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Escherichia coli K-12 substr. MG1655 Enzyme: UDP-galactopyranose mutase



Gene: glf Accession Numbers: EG11981 (EcoCyc), b2036, ECK2030

Synonyms: yefE

Regulation Summary Diagram: ?

Summary:
UDP-D-galactopyranose mutase catalyzes the reversible interconversion of UDP-galactopyranose and UDP-galactofuranose [Nassau96]. UDP-galactofuranose is required for repeat-unit synthesis in O antigen biosynthesis [Stevenson94].

When the rfb-50 mutation, an IS5 insertion in the gene encoding rhamnosyl transferase, wbbL, is complemented with a wild type wbbL gene, E. coli K-12 produces the O16 variant of O antigen, with a β-D-galactofuranosyl moiety in the repeating unit [Stevenson94].

The reaction mechanism of UDP-D-galactopyranose mutase has been studied, and it was shown that FAD plays an active role in regulating catalysis [Zhang01]. Studies using deaza-FAD analogs support a radical mechanism for catalysis [Huang03].

A crystal structure of the enzyme has been solved at 2.4 Å resolution [Sanders01].

Citations: [Lee96]

Locations: cytosol

Map Position: [2,105,250 <- 2,106,353] (45.37 centisomes)
Length: 1104 bp / 367 aa

Molecular Weight of Polypeptide: 42.966 kD (from nucleotide sequence), 42.9 kD (experimental) [Nassau96 ]

Unification Links: ASAP:ABE-0006755 , DIP:DIP-6863N , EchoBASE:EB1924 , EcoGene:EG11981 , EcoliWiki:b2036 , Mint:MINT-1308638 , ModBase:P37747 , OU-Microarray:b2036 , PortEco:glf , PR:PRO_000022775 , Pride:P37747 , Protein Model Portal:P37747 , RefSeq:NP_416540 , RegulonDB:EG11981 , SMR:P37747 , String:511145.b2036 , UniProt:P37747

Relationship Links: InterPro:IN-FAMILY:IPR004379 , InterPro:IN-FAMILY:IPR015899 , InterPro:IN-FAMILY:IPR016040 , Panther:IN-FAMILY:PTHR21197 , PDB:Structure:1I8T , Pfam:IN-FAMILY:PF03275

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0009103 - lipopolysaccharide biosynthetic process Inferred by computational analysis [UniProtGOA12, UniProtGOA11a]
GO:0009243 - O antigen biosynthetic process
Molecular Function: GO:0008767 - UDP-galactopyranose mutase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Nassau96]
GO:0050660 - flavin adenine dinucleotide binding Inferred from experiment [Nassau96]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]

MultiFun Terms: cell structure murein
cell structure surface antigens (ECA, O antigen of LPS)
metabolism biosynthesis of macromolecules (cellular constituents) lipopolysaccharide O antigen

Credits:
Last-Curated ? 05-Jan-2007 by Keseler I , SRI International


Enzymatic reaction of: UDP-galactopyranose mutase

Synonyms: UDP-D-galactopyranose furanomutase

EC Number: 5.4.99.9

UDP-α-D-galactose <=> UDP-α-D-galactofuranose

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible.

In Pathways: O-antigen building blocks biosynthesis (E. coli)

Summary:
The equilibrium constant for the reversible reaction is 0.057 in the forward direction, i.e. the enzyme has a preference for the pyranose product. The catalytic efficiency is increased by reducing the FAD coenzyme [Zhang00].

Cofactors or Prosthetic Groups: FAD [Comment 1, Nassau96]

Inhibitors (Irreversible): UDP-[3-F]galactofuranose [Zhang01]

Kinetic Parameters:

Substrate
Km (μM)
Citations
UDP-α-D-galactofuranose
22.0
[Zhang01]


Sequence Features

Feature Class Location Attached Group Citations Comment
Amino-Acid-Sites-That-Bind 12  
[UniProt13]
UniProt: FAD; via amide nitrogen.
Nucleotide-Phosphate-Binding-Region 31 -> 32 FAD
[UniProt14]
UniProt: FAD.
Amino-Acid-Sites-That-Bind 39  
[UniProt13]
UniProt: FAD; via amide nitrogen.
Nucleotide-Phosphate-Binding-Region 56 -> 57 FAD
[UniProt14]
UniProt: FAD.
Amino-Acid-Sites-That-Bind 80  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 151  
[Sanders01, UniProt13]
Alternate sequence: Y → F; UniProt: 3-fold decrease in the mutase activity.
Amino-Acid-Sites-That-Bind 152  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 156  
[Sanders01, UniProt13]
Alternate sequence: W → Y; UniProt: 2-fold decrease in the mutase activity.
Alternate sequence: W → A; UniProt: Loss of mutase activity.
Amino-Acid-Sites-That-Bind 156  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 181  
[Sanders01, UniProt13]
Alternate sequence: Y → F; UniProt: Increase in the mutase activity.
Amino-Acid-Sites-That-Bind 181  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 212 -> 213 FAD
[UniProt14]
UniProt: FAD.
Amino-Acid-Sites-That-Bind 268  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 278  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 311  
[Sanders01, UniProt13]
Alternate sequence: Y → F; UniProt: Loss of mutase activity.
Amino-Acid-Sites-That-Bind 311  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Amino-Acid-Sites-That-Bind 340  
[UniProt13]
UniProt: FAD; Non-Experimental Qualifier: by similarity.
Mutagenesis-Variant 346  
[Sanders01, UniProt13]
Alternate sequence: Y → F; UniProt: Loss of mutase activity.
Amino-Acid-Sites-That-Bind 346  
[UniProt13]
UniProt: UDP-GalP; Non-Experimental Qualifier: by similarity.
Nucleotide-Phosphate-Binding-Region 347 -> 352 FAD
[UniProt14]
UniProt: FAD.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b2036 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11981; confirmed by SwissProt match.


References

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, 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."

Huang03: Huang Z, Zhang Q, Liu HW (2003). "Reconstitution of UDP-galactopyranose mutase with 1-deaza-FAD and 5-deaza-FAD: analysis and mechanistic implications." Bioorg Chem 31(6);494-502. PMID: 14613770

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

Lee96: Lee R, Monsey D, Weston A, Duncan K, Rithner C, McNeil M (1996). "Enzymatic synthesis of UDP-galactofuranose and an assay for UDP-galactopyranose mutase based on high-performance liquid chromatography." Anal Biochem 242(1);1-7. PMID: 8923956

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

Nassau96: Nassau PM, Martin SL, Brown RE, Weston A, Monsey D, McNeil MR, Duncan K (1996). "Galactofuranose biosynthesis in Escherichia coli K-12: identification and cloning of UDP-galactopyranose mutase." J Bacteriol 1996;178(4);1047-52. PMID: 8576037

Sanders01: Sanders DA, Staines AG, McMahon SA, McNeil MR, Whitfield C, Naismith JH (2001). "UDP-galactopyranose mutase has a novel structure and mechanism." Nat Struct Biol 8(10);858-63. PMID: 11573090

Stevenson94: Stevenson G, Neal B, Liu D, Hobbs M, Packer NH, Batley M, Redmond JW, Lindquist L, Reeves P (1994). "Structure of the O antigen of Escherichia coli K-12 and the sequence of its rfb gene cluster." J Bacteriol 1994;176(13);4144-56. PMID: 7517391

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

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

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."

Zhang00: Zhang Q, Liu HW (2000). "Studies of UDP-Galactopyranose Mutase from Escherichia coli: An Unusual Role of reduced FAD in Its Catalysis." J Am Chem Soc 122;9065-9070.

Zhang01: Zhang Q, Liu H (2001). "Mechanistic investigation of UDP-galactopyranose mutase from Escherichia coli using 2- and 3-fluorinated UDP-galactofuranose as probes." J Am Chem Soc 123(28);6756-66. PMID: 11448178


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 Sun Dec 21, 2014, BIOCYC14A.