MalA

• Description: 6-phospho-alpha-glucosidase
  
  

Gene name	malA
Synonyms	glvG, glvA
Essential	no
Product	6-phospho-alpha-glucosidase
Function	maltose utilization
Metabolic function and regulation of this protein in SubtiPathways: Sugar catabolism
MW, pI	50 kDa, 4.74
Gene length, protein length	1347 bp, 449 aa
Immediate neighbours	yfjA, glvR
Get the DNA and protein sequences (Barbe et al., 2009)
Genetic context This image was kindly provided by SubtiList

The gene

Basic information

• Locus tag: BSU08180

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: Maltose 6'-phosphate + H₂O = D-glucose + D-glucose 6-phosphate (according to Swiss-Prot)

• Protein family: glycosyl hydrolase 4 family (according to Swiss-Prot)

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification:

• Cofactor(s):

• Effectors of protein activity:

• Interactions:

• Localization: membrane associated PubMed

Database entries

• Structure: 1U8X

• UniProt: P54716

• KEGG entry: [3]

• E.C. number: 3.2.1.122

Expression and regulation

• Operon: malA-glvR-malP PubMed

• Sigma factor: SigA PubMed

• Regulation:
  • induction by maltose (GlvR) PubMed
  • repressed by glucose (CcpA) PubMed

• Regulatory mechanism:
  • GlvR: transcription activation PubMed
  • CcpA: transcription repression PubMed

• Additional information:

Biological materials

• Mutant:

• Expression vector:

• lacZ fusion:

• GFP fusion:

• two-hybrid system:

• Antibody:

References

Hannes Hahne, Susanne Wolff, Michael Hecker, Dörte Becher
From complementarity to comprehensiveness--targeting the membrane proteome of growing Bacillus subtilis by divergent approaches.
Proteomics: 2008, 8(19);4123-36
[PubMed:18763711] [WorldCat.org] [DOI] (I p)

Vivian L Y Yip, John Thompson, Stephen G Withers
Mechanism of GlvA from Bacillus subtilis: a detailed kinetic analysis of a 6-phospho-alpha-glucosidase from glycoside hydrolase family 4.
Biochemistry: 2007, 46(34);9840-52
[PubMed:17676871] [WorldCat.org] [DOI] (P p)

Stefan Schönert, Sabine Seitz, Holger Krafft, Eva-Anne Feuerbaum, Iris Andernach, Gabriele Witz, Michael K Dahl
Maltose and maltodextrin utilization by Bacillus subtilis.
J Bacteriol: 2006, 188(11);3911-22
[PubMed:16707683] [WorldCat.org] [DOI] (P p)

Shyamala S Rajan, Xiaojing Yang, Frank Collart, Vivian L Y Yip, Stephen G Withers, Annabelle Varrot, John Thompson, Gideon J Davies, Wayne F Anderson
Novel catalytic mechanism of glycoside hydrolysis based on the structure of an NAD+/Mn2+ -dependent phospho-alpha-glucosidase from Bacillus subtilis.
Structure: 2004, 12(9);1619-29
[PubMed:15341727] [WorldCat.org] [DOI] (P p)

H Yamamoto, M Serizawa, J Thompson, J Sekiguchi
Regulation of the glv operon in Bacillus subtilis: YfiA (GlvR) is a positive regulator of the operon that is repressed through CcpA and cre.
J Bacteriol: 2001, 183(17);5110-21
[PubMed:11489864] [WorldCat.org] [DOI] (P p)

Jonathan Reizer, Steffi Bachem, Aiala Reizer, Maryvonne Arnaud, Milton H Saier, Jörg Stülke
Novel phosphotransferase system genes revealed by genome analysis - the complete complement of PTS proteins encoded within the genome of Bacillus subtilis.
Microbiology (Reading): 1999, 145 ( Pt 12);3419-3429
[PubMed:10627040] [WorldCat.org] [DOI] (P p)

J Thompson, A Pikis, S B Ruvinov, B Henrissat, H Yamamoto, J Sekiguchi
The gene glvA of Bacillus subtilis 168 encodes a metal-requiring, NAD(H)-dependent 6-phospho-alpha-glucosidase. Assignment to family 4 of the glycosylhydrolase superfamily.
J Biol Chem: 1998, 273(42);27347-56
[PubMed:9765262] [WorldCat.org] [DOI] (P p)