Glucosamine-6-phosphate deaminase

Details

Name
Glucosamine-6-phosphate deaminase
Synonyms
  • 3.5.99.6
  • GlcN6P deaminase
  • glmD
  • Glucosamine-6-phosphate isomerase
  • GNPDA
Gene Name
nagB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011155|Glucosamine-6-phosphate deaminase
MRLIPLTTAEQVGKWAARHIVNRINAFKPTADRPFVLGLPTGGTPMTTYKALVEMHKAGQ
VSFKHVVTFNMDEYVGLPKEHPESYYSFMHRNFFDHVDIPAENINLLNGNAPDIDAECRQ
YEEKIRSYGKIHLFMGGVGNDGHIAFNEPASSLASRTRIKTLTHDTRVANSRFFDNDVNQ
VPKYALTVGVGTLLDAEEVMILVLGSQKALALQAAVEGCVNHMWTISCLQLHPKAIMVCD
EPSTMELKVKTLRYFNELEAENIKGL
Number of residues
266
Molecular Weight
29774.005
Theoretical pI
6.91
GO Classification
Functions
glucosamine-6-phosphate deaminase activity / hydrolase activity / identical protein binding
Processes
carbohydrate metabolic process / N-acetylglucosamine catabolic process / N-acetylneuraminate catabolic process / UDP-N-acetylglucosamine biosynthetic process
Components
cytosol
General Function
Identical protein binding
Specific Function
Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011156|Glucosamine-6-phosphate deaminase (nagB)
ATGAGACTGATCCCCCTGACTACCGCTGAACAGGTCGGCAAATGGGCTGCTCGCCATATC
GTCAATCGTATCAATGCGTTCAAACCGACTGCCGATCGTCCGTTTGTACTGGGCCTGCCG
ACTGGCGGCACGCCGATGACCACCTATAAAGCGTTAGTCGAAATGCATAAAGCAGGCCAG
GTCAGCTTTAAGCACGTTGTCACCTTCAACATGGACGAATATGTCGGTCTGCCGAAAGAG
CATCCGGAAAGCTACTACAGCTTTATGCACCGTAATTTCTTCGATCACGTTGATATTCCA
GCAGAAAACATCAACCTTCTCAACGGCAACGCCCCGGATATCGACGCCGAGTGCCGCCAG
TATGAAGAAAAAATCCGTTCTTACGGAAAAATTCATCTGTTTATGGGCGGTGTAGGTAAC
GACGGTCATATTGCATTTAACGAACCGGCGTCTTCTCTGGCTTCTCGTACTCGTATCAAA
ACCCTGACTCATGACACTCGCGTCGCAAACTCTCGTTTCTTTGATAACGATGTTAATCAG
GTGCCAAAATATGCCCTGACTGTCGGTGTTGGTACACTGCTGGATGCCGAAGAAGTGATG
ATTCTGGTGCTGGGTAGCCAGAAAGCACTGGCGCTGCAGGCCGCCGTTGAAGGTTGCGTG
AACCATATGTGGACCATCAGCTGTCTGCAACTGCATCCGAAAGCGATCATGGTGTGCGAT
GAACCTTCCACCATGGAGCTGAAAGTTAAGACTTTAAGATATTTCAATGAATTAGAAGCA
GAAAATATCAAAGGTCTGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0A759
UniProtKB Entry NameNAGB_ECOLI
GenBank Protein ID455176
GenBank Gene IDM19284
General References
  1. Rogers MJ, Ohgi T, Plumbridge J, Soll D: 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. 1988;62(2):197-207. [Article]
  2. Peri KG, Goldie H, Waygood EB: Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli. Biochem Cell Biol. 1990 Jan;68(1):123-37. [Article]
  3. 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 al.: 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. 1996 Jun 30;3(3):137-55. [Article]
  4. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  5. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  6. Altamirano MM, Plumbridge JA, Calcagno ML: 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. 1992 Feb 4;31(4):1153-8. [Article]
  7. Altamirano MM, Plumbridge JA, Barba HA, Calcagno ML: Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides. Biochem J. 1993 Nov 1;295 ( Pt 3):645-8. [Article]
  8. Montero-Moran GM, Lara-Gonzalez S, Alvarez-Anorve LI, Plumbridge JA, Calcagno ML: On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Biochemistry. 2001 Aug 28;40(34):10187-96. [Article]
  9. Oliva G, Fontes MR, Garratt RC, Altamirano MM, Calcagno ML, Horjales E: Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1 A resolution. Structure. 1995 Dec 15;3(12):1323-32. [Article]
  10. Horjales E, Altamirano MM, Calcagno ML, Garratt RC, Oliva G: The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3 A resolution. Structure. 1999 May;7(5):527-37. [Article]
  11. Rudino-Pinera E, Morales-Arrieta S, Rojas-Trejo SP, Horjales E: Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase. Acta Crystallogr D Biol Crystallogr. 2002 Jan;58(Pt 1):10-20. Epub 2001 Dec 21. [Article]
  12. Bustos-Jaimes I, Sosa-Peinado A, Rudino-Pinera E, Horjales E, Calcagno ML: On the role of the conformational flexibility of the active-site lid on the allosteric kinetics of glucosamine-6-phosphate deaminase. J Mol Biol. 2002 May 24;319(1):183-9. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB024452-Deoxy-2-Amino Glucitol-6-PhosphateexperimentalunknownDetails
DB03951N-acetyl-D-glucosamine-6-phosphateexperimentalunknownDetails