Difference between revisions of "Pgi"
Line 119: | Line 119: | ||
=Biological materials = | =Biological materials = | ||
− | * '''Mutant:''' GP508 (spc), available in [[Stülke]] lab | + | * '''Mutant:''' GP508 (spc), available in [[Jörg Stülke]]'s lab, {{PubMed|23420519}} |
* '''Expression vector:''' | * '''Expression vector:''' | ||
− | ** pGP398 (N-terminal His-tag, in [[pWH844]]), available in [[Stülke]] lab | + | ** pGP398 (N-terminal His-tag, in [[pWH844]]), available in [[Jörg Stülke]]'s lab |
− | * '''lacZ fusion:''' pGP510 (in [[pAC6]]), available in [[Stülke]] lab | + | * '''lacZ fusion:''' pGP510 (in [[pAC6]]), available in [[Jörg Stülke]]'s lab |
* '''GFP fusion:''' | * '''GFP fusion:''' | ||
− | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Stülke]] lab | + | * '''two-hybrid system:''' B. pertussis adenylate cyclase-based bacterial two hybrid system ([[BACTH]]), available in [[Jörg Stülke]]'s lab |
* '''Antibody:''' | * '''Antibody:''' | ||
Line 140: | Line 140: | ||
=References= | =References= | ||
− | [http://www.ncbi.nlm.nih.gov/pubmed/ | + | [http://www.ncbi.nlm.nih.gov/pubmed/PubMed] |
− | <pubmed>17218307 19052382 4214896 11489127 4275311 11491085 17218307, </pubmed> | + | <pubmed>17218307 19052382 4214896 23420519 11489127 4275311 11491085 17218307, </pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:01, 13 July 2013
- Description: glucose 6-phosphate isomerase, glycolytic / gluconeogenic enzyme
Gene name | pgi |
Synonyms | yugL |
Essential | no |
Product | glucose-6-phosphate isomerase |
Function | enzyme in glycolysis / gluconeogenesis |
Gene expression levels in SubtiExpress: pgi | |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism, Sugar catabolism | |
MW, pI | 50.4 kDa, 4.85 |
Gene length, protein length | 1353 bp, 451 amino acids |
Immediate neighbours | yugM, yugK |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
carbon core metabolism, phosphoproteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU31350
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: D-glucose 6-phosphate = D-fructose 6-phosphate (according to Swiss-Prot) D-glucose 6-phosphate = D-fructose 6-phosphate
- Protein family: GPI family (according to Swiss-Prot) GPI family
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten PubMed
- Domains:
- Modification: phosphorylation on Thr-39 PubMed
- Cofactor(s):
- Effectors of protein activity: competitively inhibited by 6-phosphogluconate (in B.caldotenax, B.stearothermophilus) PubMed
- Localization:
- cytoplasm (according to Swiss-Prot), cytoplasm
Database entries
- UniProt: P80860
- KEGG entry: [3]
- E.C. number: 5.3.1.9
Additional information
- extensive information on the structure and enzymatic properties of Pgi can be found at Proteopedia
Expression and regulation
- Regulation: constitutively expressed PubMed
- Additional information:
Biological materials
- Mutant: GP508 (spc), available in Jörg Stülke's lab, PubMed
- Expression vector:
- pGP398 (N-terminal His-tag, in pWH844), available in Jörg Stülke's lab
- lacZ fusion: pGP510 (in pAC6), available in Jörg Stülke's lab
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
- Antibody:
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany homepage
Your additional remarks
References
Fabian M Commichau, Nico Pietack, Jörg Stülke
Essential genes in Bacillus subtilis: a re-evaluation after ten years.
Mol Biosyst: 2013, 9(6);1068-75
[PubMed:23420519]
[WorldCat.org]
[DOI]
(I p)
Yian Liang Lee, TienHsiung Thomas Li
Crystallization and preliminary crystallographic study of the phosphoglucose isomerase from Bacillus subtilis.
Acta Crystallogr Sect F Struct Biol Cryst Commun: 2008, 64(Pt 12);1181-3
[PubMed:19052382]
[WorldCat.org]
[DOI]
(I p)
Boris Macek, Ivan Mijakovic, Jesper V Olsen, Florian Gnad, Chanchal Kumar, Peter R Jensen, Matthias Mann
The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis.
Mol Cell Proteomics: 2007, 6(4);697-707
[PubMed:17218307]
[WorldCat.org]
[DOI]
(P p)
J Stülke, I Martin-Verstraete, P Glaser, G Rapoport
Characterization of glucose-repression-resistant mutants of Bacillus subtilis: identification of the glcR gene.
Arch Microbiol: 2001, 175(6);441-9
[PubMed:11491085]
[WorldCat.org]
[DOI]
(P p)
H Ludwig, G Homuth, M Schmalisch, F M Dyka, M Hecker, J Stülke
Transcription of glycolytic genes and operons in Bacillus subtilis: evidence for the presence of multiple levels of control of the gapA operon.
Mol Microbiol: 2001, 41(2);409-22
[PubMed:11489127]
[WorldCat.org]
[DOI]
(P p)
J Y Lin, C Prasad
Selection of a mutant of Bacillus subtilis deficient in glucose-6-phosphate dehydrogenase and phosphoglucoisomerase.
J Gen Microbiol: 1974, 83(2);419-21
[PubMed:4214896]
[WorldCat.org]
[DOI]
(P p)
C Prasad, E Freese
Cell lysis of Bacillus subtilis caused by intracellular accumulation of glucose-1-phosphate.
J Bacteriol: 1974, 118(3);1111-22
[PubMed:4275311]
[WorldCat.org]
[DOI]
(P p)