Sequence of NAGB_ECOLI
EC Number:3.5.99.6
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
alpha-D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3
Other sequences found for EC No. 3.5.99.6
General information:
Sequence
0 MRLIPLTTAE QVGKWAARHI VNRINAFKPT ADRPFVLGLP TGGTPMTTYK ALVEMHKAGQ
60 VSFKHVVTFN MDEYVGLPKE HPESYYSFMH RNFFDHVDIP AENINLLNGN APDIDAECRQ
120 YEEKIRSYGK IHLFMGGVGN DGHIAFNEPA SSLASRTRIK TLTHDTRVAN SRFFDNDVNQ
180 VPKYALTVGV GTLLDAEEVM ILVLGSQKAL ALQAAVEGCV NHMWTISCLQ LHPKAIMVCD
240 EPSTMELKVK TLRYFNELEA ENIKGL
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
959703
Rogers M.J.,Ohgi T.,Plumbridge J.,Soell 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
62
197-207
1988
959704
Peri K.G.,Goldie H.,Waygood E.B.
Cloning and characterization of the N-acetylglucosamine operon of Escherichia coli.
Biochem. Cell Biol.
68
123-137
1990
959705
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.,Sampei G.,Seki Y.,Tagami H.,Takemoto K.,Wada C.,Yamamoto Y.,Yano M.,Horiuchi T.
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
1996
959706
Blattner F.R.,Plunkett G. III,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.
The complete genome sequence of Escherichia coli K-12.
Science
277
1453-1462
1997
959707
Hayashi K.,Morooka N.,Yamamoto Y.,Fujita K.,Isono K.,Choi S.,Ohtsubo E.,Baba T.,Wanner B.L.,Mori H.,Horiuchi T.
Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.
Mol. Syst. Biol.
2
0-0
2006
959708
Altamirano M.M.,Mulliert G.,Calcagno M.
Sulfhydryl groups of glucosamine-6-phosphate isomerase deaminase from Escherichia coli.
Arch. Biochem. Biophys.
258
95-100
1987
959709
Altamirano M.M.,Plumbridge J.A.,Calcagno M.L.
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
1992
959710
Altamirano M.M.,Plumbridge J.A.,Barba H.A.,Calcagno M.L.
Glucosamine-6-phosphate deaminase from Escherichia coli has a trimer of dimers structure with three intersubunit disulphides.
Biochem. J.
295
645-648
1993
959711
Montero-Moran G.M.,Lara-Gonzalez S.,Alvarez-Anorve L.I.,Plumbridge J.A.,Calcagno M.L.
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
2001
959712
Oliva G.,Fontes M.R.M.,Garratt R.C.,Altamirano M.M.,Calcagno M.L.,Horjales E.
Structure and catalytic mechanism of glucosamine 6-phosphate deaminase from Escherichia coli at 2.1-A resolution.
Structure
3
1323-1332
1995
959713
Horjales E.,Altamirano M.M.,Calcagno M.L.,Garratt R.C.,Oliva G.
The allosteric transition of glucosamine-6-phosphate deaminase: the structure of the T state at 2.3-A resolution.
Structure
7
527-537
1999
959714
Rudino-Pinera E.,Morales-Arrieta S.,Rojas-Trejo S.P.,Horjales E.
Structural flexibility, an essential component of the allosteric activation in Escherichia coli glucosamine-6-phosphate deaminase.
Acta Crystallogr. D
58
10-20
2002
959715
Bustos-Jaimes I.,Sosa-Peinado A.,Rudino-Pinera E.,Horjales E.,Calcagno M.L.
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
2002
