Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
twitter

Escherichia coli K-12 substr. MG1655 Enzyme: phosphoglucosamine mutase



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

Synonyms: yhbF, mrsA

Regulation Summary Diagram: ?

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] (71.57 centisomes)
Length: 1338 bp / 445 aa

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

In Paralogous Gene Group: 179 (3 members)

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 [GOA01]
Molecular Function: GO:0008966 - phosphoglucosamine mutase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01a, GOA01, Jolly99]
GO:0000287 - magnesium ion binding Inferred by computational analysis [GOA06, GOA01]
GO:0016853 - isomerase activity Inferred by computational analysis [UniProtGOA11]
GO:0016868 - intramolecular transferase activity, phosphotransferases Inferred by computational analysis [GOA01]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
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

Essentiality data for glmM 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 No 37 Aerobic 7   No [Baba06, Yamamoto09]

Credits:
Last-Curated ? 03-Oct-2007 by Keseler I , SRI International


Enzymatic reaction of: phosphoglucosamine mutase

EC Number: 5.4.2.10

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

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.

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

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

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

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
[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  
[Wang93e, UniProt10a]
Alternate sequence: A → R; UniProt: (in Ref. 2; AAA97510);
Mutagenesis-Variant 100  
[Jolly99, UniProt11]
Alternate sequence: S → T; UniProt: 20-fold increase in the non- specific phosphoglucomutase activity towards glucose-phosphate substrates (non aminated).
Alternate sequence: S → A; UniProt: 2% of wild-type activity.
Mutagenesis-Variant 102  
[Jolly99, UniProt11]
Alternate sequence: S → A; 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  
[UniProt10]
UniProt: Magnesium; via phosphate group; Non-Experimental Qualifier: by similarity;
Phosphorylation-Modification 102 phosphorylated residue
[Jolly00, Jolly99]
 
Sequence-Conflict 162  
[Wang93e, UniProt10a]
Alternate sequence: C → S; UniProt: (in Ref. 2; AAA97510);
Sequence-Conflict 167  
[Wang93e, UniProt10a]
Alternate sequence: P → R; UniProt: (in Ref. 2; AAA97510);
Sequence-Conflict 178 -> 181  
[Wang93e, UniProt10a]
Alternate sequence: VVDC → LVIG; UniProt: (in Ref. 2; AAA97510);
Metal-Binding-Site 241  
[UniProt10]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 243  
[UniProt10]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 245  
[UniProt10]
UniProt: Magnesium; Non-Experimental Qualifier: by similarity;
Acetylation-Modification 314  
[Yu08]
 
Sequence-Conflict 411  
[Wang93e, UniProt10a]
Alternate sequence: R → C; UniProt: (in Ref. 2; AAA97510);
Sequence-Conflict 417  
[Wang93e, UniProt10a]
Alternate sequence: P → R; UniProt: (in Ref. 2; AAA97510);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

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


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

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

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."

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 2010-07 released on 2010-06-15 00:00:00." Database.

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

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

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Wang93e: Wang R., Kushner S.R. (1993). Data submission to EMBL/GenBank/DDBJ databases on 1993-09.

Yamamoto09: Yamamoto N, Nakahigashi K, Nakamichi T, Yoshino M, Takai Y, Touda Y, Furubayashi A, Kinjyo S, Dose H, Hasegawa M, Datsenko KA, Nakayashiki T, Tomita M, Wanner BL, Mori H (2009). "Update on the Keio collection of Escherichia coli single-gene deletion mutants." Mol Syst Biol 5;335. PMID: 20029369

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 EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Sun Nov 23, 2014, biocyc14.