Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] (P17169)

Identification
Name:Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]
Synonyms:
  • D-fructose-6-phosphate amidotransferase
  • GFAT
  • Glucosamine-6-phosphate synthase
  • Hexosephosphate aminotransferase
  • L-glutamine-D-fructose-6-phosphate amidotransferase
Gene Name:glmS
Enzyme Class:
Biological Properties
General Function:Involved in metabolic process
Specific Function:Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Alanine, aspartate and glutamate metabolism ec00250
  • Amino sugar and nucleotide sugar metabolism ec00520
  • Lipopolysaccharide biosynthesis ec00540
  • Metabolic pathways eco01100
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 6-phosphate + 1.0L-Glutamine ↔ 1.0Glucosamine 6-phosphate + 1.0L-Glutamate
ReactionCard
SMPDB Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0L-Glutamic acid+1.0Thumb
1.0D-tagatofuranose 6-phosphate + 1.0L-Glutamine ↔ 1.0Glucosamine 6-phosphate + 1.0L-Glutamic acid + 1.0L-Glutamate
ReactionCard
1.0Fructose 6-phosphate+1.0Thumb+1.0Thumb → 1.0L-Glutamic acid+1.0Thumb+1.0Thumb
1.0Fructose 6-phosphate + 1.0L-Glutamine + 1.0Fructose 6-phosphate → 1.0L-Glutamic acid + 1.0Glucosamine 6-phosphate + 1.0L-Glutamate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0D-glucosamine 6-phosphate+1.0Thumb
1.0D-tagatofuranose 6-phosphate + 1.0L-Glutamine ↔ 1.0D-glucosamine 6-phosphate + 1.0L-Glutamate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Fructose 6-phosphate + 1.0L-Glutamine ↔ 1.0Glucosamine 6-phosphate + 1.0L-Glutamate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB24205D-tagatofuranose 6-phosphateMetaboCard
ECMDB00124Fructose 6-phosphateMetaboCard
ECMDB01254Glucosamine 6-phosphateMetaboCard
ECMDB00148L-GlutamateMetaboCard
ECMDB00641L-GlutamineMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
carbohydrate binding
catalytic activity
glutamine-fructose-6-phosphate transaminase (isomerizing) activity
sugar binding
transaminase activity
transferase activity
transferase activity, transferring nitrogenous groups
Process
carbohydrate biosynthetic process
carbohydrate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b3729
Gene OrientationCounterclockwise
Centisome Percentage:84.27
Left Sequence End3909862
Right Sequence End3911691
Gene Sequence:
>1830 bp
ATGTGTGGAATTGTTGGCGCGATCGCGCAACGTGATGTAGCAGAAATCCTTCTTGAAGGT
TTACGTCGTCTGGAATACCGCGGATATGACTCTGCCGGTCTGGCCGTTGTTGATGCAGAA
GGTCATATGACCCGCCTGCGTCGCCTCGGTAAAGTCCAGATGCTGGCACAGGCAGCGGAA
GAACATCCTCTGCATGGCGGCACTGGTATTGCTCACACTCGCTGGGCGACCCACGGTGAA
CCTTCAGAAGTGAATGCGCATCCGCATGTTTCTGAACACATTGTGGTGGTGCATAACGGC
ATCATCGAAAACCATGAACCGCTGCGTGAAGAGCTAAAAGCGCGTGGCTATACCTTCGTT
TCTGAAACCGACACCGAAGTGATTGCCCATCTGGTGAACTGGGAGCTGAAACAAGGCGGG
ACTCTGCGTGAGGCCGTTCTGCGTGCTATCCCGCAGCTGCGTGGTGCGTACGGTACAGTG
ATCATGGACTCCCGTCACCCGGATACCCTGCTGGCGGCACGTTCTGGTAGTCCGCTGGTG
ATTGGCCTGGGGATGGGCGAAAACTTTATCGCTTCTGACCAGCTGGCGCTGTTGCCGGTG
ACCCGTCGCTTTATCTTCCTTGAAGAGGGCGATATTGCGGAAATCACTCGCCGTTCGGTA
AACATCTTCGATAAAACTGGCGCGGAAGTAAAACGTCAGGATATCGAATCCAATCTGCAA
TATGACGCGGGCGATAAAGGCATTTACCGTCACTACATGCAGAAAGAGATCTACGAACAG
CCGAACGCGATCAAAAACACCCTTACCGGACGCATCAGCCACGGTCAGGTTGATTTAAGC
GAGCTGGGACCGAACGCCGACGAACTGCTGTCGAAGGTTGAGCATATTCAGATCCTCGCC
TGTGGTACTTCTTATAACTCCGGTATGGTTTCCCGCTACTGGTTTGAATCGCTAGCAGGT
ATTCCGTGCGACGTCGAAATCGCCTCTGAATTCCGCTATCGCAAATCTGCCGTGCGTCGT
AACAGCCTGATGATCACCTTGTCACAGTCTGGCGAAACCGCGGATACCCTGGCTGGCCTG
CGTCTGTCGAAAGAGCTGGGTTACCTTGGTTCACTGGCAATCTGTAACGTTCCGGGTTCT
TCTCTGGTGCGCGAATCCGATCTGGCGCTAATGACCAACGCGGGTACAGAAATCGGCGTG
GCATCCACTAAAGCATTCACCACTCAGTTAACTGTGCTGTTGATGCTGGTGGCGAAGCTG
TCTCGCCTGAAAGGTCTGGATGCCTCCATTGAACATGACATCGTGCATGGTCTGCAGGCG
CTGCCGAGCCGTATTGAGCAGATGCTGTCTCAGGACAAACGCATTGAAGCGCTGGCAGAA
GATTTCTCTGACAAACATCACGCGCTGTTCCTGGGCCGTGGCGATCAGTACCCAATCGCG
CTGGAAGGCGCATTGAAGTTGAAAGAGATCTCTTACATTCACGCTGAAGCCTACGCTGCT
GGCGAACTGAAACACGGTCCGCTGGCGCTAATTGATGCCGATATGCCGGTTATTGTTGTT
GCACCGAACAACGAATTGCTGGAAAAACTGAAATCCAACATTGAAGAAGTTCGCGCGCGT
GGCGGTCAGTTGTATGTCTTCGCCGATCAGGATGCGGGTTTTGTAAGTAGCGATAACATG
CACATCATCGAGATGCCGCATGTGGAAGAGGTGATTGCACCGATCTTCTACACCGTTCCG
CTGCAGCTGCTGGCTTACCATGTCGCGCTGATCAAAGGCACCGACGTTGACCAGCCGCGT
AACCTGGCAAAATCGGTTACGGTTGAGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:609
Protein Molecular Weight:66894
Protein Theoretical pI:6
PDB File:1JXA
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glucosamine--fructose-6-phosphate aminotransferase [isomerizing]
MCGIVGAIAQRDVAEILLEGLRRLEYRGYDSAGLAVVDAEGHMTRLRRLGKVQMLAQAAE
EHPLHGGTGIAHTRWATHGEPSEVNAHPHVSEHIVVVHNGIIENHEPLREELKARGYTFV
SETDTEVIAHLVNWELKQGGTLREAVLRAIPQLRGAYGTVIMDSRHPDTLLAARSGSPLV
IGLGMGENFIASDQLALLPVTRRFIFLEEGDIAEITRRSVNIFDKTGAEVKRQDIESNLQ
YDAGDKGIYRHYMQKEIYEQPNAIKNTLTGRISHGQVDLSELGPNADELLSKVEHIQILA
CGTSYNSGMVSRYWFESLAGIPCDVEIASEFRYRKSAVRRNSLMITLSQSGETADTLAGL
RLSKELGYLGSLAICNVPGSSLVRESDLALMTNAGTEIGVASTKAFTTQLTVLLMLVAKL
SRLKGLDASIEHDIVHGLQALPSRIEQMLSQDKRIEALAEDFSDKHHALFLGRGDQYPIA
LEGALKLKEISYIHAEAYAAGELKHGPLALIDADMPVIVVAPNNELLEKLKSNIEEVRAR
GGQLYVFADQDAGFVSSDNMHIIEMPHVEEVIAPIFYTVPLQLLAYHVALIKGTDVDQPR
NLAKSVTVE
References
External Links:
ResourceLink
Uniprot ID:P17169
Uniprot Name:GLMS_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85676309
PDB ID:1JXA
Ecogene ID:EG10382
Ecocyc:EG10382
ColiBase:b3729
Kegg Gene:b3729
EchoBASE ID:EB0377
CCDB:GLMS_ECOLI
BacMap:16131597
General Reference:
  • 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
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Dutka-Malen, S., Mazodier, P., Badet, B. (1988). "Molecular cloning and overexpression of the glucosamine synthetase gene from Escherichia coli." Biochimie 70:287-290. Pubmed: 3134953
  • Gay, N. J., Tybulewicz, V. L., Walker, J. E. (1986). "Insertion of transposon Tn7 into the Escherichia coli glmS transcriptional terminator." Biochem J 234:111-117. Pubmed: 3010949
  • Golinelli-Pimpaneau, B., Badet, B. (1991). "Possible involvement of Lys603 from Escherichia coli glucosamine-6-phosphate synthase in the binding of its substrate fructose 6-phosphate." Eur J Biochem 201:175-182. Pubmed: 1915361
  • 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
  • Isupov, M. N., Obmolova, G., Butterworth, S., Badet-Denisot, M. A., Badet, B., Polikarpov, I., Littlechild, J. A., Teplyakov, A. (1996). "Substrate binding is required for assembly of the active conformation of the catalytic site in Ntn amidotransferases: evidence from the 1.8 A crystal structure of the glutaminase domain of glucosamine 6-phosphate synthase." Structure 4:801-810. Pubmed: 8805567
  • Lichtenstein, C., Brenner, S. (1982). "Unique insertion site of Tn7 in the E. coli chromosome." Nature 297:601-603. Pubmed: 6283361
  • McKown, R. L., Orle, K. A., Chen, T., Craig, N. L. (1988). "Sequence requirements of Escherichia coli attTn7, a specific site of transposon Tn7 insertion." J Bacteriol 170:352-358. Pubmed: 2826397
  • Teplyakov, A., Obmolova, G., Badet-Denisot, M. A., Badet, B. (1999). "The mechanism of sugar phosphate isomerization by glucosamine 6-phosphate synthase." Protein Sci 8:596-602. Pubmed: 10091662
  • Teplyakov, A., Obmolova, G., Badet-Denisot, M. A., Badet, B., Polikarpov, I. (1998). "Involvement of the C terminus in intramolecular nitrogen channeling in glucosamine 6-phosphate synthase: evidence from a 1.6 A crystal structure of the isomerase domain." Structure 6:1047-1055. Pubmed: 9739095
  • Walker, J. E., Gay, N. J., Saraste, M., Eberle, A. N. (1984). "DNA sequence around the Escherichia coli unc operon. Completion of the sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and phoS." Biochem J 224:799-815. Pubmed: 6395859