


Enzymatic reaction of: ThiG

EC Number: 2.8.1.10

1-deoxy-D-xylulose 5-phosphate + 2-iminoacetate + a thiocarboxy-adenylated-[ThiS-Protein] <=> 2-[(2R,5Z)-(2-carboxy-4-methylthiazol-5(2H)-ylidene]ethyl phosphate + a ThiS sulfur-carrier protein + 2 H2O

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 , thiazole biosynthesis I (E. coli)

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


Subunit of: thiazole synthase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of thiazole synthase = [ThiG][ThiH]
         tyrosine lyase = ThiH (extended summary available)

Component of: thiazole synthase (summary available)

Summary:
The ThiGH complex catalyzes the conversion of 1-deoxy-D-xylulose 5-phosphate to a thiazole as part of thiamine synthesis.

ThiG and ThiH combine to form a complex containing an iron-sulfuer cluster [Leonardi03]. Together, they are required for the synthesis of 4-methyl-5-(β-hydroxyethyl)thiazole phosphate, which is the rate-limiting step in thiamine synthesis [Vander93, Leonardi04].

Molecular Weight: 440 kD (experimental) [Leonardi03]

Credits:
Created in EcoCyc 15-Mar-2006 by Shearer A , SRI International
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Subunit of: thiazole synthase

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of thiazole synthase = [(ThiG)(ThiH)]6
         thiazole synthase = (ThiG)(ThiH)
                 tyrosine lyase = ThiH (extended summary available)

Summary:
The ThiGH complex catalyzes the conversion of 1-deoxy-D-xylulose 5-phosphate to a thiazole as part of thiamine synthesis.

ThiG and ThiH combine to form a complex containing an iron-sulfuer cluster [Leonardi03]. Together, they are required for the synthesis of 4-methyl-5-(β-hydroxyethyl)thiazole phosphate, which is the rate-limiting step in thiamine synthesis [Vander93, Leonardi04].

Molecular Weight: 440.0 kD (experimental) [Challand10]

Credits:
Created 15-Mar-2010 by Caspi R , SRI International


Sequence Features

Feature Class Location Citations Comment
Active-Site 95
[UniProt10a]
UniProt: Schiff-base intermediate with DXP; Non-Experimental Qualifier: by similarity;
Amino-Acid-Sites-That-Bind 156
[UniProt10a]
UniProt: DXP; via amide nitrogen; Non-Experimental Qualifier: by similarity;
Protein-Segment 182 -> 183
[UniProt10a]
UniProt: DXP binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;
Protein-Segment 204 -> 205
[UniProt10a]
UniProt: DXP binding; Sequence Annotation Type: region of interest; Non-Experimental Qualifier: by similarity;

History:
Suzanne Paley on Thu Oct 21, 2004:
Position updated based on U00096.2 release of genome
10/20/97 Gene b3991 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11589; confirmed by SwissProt match.


References

Challand10: Challand MR, Martins FT, Roach PL (2010). "Catalytic activity of the anaerobic tyrosine lyase required for thiamine biosynthesis in Escherichia coli." J Biol Chem 285(8);5240-8. PMID: 19923213

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

Dorrestein04: Dorrestein PC, Zhai H, McLafferty FW, Begley TP (2004). "The biosynthesis of the thiazole phosphate moiety of thiamin: the sulfur transfer mediated by the sulfur carrier protein ThiS." Chem Biol 11(10);1373-81. PMID: 15489164

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."

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

Kelleher98: Kelleher NL, Taylor SV, Grannis D, Kinsland C, Chiu HJ, Begley TP, McLafferty FW (1998). "Efficient sequence analysis of the six gene products (7-74 kDa) from the Escherichia coli thiamin biosynthetic operon by tandem high-resolution mass spectrometry." Protein Sci 7(8);1796-801. PMID: 10082377

Kriek07: Kriek M, Martins F, Leonardi R, Fairhurst SA, Lowe DJ, Roach PL (2007). "Thiazole synthase from Escherichia coli: an investigation of the substrates and purified proteins required for activity in vitro." J Biol Chem 282(24);17413-23. PMID: 17403671

Leonardi03: Leonardi R, Fairhurst SA, Kriek M, Lowe DJ, Roach PL (2003). "Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex." FEBS Lett 539(1-3);95-9. PMID: 12650933

Leonardi04: Leonardi R, Roach PL (2004). "Thiamine biosynthesis in Escherichia coli: in vitro reconstitution of the thiazole synthase activity." J Biol Chem 279(17);17054-62. PMID: 14757766

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

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 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."

Vander93: Vander Horn PB, Backstrom AD, Stewart V, Begley TP (1993). "Structural genes for thiamine biosynthetic enzymes (thiCEFGH) in Escherichia coli K-12." J Bacteriol 1993;175(4);982-92. PMID: 8432721


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 Sat Dec 20, 2014, biocyc14.