Glucosamine-6-phosphate deaminase (P0A759)

Identification
Name:Glucosamine-6-phosphate deaminase
Synonyms:
  • GlcN6P deaminase
  • GNPDA
  • Glucosamine-6-phosphate isomerase
Gene Name:nagB
Enzyme Class:
Biological Properties
General Function:Involved in carbohydrate metabolic process
Specific Function:Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion
Cellular Location:Not Available
SMPDB Pathways:
  • Amino sugar and nucleotide sugar metabolism I PW000886
  • Amino sugar and nucleotide sugar metabolism II PW000887
  • Amino sugar and nucleotide sugar metabolism III PW000895
  • N-acetylneuraminate and N-acetylmannosamine and N-acetylglucosamine degradation PW002030
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Glucosamine 6-phosphate + 1.0Water ↔ 1.0Fructose 6-phosphate + 1.0Ammonia
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glucosamine 6-phosphate + 1.0Water → 1.0Ammonium + 1.0D-tagatofuranose 6-phosphate
ReactionCard
1.0D-glucosamine 6-phosphate+1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-glucosamine 6-phosphate + 1.0Water → 1.0Ammonium + 1.0D-tagatofuranose 6-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Glucosamine 6-phosphate + 1.0Water ↔ 1.0Fructose 6-phosphate + 1.0Ammonia
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glucosamine 6-phosphate + 1.0Water → 1.0Fructose 6-phosphate + 1.0Ammonium
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00051AmmoniaMetaboCard
ECMDB21186AmmoniumMetaboCard
ECMDB24205D-tagatofuranose 6-phosphateMetaboCard
ECMDB00124Fructose 6-phosphateMetaboCard
ECMDB01254Glucosamine 6-phosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
catalytic activity
glucosamine-6-phosphate deaminase activity
intramolecular oxidoreductase activity
intramolecular oxidoreductase activity, interconverting aldoses and ketoses
isomerase activity
Process
alcohol metabolic process
amino sugar metabolic process
carbohydrate metabolic process
glucosamine metabolic process
metabolic process
monosaccharide metabolic process
N-acetylglucosamine metabolic process
primary metabolic process
small molecule metabolic process
Gene Properties
Blattner:b0678
Gene OrientationCounterclockwise
Centisome Percentage:15.13
Left Sequence End702034
Right Sequence End702834
Gene Sequence:
>801 bp
ATGAGACTGATCCCCCTGACTACCGCTGAACAGGTCGGCAAATGGGCTGCTCGCCATATC
GTCAATCGTATCAATGCGTTCAAACCGACTGCCGATCGTCCGTTTGTACTGGGCCTGCCG
ACTGGCGGCACGCCGATGACCACCTATAAAGCGTTAGTCGAAATGCATAAAGCAGGCCAG
GTCAGCTTTAAGCACGTTGTCACCTTCAACATGATGGACGAATATGTCGGTCTGCCGAAA
GAGCATCCGGAAAGCTACTACAGCTTTATGCACAATTTCTTCGATCACGTTGATATTCCA
GCAGAAAACATCAACCTTCTCAACGGCAACGCCCCGGATATCGACGCCGAGTGCCGCCAG
TATGAAGAAAAAATCCGTTCTTACGGAAAAATTCATCTGTTTATGGGCGGTGTAGGTAAC
GACGGTCATATTGCATTTAACGAACCGGCGTCTTCTCTGGCTTCTCGTACTCGTATCAAA
ACCCTGACTCATGACACTCGCGTCGCAAACTCTCGTTTCTTTGATAACGATGTTAATCAG
GTGCCAAAATATGCCCTGACTGTCGGTGTTGGTACACTGCTGGATGCCGAAGAAGTGATG
ATTCTGGTGCTGGGTAGCCAGAAAGCACTGGCGCTGCAGGCCGCCGTTGAAGGTTGCGTG
AACCATATGTGGACCATCAGCTGTCTGCAACTGCATCCGAAAGCGATCATGGTGTGCGAT
GAACCTTCCACCATGGAGCTGAAAGTTAAGACTTTAAGATATTTCAATGAATTAGAAGCA
GAAAATATCAAAGGTCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:266
Protein Molecular Weight:29774
Protein Theoretical pI:7
PDB File:1FQO
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glucosamine-6-phosphate deaminase
MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQ
VSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQ
YEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDNDVNQ
VPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCD
EPSTMELKVKTLRYFNELEAENIKGL
References
External Links:
ResourceLink
Uniprot ID:P0A759
Uniprot Name:NAGB_ECOLI
GenBank Gene ID:AF052007
Genebank Protein ID:3005594
PDB ID:1FQO
Ecogene ID:EG10633
Ecocyc:EG10633
ColiBase:b0678
Kegg Gene:b0678
EchoBASE ID:EB0627
CCDB:NAGB_ECOLI
BacMap:16128654
General Reference:
  • Altamirano, M. M., Plumbridge, J. A., Barba, H. A., Calcagno, M. L. (1993). "Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides." Biochem J 295 ( Pt 3):645-648. Pubmed: 8240271
  • Altamirano, M. M., Plumbridge, J. A., Calcagno, M. L. (1992). "Identification of two cysteine residues forming a pair of vicinal thiols in glucosamine-6-phosphate deaminase from Escherichia coli and a study of their functional role by site-directed mutagenesis." Biochemistry 31:1153-1158. Pubmed: 1734962
  • 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
  • Bustos-Jaimes, I., Sosa-Peinado, A., Rudino-Pinera, E., Horjales, E., Calcagno, M. L. (2002). "On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase." J Mol Biol 319:183-189. Pubmed: 12051945
  • 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
  • Horjales, E., Altamirano, M. M., Calcagno, M. L., Garratt, R. C., Oliva, G. (1999). "The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution." Structure 7:527-537. Pubmed: 10378272
  • Montero-Moran, G. M., Lara-Gonzalez, S., Alvarez-Anorve, L. I., Plumbridge, J. A., Calcagno, M. L. (2001). "On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase." Biochemistry 40:10187-10196. Pubmed: 11513596
  • Oliva, G., Fontes, M. R., Garratt, R. C., Altamirano, M. M., Calcagno, M. L., Horjales, E. (1995). "Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution." Structure 3:1323-1332. Pubmed: 8747459
  • Oshima, T., Aiba, H., Baba, T., Fujita, K., Hayashi, K., Honjo, A., Ikemoto, K., Inada, T., Itoh, T., Kajihara, M., Kanai, K., Kashimoto, K., Kimura, S., Kitagawa, M., Makino, K., Masuda, S., Miki, T., Mizobuchi, K., Mori, H., Motomura, K., Nakamura, Y., Nashimoto, H., Nishio, Y., Saito, N., Horiuchi, T., et, a. l. .. (1996). "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." DNA Res 3:137-155. Pubmed: 8905232
  • Peri, K. G., Goldie, H., Waygood, E. B. (1990). "Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli." Biochem Cell Biol 68:123-137. Pubmed: 2190615
  • Rogers, M. J., Ohgi, T., Plumbridge, J., Soll, D. (1988). "Nucleotide sequences of the Escherichia coli nagE and nagB genes: the structural genes for the N-acetylglucosamine transport protein of the bacterial phosphoenolpyruvate: sugar phosphotransferase system and for glucosamine-6-phosphate deaminase." Gene 62:197-207. Pubmed: 3284790
  • Rudino-Pinera, E., Morales-Arrieta, S., Rojas-Trejo, S. P., Horjales, E. (2002). "Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase." Acta Crystallogr D Biol Crystallogr 58:10-20. Pubmed: 11752775