Glucose-1-phosphate adenylyltransferase (P0A6V1)

Identification
Name:Glucose-1-phosphate adenylyltransferase
Synonyms:
  • ADP-glucose pyrophosphorylase
  • ADPGlc PPase
  • ADP-glucose synthase
Gene Name:glgC
Enzyme Class:
Biological Properties
General Function:Involved in glycogen biosynthetic process
Specific Function:ATP + alpha-D-glucose 1-phosphate = diphosphate + ADP-glucose
Cellular Location:Not Available
SMPDB Pathways:
  • Amino sugar and nucleotide sugar metabolism II PW000887
  • Secondary metabolites: Trehalose Biosynthesis and Metabolism PW000968
  • Starch and sucrose metabolism PW000941
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glucose 1-phosphate + 1.0Hydrogen ion ↔ 1.0ADP-Glucose + 1.0Pyrophosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glucose 1-phosphate ↔ 1.0Pyrophosphate + 1.0ADP-Glucose
ReactionCard
SMPDB Reactions:
1.0Alpha-D-glucose 1-phosphate+1.0Thumb → 1.0Thumb+1.0Pyrophosphate
1.0Alpha-D-glucose 1-phosphate + 1.0Adenosine triphosphate → 1.0ADP-Glucose + 1.0Pyrophosphate
ReactionCard
1.0Alpha-D-glucose 1-phosphate+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Pyrophosphate
1.0Alpha-D-glucose 1-phosphate + 1.0Adenosine triphosphate + 1.0Hydrogen ion → 1.0ADP-Glucose + 1.0Pyrophosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Glucose 1-phosphate + 1.0Hydrogen ion ↔ 1.0ADP-Glucose + 1.0Pyrophosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB06557ADP-GlucoseMetaboCard
ECMDB03514alpha-D-Glucose 1,6-bisphosphateMetaboCard
ECMDB01586Glucose 1-phosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB04142PyrophosphateMetaboCard
GO Classification:
Function
adenylyltransferase activity
catalytic activity
glucose-1-phosphate adenylyltransferase activity
nucleotidyltransferase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Process
alcohol metabolic process
biosynthetic process
glucose metabolic process
glycogen biosynthetic process
glycogen metabolic process
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b3430
Gene OrientationCounterclockwise
Centisome Percentage:76.86
Left Sequence End3566056
Right Sequence End3567351
Gene Sequence:
>1296 bp
GTGCTGGAACGGCTGTCGTGGAAAAGGCTGGTGCTGGAGCTGCTACTTTGCTGCCTCCCG
GCTTTCATCCTGGGTGCATTTTTTGGTTACCTGCCCTGGTTTTTGCTGGCATCGGTAACA
GGACTGCTTATCTGGCATTTCTGGAATTTATTGCGCCTTTCATGGTGGCTGTGGGTGGAT
CGCAGTATGACCCCGCCACCGGGGCGTGGTAGCTGGGAACCGCTACTATACGGCTTACAC
CAGATGCAGCTGCGAAATAAAAAACGCCGCCGTGAACTGGGCAATCTGATTAAACGCTTT
CGTAGCGGCGCGGAGTCGCTGCCCGACGCGGTGGTGCTGACCACGGAAGAGGGCGGTATT
TTCTGGTGTAACGGTCTGGCGCAACAAATTCTTGGTTTGCGCTGGCCGGAAGATAACGGG
CAGAACATCCTTAACCTACTGCGTTACCCGGAGTTTACGCAATATCTGAAAACGCGTGAT
TTTTCTCGCCCGCTCAATCTGGTGCTCAACACCGGGCGGCATCTGGAAATTCGCGTCATG
CCTTATACCCACAAACAGTTGCTGATGGTGGCGCGTGATGTCACGCAAATGCATCAACTG
GAAGGGGCGCGGCGTAACTTTTTTGCCAACGTGAGCCATGAGTTACGTACGCCATTGACC
GTGTTACAGGGTTACCTGGAGATGATGAATGAGCAGCCGCTGGAAGGCGCGGTACGCGAA
AAAGCGTTGCACACCATGCGCGAGCAGACCCAGCGGATGGAAGGACTGGTGAAGCAATTG
CTGACGCTGTCGAAAATAGAAGCCGCACCGACGCATTTGCTCAATGAAAAGGTTGATGTG
CCGATGATGCTGCGCGTTGTTGAGCGCGAGGCTCAGACTCTGAGTCAGAAAAAACAGACA
TTTACCTTTGAGATAGATAACGGCCTCAAGGTGTCTGGCAACGAAGATCAGCTACGCAGT
GCGATTTCGAACCTGGTCTATAACGCCGTGAATCATACGCCGGAAGGCACGCATATCACC
GTACGCTGGCAGCGAGTGCCGCACGGTGCCGAATTTAGCGTTGAAGATAACGGACCGGGC
ATTGCACCGGAGCATATTCCGCGCCTGACCGAGCGTTTTTATCGCGTTGATAAAGCGCGT
TCCCGGCAAACCGGCGGTAGCGGATTAGGGTTAGCGATCGTGAAACATGCTGTGAATCAT
CACGAAAGTCGCCTGAATATTGAGAGTACAGTAGGAAAAGGAACACGTTTCAGTTTTGTT
ATCCCGGAACGTTTAATTGCCAAAAACAGCGATTAA
Protein Properties
Pfam Domain Function:
Protein Residues:431
Protein Molecular Weight:48697
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glucose-1-phosphate adenylyltransferase
MVSLEKNDHLMLARQLPLKSVALILAGGRGTRLKDLTNKRAKPAVHFGGKFRIIDFALSN
CINSGIRRMGVITQYQSHTLVQHIQRGWSFFNEEMNEFVDLLPAQQRMKGENWYRGTADA
VTQNLDIIRRYKAEYVVILAGDHIYKQDYSRMLIDHVEKGARCTVACMPVPIEEASAFGV
MAVDENDKIIEFVEKPANPPSMPNDPSKSLASMGIYVFDADYLYELLEEDDRDENSSHDF
GKDLIPKITEAGLAYAHPFPLSCVQSDPDAEPYWRDVGTLEAYWKANLDLASVVPELDMY
DRNWPIRTYNESLPPAKFVQDRSGSHGMTLNSLVSGGCVISGSVVVQSVLFSRVRVNSFC
NIDSAVLLPEVWVGRSCRLRRCVIDRACVIPEGMVIGENAEEDARRFYRSEEGIVLVTRE
MLRKLGHKQER
References
External Links:
ResourceLink
Uniprot ID:P0A6V1
Uniprot Name:GLGC_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674540
Ecogene ID:EG10379
Ecocyc:EG10379
ColiBase:b3430
Kegg Gene:b3430
EchoBASE ID:EB0374
CCDB:GLGC_ECOLI
BacMap:16131304
General Reference:
  • Baecker, P. A., Furlong, C. E., Preiss, J. (1983). "Biosynthesis of bacterial glycogen. Primary structure of Escherichia coli ADP-glucose synthetase as deduced from the nucleotide sequence of the glg C gene." J Biol Chem 258:5084-5088. Pubmed: 6300111
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Ghosh, P., Meyer, C., Remy, E., Peterson, D., Preiss, J. (1992). "Cloning, expression, and nucleotide sequence of glgC gene from an allosteric mutant of Escherichia coli B." Arch Biochem Biophys 296:122-128. Pubmed: 1339262
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hill, M. A., Kaufmann, K., Otero, J., Preiss, J. (1991). "Biosynthesis of bacterial glycogen. Mutagenesis of a catalytic site residue of ADP-glucose pyrophosphorylase from Escherichia coli." J Biol Chem 266:12455-12460. Pubmed: 1648099
  • Kumar, A., Ghosh, P., Lee, Y. M., Hill, M. A., Preiss, J. (1989). "Biosynthesis of bacterial glycogen. Determination of the amino acid changes that alter the regulatory properties of a mutant Escherichia coli ADP-glucose synthetase." J Biol Chem 264:10464-10471. Pubmed: 2543670
  • Kumar, A., Tanaka, T., Lee, Y. M., Preiss, J. (1988). "Biosynthesis of bacterial glycogen. Use of site-directed mutagenesis to probe the role of tyrosine 114 in the catalytic mechanism of ADP-glucose synthetase from Escherichia coli." J Biol Chem 263:14634-14639. Pubmed: 2844780
  • Meyer, C. R., Ghosh, P., Nadler, S., Preiss, J. (1993). "Cloning, expression, and sequence of an allosteric mutant ADPglucose pyrophosphorylase from Escherichia coli B." Arch Biochem Biophys 302:64-71. Pubmed: 8385906
  • Meyer, C. R., Ghosh, P., Remy, E., Preiss, J. (1992). "Cloning, expression, and nucleotide sequence of a mutant glgC gene from Escherichia coli B." J Bacteriol 174:4509-4512. Pubmed: 1320612
  • Parsons, T. F., Preiss, J. (1978). "Biosynthesis of bacterial glycogen. Isolation and characterization of the pyridoxal-P allosteric activator site and the ADP-glucose-protected pyridoxal-P binding site of Escherichia coli B ADP-glucose synthase." J Biol Chem 253:7638-7645. Pubmed: 359552