ID GFPT1_HUMAN Reviewed; 699 AA. AC Q06210; Q53QE6; Q9BXF8; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 219. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1; DE EC=2.6.1.16 {ECO:0000250|UniProtKB:P82808}; DE AltName: Full=D-fructose-6-phosphate amidotransferase 1; DE AltName: Full=Glutamine:fructose-6-phosphate amidotransferase 1; DE Short=GFAT 1; DE Short=GFAT1 {ECO:0000303|PubMed:26887390}; DE AltName: Full=Hexosephosphate aminotransferase 1; GN Name=GFPT1; Synonyms=GFAT, GFPT; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=1460020; DOI=10.1016/s0021-9258(19)74026-5; RA McKnight G.L., Mudri S.L., Mathewes S.L., Traxinger R.R., Marshall S., RA Sheppard P.O., O'Hara P.J.; RT "Molecular cloning, cDNA sequence, and bacterial expression of human RT glutamine:fructose-6-phosphate amidotransferase."; RL J. Biol. Chem. 267:25208-25212(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] OF 124-275 (ISOFORM 1), AND TISSUE SPECIFICITY. RX PubMed=11679416; DOI=10.2337/diabetes.50.11.2419; RA DeHaven J.E., Robinson K.A., Nelson B.A., Buse M.G.; RT "A novel variant of glutamine:fructose-6-phosphate amidotransferase-1 RT (GFAT1) mRNA is selectively expressed in striated muscle."; RL Diabetes 50:2419-2424(2001). RN [5] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-261, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-261, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [17] RP FUNCTION. RX PubMed=26887390; DOI=10.1093/glycob/cww019; RA Oikari S., Makkonen K., Deen A.J., Tyni I., Kaernae R., Tammi R.H., RA Tammi M.I.; RT "Hexosamine biosynthesis in keratinocytes: roles of GFAT and GNPDA enzymes RT in the maintenance of UDP-GlcNAc content and hyaluronan synthesis."; RL Glycobiology 26:710-722(2016). RN [18] {ECO:0007744|PDB:2ZJ3, ECO:0007744|PDB:2ZJ4} RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 332-699, SUBUNIT, AND RP SUBSTRATE-BINDING SITES. RX PubMed=19059404; DOI=10.1016/j.febslet.2008.11.041; RA Nakaishi Y., Bando M., Shimizu H., Watanabe K., Goto F., Tsuge H., RA Kondo K., Komatsu M.; RT "Structural analysis of human glutamine:fructose-6-phosphate RT amidotransferase, a key regulator in type 2 diabetes."; RL FEBS Lett. 583:163-167(2009). RN [19] RP VARIANTS CMS12 ALA-15; MET-15; VAL-43; CYS-111; THR-121; PHE-199; TYR-366; RP HIS-403; HIS-452; THR-509; THR-510; TRP-514 AND TRP-530. RX PubMed=21310273; DOI=10.1016/j.ajhg.2011.01.008; RA Senderek J., Muller J.S., Dusl M., Strom T.M., Guergueltcheva V., RA Diepolder I., Laval S.H., Maxwell S., Cossins J., Krause S., Muelas N., RA Vilchez J.J., Colomer J., Mallebrera C.J., Nascimento A., Nafissi S., RA Kariminejad A., Nilipour Y., Bozorgmehr B., Najmabadi H., Rodolico C., RA Sieb J.P., Steinlein O.K., Schlotter B., Schoser B., Kirschner J., RA Herrmann R., Voit T., Oldfors A., Lindbergh C., Urtizberea A., RA von der Hagen M., Hubner A., Palace J., Bushby K., Straub V., Beeson D., RA Abicht A., Lochmuller H.; RT "Hexosamine biosynthetic pathway mutations cause neuromuscular transmission RT defect."; RL Am. J. Hum. Genet. 88:162-172(2011). CC -!- FUNCTION: Controls the flux of glucose into the hexosamine pathway. CC Most likely involved in regulating the availability of precursors for CC N- and O-linked glycosylation of proteins. Regulates the circadian CC expression of clock genes BMAL1 and CRY1 (By similarity). Has a role in CC fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc and its CC effects on hyaluronan synthesis that occur during tissue remodeling CC (PubMed:26887390). {ECO:0000250|UniProtKB:P47856, CC ECO:0000269|PubMed:26887390}. CC -!- CATALYTIC ACTIVITY: CC Reaction=D-fructose 6-phosphate + L-glutamine = D-glucosamine 6- CC phosphate + L-glutamate; Xref=Rhea:RHEA:13237, ChEBI:CHEBI:29985, CC ChEBI:CHEBI:58359, ChEBI:CHEBI:58725, ChEBI:CHEBI:61527; EC=2.6.1.16; CC Evidence={ECO:0000250|UniProtKB:P82808}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; alpha-D-glucosamine 6-phosphate from D- CC fructose 6-phosphate: step 1/1. {ECO:0000250|UniProtKB:P82808}. CC -!- SUBUNIT: Homotetramer (Probable), may also exist as homodimers. CC {ECO:0000269|PubMed:19059404}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=GFAT1m; CC IsoId=Q06210-1; Sequence=Displayed; CC Name=2; CC IsoId=Q06210-2; Sequence=VSP_007497; CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in skeletal CC muscle. Not expressed in brain. Seems to be selectively expressed in CC striated muscle. {ECO:0000269|PubMed:11679416}. CC -!- DISEASE: Myasthenic syndrome, congenital, 12 (CMS12) [MIM:610542]: A CC form of congenital myasthenic syndrome, a group of disorders CC characterized by failure of neuromuscular transmission, including pre- CC synaptic, synaptic, and post-synaptic disorders that are not of CC autoimmune origin. Clinical features are easy fatigability and muscle CC weakness. CMS12 is characterized by onset of proximal muscle weakness CC in the first decade. Individuals with this condition have a CC recognizable pattern of weakness of shoulder and pelvic girdle muscles, CC and sparing of ocular or facial muscles. EMG classically shows a CC decremental response to repeated nerve stimulation, a sign of CC neuromuscular junction dysfunction. Affected individuals show a CC favorable response to acetylcholinesterase (AChE) inhibitors. CC {ECO:0000269|PubMed:21310273}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M90516; AAA58502.1; -; mRNA. DR EMBL; AC114772; AAY14827.1; -; Genomic_DNA. DR EMBL; BC045641; AAH45641.1; -; mRNA. DR EMBL; AF334737; AAK15342.1; -; mRNA. DR CCDS; CCDS33216.1; -. [Q06210-2] DR CCDS; CCDS58713.1; -. [Q06210-1] DR PIR; A45055; A45055. DR RefSeq; NP_001231639.1; NM_001244710.1. [Q06210-1] DR RefSeq; NP_002047.2; NM_002056.3. [Q06210-2] DR PDB; 2V4M; X-ray; 2.29 A; A/B/C/D=332-699. DR PDB; 2ZJ3; X-ray; 1.90 A; A=332-699. DR PDB; 2ZJ4; X-ray; 2.20 A; A=332-699. DR PDB; 6R4E; X-ray; 2.35 A; A/B=1-699. DR PDB; 6R4F; X-ray; 2.50 A; A/B=1-699. DR PDB; 6R4G; X-ray; 2.50 A; A/B=1-699. DR PDB; 6R4H; X-ray; 2.24 A; A/B=1-699. DR PDB; 6R4I; X-ray; 2.59 A; A/B=1-699. DR PDB; 6R4J; X-ray; 2.42 A; A/B=1-699. DR PDB; 6SVM; X-ray; 2.48 A; A/B=1-699. DR PDB; 6SVO; X-ray; 2.33 A; A/B=1-699. DR PDB; 6SVP; X-ray; 2.53 A; A/B=1-699. DR PDB; 6SVQ; X-ray; 2.72 A; A/B=1-699. DR PDB; 6ZMJ; X-ray; 2.77 A; A/B=1-699. DR PDB; 6ZMK; X-ray; 2.38 A; A/B=1-699. DR PDB; 7NDL; X-ray; 2.22 A; A/B=2-699. DR PDBsum; 2V4M; -. DR PDBsum; 2ZJ3; -. DR PDBsum; 2ZJ4; -. DR PDBsum; 6R4E; -. DR PDBsum; 6R4F; -. DR PDBsum; 6R4G; -. DR PDBsum; 6R4H; -. DR PDBsum; 6R4I; -. DR PDBsum; 6R4J; -. DR PDBsum; 6SVM; -. DR PDBsum; 6SVO; -. DR PDBsum; 6SVP; -. DR PDBsum; 6SVQ; -. DR PDBsum; 6ZMJ; -. DR PDBsum; 6ZMK; -. DR PDBsum; 7NDL; -. DR AlphaFoldDB; Q06210; -. DR SMR; Q06210; -. DR BioGRID; 108941; 144. DR IntAct; Q06210; 26. DR MINT; Q06210; -. DR STRING; 9606.ENSP00000349860; -. DR BindingDB; Q06210; -. DR ChEMBL; CHEMBL1909481; -. DR MEROPS; C44.970; -. DR GlyGen; Q06210; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q06210; -. DR MetOSite; Q06210; -. DR PhosphoSitePlus; Q06210; -. DR SwissPalm; Q06210; -. DR BioMuta; GFPT1; -. DR DMDM; 30923274; -. DR CPTAC; CPTAC-377; -. DR CPTAC; CPTAC-378; -. DR EPD; Q06210; -. DR jPOST; Q06210; -. DR MassIVE; Q06210; -. DR MaxQB; Q06210; -. DR PaxDb; 9606-ENSP00000349860; -. DR PeptideAtlas; Q06210; -. DR ProteomicsDB; 58423; -. [Q06210-1] DR ProteomicsDB; 58424; -. [Q06210-2] DR Pumba; Q06210; -. DR Antibodypedia; 47446; 253 antibodies from 33 providers. DR DNASU; 2673; -. DR Ensembl; ENST00000357308.9; ENSP00000349860.4; ENSG00000198380.13. [Q06210-1] DR Ensembl; ENST00000361060.5; ENSP00000354347.4; ENSG00000198380.13. [Q06210-2] DR GeneID; 2673; -. DR KEGG; hsa:2673; -. DR MANE-Select; ENST00000357308.9; ENSP00000349860.4; NM_001244710.2; NP_001231639.1. DR UCSC; uc002sfh.4; human. [Q06210-1] DR AGR; HGNC:4241; -. DR CTD; 2673; -. DR DisGeNET; 2673; -. DR GeneCards; GFPT1; -. DR GeneReviews; GFPT1; -. DR HGNC; HGNC:4241; GFPT1. DR HPA; ENSG00000198380; Low tissue specificity. DR MalaCards; GFPT1; -. DR MIM; 138292; gene. DR MIM; 610542; phenotype. DR neXtProt; NX_Q06210; -. DR OpenTargets; ENSG00000198380; -. DR Orphanet; 353327; Congenital myasthenic syndromes with glycosylation defect. DR PharmGKB; PA28651; -. DR VEuPathDB; HostDB:ENSG00000198380; -. DR eggNOG; KOG1268; Eukaryota. DR GeneTree; ENSGT00940000158488; -. DR HOGENOM; CLU_012520_5_0_1; -. DR InParanoid; Q06210; -. DR OMA; ASEYRYA; -. DR OrthoDB; 1705390at2759; -. DR PhylomeDB; Q06210; -. DR TreeFam; TF300864; -. DR BioCyc; MetaCyc:HS09974-MONOMER; -. DR BRENDA; 2.6.1.16; 2681. DR PathwayCommons; Q06210; -. DR Reactome; R-HSA-381038; XBP1(S) activates chaperone genes. DR Reactome; R-HSA-4085023; Defective GFPT1 causes CMSTA1. DR Reactome; R-HSA-446210; Synthesis of UDP-N-acetyl-glucosamine. DR SignaLink; Q06210; -. DR SIGNOR; Q06210; -. DR UniPathway; UPA00113; UER00528. DR BioGRID-ORCS; 2673; 280 hits in 1154 CRISPR screens. DR ChiTaRS; GFPT1; human. DR EvolutionaryTrace; Q06210; -. DR GeneWiki; GFPT1; -. DR GenomeRNAi; 2673; -. DR Pharos; Q06210; Tchem. DR PRO; PR:Q06210; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q06210; Protein. DR Bgee; ENSG00000198380; Expressed in mucosa of sigmoid colon and 210 other cell types or tissues. DR ExpressionAtlas; Q06210; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central. DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB. DR GO; GO:0006112; P:energy reserve metabolic process; TAS:ProtInc. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:UniProtKB. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central. DR CDD; cd00714; GFAT; 1. DR CDD; cd05008; SIS_GlmS_GlmD_1; 1. DR CDD; cd05009; SIS_GlmS_GlmD_2; 1. DR Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR005855; GFAT. DR InterPro; IPR047084; GFAT_N. DR InterPro; IPR035466; GlmS/AgaS_SIS. DR InterPro; IPR035490; GlmS/FrlB_SIS. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001347; SIS_dom. DR InterPro; IPR046348; SIS_dom_sf. DR NCBIfam; TIGR01135; glmS; 1. DR PANTHER; PTHR10937; GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING; 1. DR PANTHER; PTHR10937:SF12; GLUTAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE [ISOMERIZING] 1; 1. DR Pfam; PF13522; GATase_6; 1. DR Pfam; PF01380; SIS; 2. DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1. DR SUPFAM; SSF53697; SIS domain; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS51464; SIS; 2. DR Genevisible; Q06210; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Aminotransferase; Biological rhythms; KW Congenital myasthenic syndrome; Disease variant; KW Glutamine amidotransferase; Phosphoprotein; Reference proteome; Repeat; KW Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..699 FT /note="Glutamine--fructose-6-phosphate aminotransferase FT [isomerizing] 1" FT /id="PRO_0000135280" FT DOMAIN 2..305 FT /note="Glutamine amidotransferase type-2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00609" FT DOMAIN 377..516 FT /note="SIS 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797" FT DOMAIN 548..689 FT /note="SIS 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00797" FT REGION 313..680 FT /note="Isomerase" FT ACT_SITE 2 FT /note="For GATase activity" FT /evidence="ECO:0000250|UniProtKB:P14742" FT BINDING 394..395 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19059404, FT ECO:0007744|PDB:2V4M, ECO:0007744|PDB:2ZJ3, FT ECO:0007744|PDB:2ZJ4" FT BINDING 439..441 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19059404, FT ECO:0007744|PDB:2V4M, ECO:0007744|PDB:2ZJ3, FT ECO:0007744|PDB:2ZJ4" FT BINDING 444 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19059404, FT ECO:0007744|PDB:2V4M, ECO:0007744|PDB:2ZJ3, FT ECO:0007744|PDB:2ZJ4" FT BINDING 595 FT /ligand="substrate" FT /evidence="ECO:0000269|PubMed:19059404, FT ECO:0007744|PDB:2V4M, ECO:0007744|PDB:2ZJ3, FT ECO:0007744|PDB:2ZJ4" FT MOD_RES 103 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 261 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VAR_SEQ 229..246 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:1460020, FT ECO:0000303|PubMed:15489334" FT /id="VSP_007497" FT VARIANT 15 FT /note="T -> A (in CMS12; dbSNP:rs387906638)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065339" FT VARIANT 15 FT /note="T -> M (in CMS12; dbSNP:rs751097758)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065340" FT VARIANT 43 FT /note="D -> V (in CMS12)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065341" FT VARIANT 111 FT /note="R -> C (in CMS12; dbSNP:rs201322234)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065342" FT VARIANT 121 FT /note="I -> T (in CMS12; dbSNP:rs753866967)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065343" FT VARIANT 199 FT /note="V -> F (in CMS12; dbSNP:rs1378864996)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065344" FT VARIANT 366 FT /note="D -> Y (in CMS12; dbSNP:rs1574058076)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065345" FT VARIANT 403 FT /note="R -> H (in CMS12; dbSNP:rs1363498649)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065346" FT VARIANT 452 FT /note="R -> H (in CMS12)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065347" FT VARIANT 509 FT /note="M -> T (in CMS12; dbSNP:rs1558728601)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065348" FT VARIANT 510 FT /note="M -> T (in CMS12)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065349" FT VARIANT 514 FT /note="R -> W (in CMS12)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065350" FT VARIANT 530 FT /note="R -> W (in CMS12; dbSNP:rs1024585946)" FT /evidence="ECO:0000269|PubMed:21310273" FT /id="VAR_065351" FT STRAND 3..15 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 16..28 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 29..33 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 36..43 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 57..64 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 66..74 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 84..95 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 98..100 FT /evidence="ECO:0007829|PDB:7NDL" FT TURN 104..106 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 107..113 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 117..126 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 129..138 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 146..149 FT /evidence="ECO:0007829|PDB:6ZMK" FT HELIX 150..161 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 170..178 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 183..191 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 198..205 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 220..226 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 263..265 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 267..269 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 273..280 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 281..283 FT /evidence="ECO:0007829|PDB:7NDL" FT TURN 284..287 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 289..293 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 299..303 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 306..311 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:7NDL" FT HELIX 331..334 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 339..341 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 342..348 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 350..358 FT /evidence="ECO:0007829|PDB:2ZJ3" FT TURN 359..361 FT /evidence="ECO:0007829|PDB:2ZJ3" FT TURN 364..367 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 372..374 FT /evidence="ECO:0007829|PDB:2ZJ3" FT TURN 375..377 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 378..383 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 385..391 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 393..410 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 414..418 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 419..424 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 433..442 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 445..456 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 460..466 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 471..475 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 476..481 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 489..491 FT /evidence="ECO:0007829|PDB:2ZJ4" FT HELIX 494..510 FT /evidence="ECO:0007829|PDB:2ZJ3" FT TURN 511..513 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 515..517 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 518..539 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 542..552 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 556..562 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 564..566 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 567..581 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 584..589 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 590..595 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 597..600 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 602..605 FT /evidence="ECO:0007829|PDB:7NDL" FT STRAND 607..611 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 617..629 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 635..639 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 643..648 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 650..655 FT /evidence="ECO:0007829|PDB:2ZJ3" FT TURN 660..662 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 663..667 FT /evidence="ECO:0007829|PDB:2ZJ3" FT HELIX 669..681 FT /evidence="ECO:0007829|PDB:2ZJ3" FT STRAND 686..688 FT /evidence="ECO:0007829|PDB:2ZJ3" SQ SEQUENCE 699 AA; 78806 MW; F0533A7B762C7B98 CRC64; MCGIFAYLNY HVPRTRREIL ETLIKGLQRL EYRGYDSAGV GFDGGNDKDW EANACKIQLI KKKGKVKALD EEVHKQQDMD LDIEFDVHLG IAHTRWATHG EPSPVNSHPQ RSDKNNEFIV IHNGIITNYK DLKKFLESKG YDFESETDTE TIAKLVKYMY DNRESQDTSF TTLVERVIQQ LEGAFALVFK SVHFPGQAVG TRRGSPLLIG VRSEHKLSTD HIPILYRTAR TQIGSKFTRW GSQGERGKDK KGSCNLSRVD STTCLFPVEE KAVEYYFASD ASAVIEHTNR VIFLEDDDVA AVVDGRLSIH RIKRTAGDHP GRAVQTLQME LQQIMKGNFS SFMQKEIFEQ PESVVNTMRG RVNFDDYTVN LGGLKDHIKE IQRCRRLILI ACGTSYHAGV ATRQVLEELT ELPVMVELAS DFLDRNTPVF RDDVCFFLSQ SGETADTLMG LRYCKERGAL TVGITNTVGS SISRETDCGV HINAGPEIGV ASTKAYTSQF VSLVMFALMM CDDRISMQER RKEIMLGLKR LPDLIKEVLS MDDEIQKLAT ELYHQKSVLI MGRGYHYATC LEGALKIKEI TYMHSEGILA GELKHGPLAL VDKLMPVIMI IMRDHTYAKC QNALQQVVAR QGRPVVICDK EDTETIKNTK RTIKVPHSVD CLQGILSVIP LQLLAFHLAV LRGYDVDFPR NLAKSVTVE //