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Identification
HMDB Protein ID HMDBP00216
Secondary Accession Numbers
  • 5448
  • HMDBP09362
Name Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1
Synonyms
  1. D-fructose-6-phosphate amidotransferase 1
  2. GFAT 1
  3. GFAT1
  4. Glutamine:fructose 6 phosphate amidotransferase 1
  5. Hexosephosphate aminotransferase 1
  6. Glutamine:fructose-6-phosphate amidotransferase 1
Gene Name GFPT1
Protein Type Enzyme
Biological Properties
General Function Involved in metabolic process
Specific Function Controls the flux of glucose into the hexosamine pathway. Most likely involved in regulating the availability of precursors for N- and O-linked glycosylation of proteins.
Pathways
  • 2-Hydroxyglutric Aciduria (D And L Form)
  • 4-Hydroxybutyric Aciduria/Succinic Semialdehyde Dehydrogenase Deficiency
  • Alanine, aspartate and glutamate metabolism
  • Amino sugar and nucleotide sugar metabolism
  • Amino Sugar Metabolism
  • G(M2)-Gangliosidosis: Variant B, Tay-sachs disease
  • Glutamate Metabolism
  • Homocarnosinosis
  • Hyperinsulinism-Hyperammonemia Syndrome
  • Salla Disease/Infantile Sialic Acid Storage Disease
  • Sialuria or French Type Sialuria
  • Sialuria or French Type Sialuria
  • Succinic semialdehyde dehydrogenase deficiency
  • Tay-Sachs Disease
  • UDP-N-acetyl-alpha-D-glucosamine biosynthesis
Reactions
L-Glutamine + Fructose 6-phosphate → L-Glutamic acid + Glucosamine 6-phosphate details
GO Classification
Biological Process
glutamine metabolic process
negative regulation of glycogen biosynthetic process
dolichol-linked oligosaccharide biosynthetic process
post-translational protein modification
protein N-linked glycosylation via asparagine
UDP-N-acetylglucosamine biosynthetic process
cellular response to insulin stimulus
response to sucrose stimulus
glucosamine biosynthetic process
carbohydrate biosynthetic process
fructose 6-phosphate metabolic process
energy reserve metabolic process
protein homotetramerization
activation of signaling protein activity involved in unfolded protein response
Cellular Component
cytosol
Component
cell part
intracellular part
cytoplasm
intracellular
cell
Function
binding
catalytic activity
transferase activity
transferase activity, transferring nitrogenous groups
transaminase activity
glutamine-fructose-6-phosphate transaminase (isomerizing) activity
carbohydrate binding
sugar binding
Molecular Function
carbohydrate binding
glutamine-fructose-6-phosphate transaminase (isomerizing) activity
amino acid binding
Process
metabolic process
primary metabolic process
carbohydrate metabolic process
physiological process
metabolism
macromolecule metabolism
carbohydrate biosynthesis
carbohydrate biosynthetic process
macromolecule biosynthesis
carbohydrate metabolism
Cellular Location Not Available
Gene Properties
Chromosome Location 2
Locus 2p13
SNPs GFPT1
Gene Sequence
>2046 bp
ATGTGTGGTATATTTGCTTACTTAAACTACCATGTTCCTCGAACGAGACGAGAAATCCTG
GAGACCCTAATCAAAGGCCTTCAGAGACTGGAGTACAGAGGATATGATTCTGCTGGTGTG
GGATTTGATGGAGGCAATGATAAAGATTGGGAAGCCAATGCCTGCAAAATCCAGCTTATT
AAGAAGAAAGGAAAAGTTAAGGCACTGGATGAAGAAGTTCACAAGCAACAAGATATGGAT
TTGGATATAGAATTTGATGTACACCTTGGAATAGCTCATACCCGTTGGGCAACACATGGA
GAACCCAGTCCTGTCAATAGCCACCCCCAGCGCTCTGATAAAAATAATGAATTTATCGTT
ATTCACAATGGAATCATCACCAACTACAAAGACTTGAAAAAGTTTTTGGAAAGCAAAGGC
TATGACTTCGAATCTGAAACAGACACAGAGACAATTGCCAAGCTCGTTAAGTATATGTAT
GACAATCGGGAAAGTCAAGATACCAGCTTTACTACCTTGGTGGAGAGAGTTATCCAACAA
TTGGAAGGTGCTTTTGCACTTGTGTTTAAAAGTGTTCATTTTCCCGGGCAAGCAGTTGGC
ACAAGGCGAGGTAGCCCTCTGTTGATTGGTGTACGGAGTGAACATAAACTTTCTACTGAT
CACATTCCTATACTCTACAGAACAGGCAAAGACAAGAAAGGAAGCTGCAATCTCTCTCGT
GTGGACAGCACAACCTGCCTTTTCCCGGTGGAAGAAAAAGCAGTGGAGTATTACTTTGCT
TCTGATGCAAGTGCTGTCATAGAACACACCAATCGCGTCATCTTTCTGGAAGATGATGAT
GTTGCAGCAGTAGTGGATGGACGTCTTTCTATCCATCGAATTAAACGAACTGCAGGAGAT
CACCCCGGACGAGCTGTGCAAACACTCCAGATGGAACTCCAGCAGATCATGAAGGGCAAC
TTCAGTTCATTTATGCAGAAGGAAATATTTGAGCAGCCAGAGTCTGTCGTGAACACAATG
AGAGGAAGAGTCAACTTTGATGACTATACTGTGAATTTGGGTGGTTTGAAGGATCACATA
AAGGAGATCCAGAGATGCCGGCGTTTGATTCTTATTGCTTGTGGAACAAGTTACCATGCT
GGTGTAGCAACACGTCAAGTTCTTGAGGAGCTGACTGAGTTGCCTGTGATGGTGGAACTA
GCAAGTGACTTCCTGGACAGAAACACACCAGTCTTTCGAGATGATGTTTGCTTTTTCCTT
AGTCAATCAGGTGAGACAGCAGATACTTTGATGGGTCTTCGTTACTGTAAGGAGAGAGGA
GCTTTAACTGTGGGGATCACAAACACAGTTGGCAGTTCCATATCACGGGAGACAGATTGT
GGAGTTCATATTAATGCTGGTCCTGAGATTGGTGTGGCCAGTACAAAGGCTTATACCAGC
CAGTTTGTATCCCTTGTGATGTTTGCCCTTATGATGTGTGATGATCGGATCTCCATGCAA
GAAAGACGCAAAGAGATCATGCTTGGATTGAAACGGCTGCCTGATTTGATTAAGGAAGTA
CTGAGCATGGATGACGAAATTCAGAAACTAGCAACAGAACTTTATCATCAGAAGTCAGTT
CTGATAATGGGACGAGGCTATCATTATGCTACTTGTCTTGAAGGGGCACTGAAAATCAAA
GAAATTACTTATATGCACTCTGAAGGCATCCTTGCTGGTGAATTGAAACATGGCCCTCTG
GCTTTGGTGGATAAATTGATGCCTGTGATCATGATCATCATGAGAGATCACACTTATGCC
AAGTGTCAGAATGCTCTTCAGCAAGTGGTTGCTCGGCAGGGGCGGCCTGTGGTAATTTGT
GATAAGGAGGATACTGAGACCATTAAGAACACAAAAAGAACGATCAAGGTGCCCCACTCA
GTGGACTGCTTGCAGGGCATTCTCAGCGTGATCCCTTTACAGTTGCTGGCTTTCCACCTT
GCTGTGCTGAGAGGCTATGATGTTGATTTCCCACGGAATCTTGCCAAATCTGTGACTGTA
GAGTGA
Protein Properties
Number of Residues 699
Molecular Weight 78805.81
Theoretical pI 7.107
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Glucosamine--fructose-6-phosphate aminotransferase [isomerizing] 1
MCGIFAYLNYHVPRTRREILETLIKGLQRLEYRGYDSAGVGFDGGNDKDWEANACKIQLI
KKKGKVKALDEEVHKQQDMDLDIEFDVHLGIAHTRWATHGEPSPVNSHPQRSDKNNEFIV
IHNGIITNYKDLKKFLESKGYDFESETDTETIAKLVKYMYDNRESQDTSFTTLVERVIQQ
LEGAFALVFKSVHFPGQAVGTRRGSPLLIGVRSEHKLSTDHIPILYRTARTQIGSKFTRW
GSQGERGKDKKGSCNLSRVDSTTCLFPVEEKAVEYYFASDASAVIEHTNRVIFLEDDDVA
AVVDGRLSIHRIKRTAGDHPGRAVQTLQMELQQIMKGNFSSFMQKEIFEQPESVVNTMRG
RVNFDDYTVNLGGLKDHIKEIQRCRRLILIACGTSYHAGVATRQVLEELTELPVMVELAS
DFLDRNTPVFRDDVCFFLSQSGETADTLMGLRYCKERGALTVGITNTVGSSISRETDCGV
HINAGPEIGVASTKAYTSQFVSLVMFALMMCDDRISMQERRKEIMLGLKRLPDLIKEVLS
MDDEIQKLATELYHQKSVLIMGRGYHYATCLEGALKIKEITYMHSEGILAGELKHGPLAL
VDKLMPVIMIIMRDHTYAKCQNALQQVVARQGRPVVICDKEDTETIKNTKRTIKVPHSVD
CLQGILSVIPLQLLAFHLAVLRGYDVDFPRNLAKSVTVE
GenBank ID Protein 205277386
UniProtKB/Swiss-Prot ID Q06210
UniProtKB/Swiss-Prot Entry Name GFPT1_HUMAN
PDB IDs
GenBank Gene ID AC114772
GeneCard ID GFPT1
GenAtlas ID GFPT1
HGNC ID HGNC:4241
References
General References
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  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. [PubMed:19690332 ]
  5. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. doi: 10.1074/mcp.M800588-MCP200. Epub 2009 Apr 15. [PubMed:19369195 ]
  6. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed:17081983 ]
  7. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  8. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed:16964243 ]
  9. McKnight GL, Mudri SL, Mathewes SL, Traxinger RR, Marshall S, Sheppard PO, O'Hara PJ: Molecular cloning, cDNA sequence, and bacterial expression of human glutamine:fructose-6-phosphate amidotransferase. J Biol Chem. 1992 Dec 15;267(35):25208-12. [PubMed:1460020 ]
  10. DeHaven JE, Robinson KA, Nelson BA, Buse MG: A novel variant of glutamine: fructose-6-phosphate amidotransferase-1 (GFAT1) mRNA is selectively expressed in striated muscle. Diabetes. 2001 Nov;50(11):2419-24. [PubMed:11679416 ]
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