Glucosamine-6-phosphate deaminase
Details
- Name
- Glucosamine-6-phosphate deaminase
- Kind
- protein
- Synonyms
- 3.5.99.6
- GlcN6P deaminase
- glmD
- Glucosamine-6-phosphate isomerase
- GNPDA
- Gene Name
- nagB
- UniProtKB Entry
- P0A759Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsglucosamine-6-phosphate deaminase activity / hydrolase activity / identical protein bindingProcessescarbohydrate metabolic process / N-acetylglucosamine catabolic process / N-acetylneuraminate catabolic process / UDP-N-acetylglucosamine biosynthetic processComponentscytosol
- General Function
- Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
- Specific Function
- glucosamine-6-phosphate deaminase activity
- Pfam Domain Function
- Glucosamine_iso (PF01182)
- Signal Regions
- Not Available
- 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
Resource Link UniProtKB ID P0A759 UniProtKB Entry Name NAGB_ECOLI GenBank Protein ID 455176 GenBank Gene ID M19284 PDB ID(s) 1CD5, 1DEA, 1FQO, 1FRZ, 1FS5, 1FS6, 1FSF, 1HOR, 1HOT, 1JT9, 2WU1 KEGG ID ecj:JW0664 NCBI Gene ID 945290 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details 2-Deoxy-2-Amino Glucitol-6-Phosphate experimental unknown target Details N-acetyl-D-glucosamine-6-phosphate experimental unknown target Details