RegulonDB RegulonDB 10.9: Gene Form
   

malQ gene in Escherichia coli K-12 genome


Gene local context to scale (view description)

malP malQ gntT malQp malQp TSS_4013 TSS_4013

Gene      
Name: malQ    Texpresso search in the literature
Synonym(s): ECK3403, EG10561, b3416, malA
Genome position(nucleotides): 3547986 <-- 3550070 Genome Browser
Strand: reverse
Sequence: Get nucleotide sequence FastaFormat
GC content %:  
55.16
External database links:  
ASAP:
ABE-0011151
CGSC:
527
ECHOBASE:
EB0556
ECOLIHUB:
malQ
OU-MICROARRAY:
b3416
STRING:
511145.b3416
COLOMBOS: malQ


Product      
Name: 4-α-glucanotransferase
Synonym(s): MalA, MalQ, amylomaltase
Sequence: Get amino acid sequence Fasta Format
Cellular location: cytosol
Molecular weight: 78.503
Isoelectric point: 6.561
Motif(s):
 
Type Positions Sequence
22 -> 22 A
462 -> 462 G
148 -> 664 VQLYTLRSEKNWGIGDFGDLKAMLVDVAKRGGSFIGLNPIHALYPANPESASPYSPSSRRWLNVIYIDVNAVEDFHLSEEAQAWWQLPTTQQTLQQARDADWVDYSTVTALKMTALRMAWKGFAQRDDEQMAAFRQFVAEQGDSLFWQAAFDALHAQQVKEDEMRWGWPAWPEMYQNVDSPEVRQFCEEHRDDVDFYLWLQWLAYSQFAACWEISQGYEMPIGLYRDLAVGVAEGGAETWCDRELYCLKASVGAPPDILGPLGQNWGLPPMDPHIITARAYEPFIELLRANMQNCGALRIDHVMSMLRLWWIPYGETADQGAYVHYPVDDLLSILALESKRHRCMVIGEDLGTVPVEIVGKLRSSGVYSYKVLYFENDHEKTFRAPKAYPEQSMAVAATHDLPTLRGYWECGDLTLGKTLGLYPDEVVLRGLYQDRELAKQGLLDALHKYGCLPKRAGHKASLMSMTPTLNRGLQRYIADSNSALLGLQPEDWLDMAEPVNIPGTSYQYKNWRRKLS
380 -> 381 AE
199 -> 200 SP

 

Classification:
Multifun Terms (GenProtEC)  
  1 - metabolism --> 1.1 - carbon utilization --> 1.1.1 - carbon compounds
  1 - metabolism --> 1.2 - degradation of macromolecules --> 1.2.4 - polysaccharides
Gene Ontology Terms (GO)  
cellular_component GO:0005737 - cytoplasm
GO:0005829 - cytosol
molecular_function GO:0102500 - beta-maltose 4-alpha-glucanotransferase activity
GO:0016757 - transferase activity, transferring glycosyl groups
GO:0016740 - transferase activity
GO:0004134 - 4-alpha-glucanotransferase activity
biological_process GO:0005975 - carbohydrate metabolic process
GO:0000025 - maltose catabolic process
GO:0005978 - glycogen biosynthetic process
GO:0005980 - glycogen catabolic process
Note(s): Note(s): ...[more].
Reference(s): [1] Bloch MA., et al., 1986
[2] Brunkhorst C., et al., 1999
[3] Bukau B., et al., 1986
[4] Burger M., et al., 1964
[5] Chao J., et al., 1974
[6] Cohen-Bazire G., et al., 1953
[7] Decker K., et al., 1993
[8] Dippel R., et al., 2005
[9] Ehrmann M., et al., 1987
[10] Granett S., et al., 1981
[11] Guidi-Rontani C., et al., 1980
[12] Gutierrez C., et al., 1985
[13] Hatfield D., et al., 1969
[14] Lu Y., et al., 2006
[15] Macaskie LE., et al., 1978
[16] Palmer TN., et al., 1976
[17] Pavlasova E. 1967
[18] Pavlasova E., et al., 1967
[19] Pavlasova E., et al., 1980
[20] Pugsley AP., et al., 1988
[21] Raibaud O., et al., 1985
[22] Raibaud O., et al., 1980
[23] Ronen A., et al., 1971
[24] Ruzanski C., et al., 2013
[25] Schwinn H., et al., 1971
External database links:  
CAZY:
GH77
DIP:
DIP-10147N
ECOCYC:
AMYLOMALT-MONOMER
ECOLIWIKI:
b3416
INTERPRO:
IPR003385
INTERPRO:
IPR017853
MODBASE:
P15977
PANTHER:
PTHR32438
PDB:
4S3R
PDB:
4S3Q
PDB:
4S3P
PFAM:
PF02446
PRIDE:
P15977
PRODB:
PRO_000023153
REFSEQ:
NP_417875
SMR:
P15977
UNIPROT:
P15977


Operon      
Name: malPQ         
Operon arrangement:
Transcription unit        Promoter
malQ
malPQ


Transcriptional Regulation      
Display Regulation             
Activated by: FNR, MalT


Elements in the selected gene context region unrelated to any object in RegulonDB      

  Type Name Post Left Post Right Strand Notes Evidence (Confirmed, Strong, Weak) References
  promoter TSS_4013 3547786 forward nd [RS-EPT-CBR] [26]


Evidence    

 [RS-EPT-CBR] RNA-seq using two enrichment strategies for primary transcripts and consistent biological replicates



Reference(s)    

 [1] Bloch MA., Raibaud O., 1986, Comparison of the malA regions of Escherichia coli and Klebsiella pneumoniae., J Bacteriol 168(3):1220-7

 [2] Brunkhorst C., Andersen C., Schneider E., 1999, Acarbose, a pseudooligosaccharide, is transported but not metabolized by the maltose-maltodextrin system of Escherichia coli., J Bacteriol 181(8):2612-9

 [3] Bukau B., Ehrmann M., Boos W., 1986, Osmoregulation of the maltose regulon in Escherichia coli., J Bacteriol 166(3):884-91

 [4] Burger M., Pavlasova E., 1964, Change in the location of amylomaltase produced by mutation in Escherichia coli., Biochem J 93(3):601-6

 [5] Chao J., Weathersbee CJ., 1974, Regulation of maltodextrin phosphorylase synthesis in Escherichia coli by cyclic adenosine 3', 5'-monophosphate and glucose., J Bacteriol 117(1):181-8

 [6] Cohen-Bazire G., Jolit M., 1953, [Selective isolation of Escherichia coli mutants which synthesize simultaneously amylomaltase and beta-galactosidase]., Ann Inst Pasteur (Paris) 84(5):937-45

 [7] Decker K., Peist R., Reidl J., Kossmann M., Brand B., Boos W., 1993, Maltose and maltotriose can be formed endogenously in Escherichia coli from glucose and glucose-1-phosphate independently of enzymes of the maltose system., J Bacteriol 175(17):5655-65

 [8] Dippel R., Bergmiller T., Bohm A., Boos W., 2005, The maltodextrin system of Escherichia coli: glycogen-derived endogenous induction and osmoregulation., J Bacteriol 187(24):8332-9

 [9] Ehrmann M., Boos W., 1987, Identification of endogenous inducers of the mal regulon in Escherichia coli., J Bacteriol 169(8):3539-45

 [10] Granett S., Villarejo M., 1981, Selective inhibition of carbohydrate transport by the local anesthetic procaine in Escherichia coli., J Bacteriol 147(2):289-96

 [11] Guidi-Rontani C., Danchin A., Ullmann A., 1980, Catabolite repression in Escherichia coli mutants lacking cyclic AMP receptor protein., Proc Natl Acad Sci U S A 77(10):5799-801

 [12] Gutierrez C., Chapon C., Schwartz M., 1985, Indirect effects of the 3'-5' cyclic adenosine monophosphate binding protein (CAP) on the transcription of the malPQ operon in Escherichia coli., Biochimie 67(1):145-8

 [13] Hatfield D., Hofnung M., Schwartz M., 1969, Nonsense mutations in the maltose A region of the genetic map of Escherichia coli., J Bacteriol 100(3):1311-5

 [14] Lu Y., Steichen JM., Yao J., Sharkey TD., 2006, The role of cytosolic alpha-glucan phosphorylase in maltose metabolism and the comparison of amylomaltase in Arabidopsis and Escherichia coli., Plant Physiol 142(3):878-89

 [15] Macaskie LE., Palmer TN., 1978, The role of amylomaltase and maltodextrin phosphorylase in the pathway of glycogen catabolism in Escherichia coli [proceedings]., Biochem Soc Trans 6(2):405-7

 [16] Palmer TN., Ryman BE., Whelan WJ., 1976, The action pattern of amylomaltase from Escherichia coli., Eur J Biochem 69(1):105-15

 [17] Pavlasova E., 1967, Genetic study of a mutation in Escherichia coli, which changes the phenotypical activity of amylomaltase., Folia Microbiol (Praha) 12(6):537-43

 [18] Pavlasova E., Stejskalova E., Necinova S., 1967, Induction of amylomaltase and beta-galactosidase in different growth phases of Escherichia coli., Curr Mod Biol 1(3):196-9

 [19] Pavlasova E., Stejskalova E., Sikyta B., 1980, Simultaneous induction of three catabolic enzymes in Escherichia coli., Folia Microbiol (Praha) 25(3):201-6

 [20] Pugsley AP., Dubreuil C., 1988, Molecular characterization of malQ, the structural gene for the Escherichia coli enzyme amylomaltase., Mol Microbiol 2(4):473-9

 [21] Raibaud O., Gutierrez C., Schwartz M., 1985, Essential and nonessential sequences in malPp, a positively controlled promoter in Escherichia coli., J Bacteriol 161(3):1201-8

 [22] Raibaud O., Schwartz M., 1980, Restriction map of the Escherichia coli malA region and identification of the malT product., J Bacteriol 143(2):761-71

 [23] Ronen A., Raanan-Ashkenazi O., 1971, Temperature sensitivity of maltose utilization and lambda resistance in Escherichia coli B., J Bacteriol 106(3):791-6

 [24] Ruzanski C., Smirnova J., Rejzek M., Cockburn D., Pedersen HL., Pike M., Willats WG., Svensson B., Steup M., Ebenhoh O., Smith AM., Field RA., 2013, A bacterial glucanotransferase can replace the complex maltose metabolism required for starch to sucrose conversion in leaves at night., J Biol Chem 288(40):28581-98

 [25] Schwinn H., Schulz GV., 1971, [Studies on amylomaltase. 3. Kinetic analysis of the reaction mechanism]., Biochim Biophys Acta 227(2):313-26

 [26] Salgado H, Peralta-Gil M, Gama-Castro S, Santos-Zavaleta A, Muñiz-Rascado L, García-Sotelo JS, Weiss V, Solano-Lira H, Martínez-Flores I, Medina-Rivera A, Salgado-Osorio G, Alquicira-Hernández S, Alquicira-Hernández K, López-Fuentes A, Porrón-Sotelo L, Huerta AM, Bonavides-Martínez C, Balderas-Martínez YI, Pannier L, Olvera M, Labastida A, Jiménez-Jacinto V, Vega-Alvarado L, Del Moral-Chávez V, Hernández-Alvarez A, Morett E, Collado-Vides J., 2012, RegulonDB v8.0: omics data sets, evolutionary conservation, regulatory phrases, cross-validated gold standards and more., Nucleic Acids Res.


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