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
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Contents
Categories containing this gene/protein
utilization of specific carbon sources, membrane proteins
This gene is a member of the following regulons
The gene
Basic information
- Locus tag: BSU08180
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
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
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Yang M Ming, Zhang W Wei, Chen Y Lin, Gong Y Sheng
Development of a Bacillus subtilis expression system using the improved Pglv promoter.
Microb Cell Fact: 2010, 9;55
[PubMed:20618987]
[WorldCat.org]
[DOI]
(I e)
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)
