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MetaCyc Enzyme: phosphoglucosamine mutase

Gene: glmM Accession Numbers: EG11553 (MetaCyc), b3176, ECK3165

Synonyms: yhbF, mrsA

Species: Escherichia coli K-12 substr. MG1655

Summary:
Phosphoglucosamine mutase catalyzes the interconversion of the glucosamine-6-phosphate (GlcN-6-P) and glucosamine-1-phosphate (GlcN-1-P) isomers.

The enzyme is active only in phosphorylated form [Jolly99]; it can autophosphorylate in vitro in the presence of ATP to a low level [Jolly00]. The modified amino acid is the serine residue S102 [Jolly99, Jolly00]. Only approximately 5% of GlmM protein purified from wild-type cells is phosphorylated, but this may be an artifact of the purification procedure [Jolly99]. When analyzed by gel filtration, the protein behaves as a trimer at pH 8.4; the degree of aggregation increases at pH 7.4 [Jolly99].

The phosphoglucosamine mutase reaction follows a ping-pong bi-bi mechanism, where glucosamine-1,6-diphosphate acts as both the first product and the second substrate [Jolly99]. Once the enzyme is phosphorylated, it no longer requires glucosamine-1,6-diphosphate as a cofactor [Jolly99]. The in vivo mechanism of activation/phosphorylation of the enzyme is still unclear.

When shifted to the restrictive temperature, conditional glmM mutant cells lose their rod shape and stop growth [MenginLecreulx96].

GlmM: "glucosamine mutase" [MenginLecreulx96]

Locations: cytosol

Map Position: [3,320,755 <- 3,322,092]

Molecular Weight of Polypeptide: 47.544 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0010439 , CGSC:38690 , DIP:DIP-10260N , EchoBASE:EB1514 , EcoGene:EG11553 , EcoliWiki:b3176 , ModBase:P31120 , OU-Microarray:b3176 , PortEco:glmM , PR:PRO_000022780 , Pride:P31120 , Protein Model Portal:P31120 , RefSeq:NP_417643 , RegulonDB:EG11553 , SMR:P31120 , String:511145.b3176 , UniProt:P31120

Relationship Links: InterPro:IN-FAMILY:IPR005841 , InterPro:IN-FAMILY:IPR005843 , InterPro:IN-FAMILY:IPR005844 , InterPro:IN-FAMILY:IPR005845 , InterPro:IN-FAMILY:IPR005846 , InterPro:IN-FAMILY:IPR006352 , InterPro:IN-FAMILY:IPR016055 , InterPro:IN-FAMILY:IPR016066 , Pfam:IN-FAMILY:PF00408 , Pfam:IN-FAMILY:PF02878 , Pfam:IN-FAMILY:PF02879 , Pfam:IN-FAMILY:PF02880 , Prints:IN-FAMILY:PR00509 , Prosite:IN-FAMILY:PS00710

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006048 - UDP-N-acetylglucosamine biosynthetic process Inferred from experiment [MenginLecreulx96]
GO:0046777 - protein autophosphorylation Inferred from experiment [Jolly00]
GO:0005975 - carbohydrate metabolic process Inferred by computational analysis [GOA01a]
GO:0071704 - organic substance metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0008966 - phosphoglucosamine mutase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Jolly99]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06, GOA01a]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016868 - intramolecular transferase activity, phosphotransferases Inferred by computational analysis [GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05, Gaudet10]
GO:0005737 - cytoplasm

MultiFun Terms: cell structure murein
cell structure surface antigens (ECA, O antigen of LPS)
metabolism biosynthesis of macromolecules (cellular constituents) enterobacterial common antigen (surface glycolipid)
metabolism biosynthesis of macromolecules (cellular constituents) lipopolysaccharide O antigen
metabolism biosynthesis of macromolecules (cellular constituents) murein (peptidoglycan)
metabolism central intermediary metabolism amino sugar conversions

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International


Enzymatic reaction of: phosphoglucosamine mutase

EC Number: 5.4.2.10

D-glucosamine 6-phosphate <=> D-glucosamine 1-phosphate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

This reaction is reversible.

Alternative Substrates for D-glucosamine 1-phosphate: α-D-glucopyranose 1-phosphate [Jolly99 ]

Alternative Substrates for D-glucosamine 6-phosphate: β-D-glucose 6-phosphate [Jolly99 ]

In Pathways: superpathway of UDP-N-acetylglucosamine-derived O-antigen building blocks biosynthesis , O-antigen building blocks biosynthesis (E. coli) , UDP-N-acetyl-D-glucosamine biosynthesis I , anhydromuropeptides recycling

Credits:
Imported from EcoCyc 02-Jun-2015 by Paley S , SRI International

Summary:
When assayed under conditions that did not involve coupled enzymes that utilized the products of the reaction, the enzyme, no formation of GlcN-1-P from GlcN-6-P could be detected, and only 10% of GlcN-1-P was converted to GlcN-6-P [Jolly99].

Formation of glucose-6-phosphate from glucose-1-phosphate in the presence of glucose-1,6-diphosphate occurs at a rate 1400-fold lower than the rate when utilizing the glucosamine substrates [Jolly99].

Cofactors or Prosthetic Groups: glucosamine 1,6-diphosphate [Jolly99]

Kinetic Parameters:

Substrate
Km (μM)
kcat (sec-1)
kcat/Km (sec-1 μM-1)
Citations
D-glucosamine 6-phosphate
50.0
2.42, 7.9
0.048, 0.16
[Jolly99, BRENDA14]
D-glucosamine 1-phosphate
80.0
[Jolly99, BRENDA14]


Sequence Features

Feature Class Location Common Name Citations Comment
Cleavage-of-Initial-Methionine 1  
[MenginLecreulx96]
 
Chain 2 -> 445  
[UniProt09]
UniProt: Phosphoglucosamine mutase;
Sequence-Conflict 69  
[Wang93b, UniProt10]
UniProt: (in Ref. 2; AAA97510);
Mutagenesis-Variant 100  
[Jolly99, UniProt11]
[Jolly99, UniProt11]
A: 2% of wild-type activity.
T: 20-fold increase in the non- specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated).
Mutagenesis-Variant 102  
[Jolly99, UniProt11]
UniProt: Loss of activity in the absence or presence of glucosamine-1,6-diP.
Active-Site 102  
[Jolly00, UniProt11]
UniProt: Phosphoserine intermediate.
Metal-Binding-Site 102  
[UniProt10a]
UniProt: Magnesium; via phosphate group; Non-Experimental Qualifier: by similarity;
Phosphorylation-Modification 102 phosphorylated residue
[Jolly99]
 
Sequence-Conflict 162  
[Wang93b, UniProt10]
UniProt: (in Ref. 2; AAA97510);
Sequence-Conflict 167  
[Wang93b, UniProt10]
UniProt: (in Ref. 2; AAA97510);
Sequence-Conflict 178 -> 181  
[Wang93b, UniProt10]
UniProt: (in Ref. 2; AAA97510);
Metal-Binding-Site 241  
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 243  
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 245  
[UniProt10a]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Acetylation-Modification 314  
[Yu08]
 
Sequence-Conflict 411  
[Wang93b, UniProt10]
UniProt: (in Ref. 2; AAA97510);
Sequence-Conflict 417  
[Wang93b, UniProt10]
UniProt: (in Ref. 2; AAA97510);

History:
2/26/1998 (pkarp) Merged genes GLMM/GLMM and EG11553/mrsA


References

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

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

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."

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

Jolly00: Jolly L, Pompeo F, van Heijenoort J, Fassy F, Mengin-Lecreulx D (2000). "Autophosphorylation of phosphoglucosamine mutase from Escherichia coli." J Bacteriol 2000;182(5);1280-5. PMID: 10671448

Jolly99: Jolly L, Ferrari P, Blanot D, Van Heijenoort J, Fassy F, Mengin-Lecreulx D (1999). "Reaction mechanism of phosphoglucosamine mutase from Escherichia coli." Eur J Biochem 262(1);202-10. PMID: 10231382

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

MenginLecreulx96: Mengin-Lecreulx D, van Heijenoort J (1996). "Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli." J Biol Chem 1996;271(1);32-9. PMID: 8550580

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.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wang93b: Wang R., Kushner S.R. (1993). Data submission to EMBL/GenBank/DDBJ databases on 1993-09.

Yu08: Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG (2008). "The diversity of lysine-acetylated proteins in Escherichia coli." J Microbiol Biotechnol 18(9);1529-36. PMID: 18852508


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 19.0 on Mon Aug 3, 2015, BIOCYC14A.