GFPT1_HUMAN
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 03-AUG-2022, entry version 210.
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 ARNTL/BMAL1 and CRY1 (By similarity). Has a
CC role in fine tuning the metabolic fluctuations of cytosolic UDP-GlcNAc
CC and its effects on hyaluronan synthesis that occur during tissue
CC remodeling (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.
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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; 122.
DR IntAct; Q06210; 23.
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; Q06210; -.
DR PeptideAtlas; Q06210; -.
DR PRIDE; Q06210; -.
DR ProteomicsDB; 58423; -. [Q06210-1]
DR ProteomicsDB; 58424; -. [Q06210-2]
DR Antibodypedia; 47446; 235 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 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; 262871at2759; -.
DR PhylomeDB; Q06210; -.
DR TreeFam; TF300864; -.
DR BioCyc; MetaCyc:HS09974-MON; -.
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; 265 hits in 1073 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 208 other tissues.
DR ExpressionAtlas; Q06210; baseline and differential.
DR Genevisible; Q06210; HS.
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; cd05008; SIS_GlmS_GlmD_1; 1.
DR CDD; cd05009; SIS_GlmS_GlmD_2; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR017932; GATase_2_dom.
DR InterPro; IPR035466; GlmS/AgaS_SIS.
DR InterPro; IPR035490; GlmS/FrlB_SIS.
DR InterPro; IPR005855; GlmS_trans.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR Pfam; PF01380; SIS; 2.
DR SUPFAM; SSF53697; SSF53697; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
DR TIGRFAMs; TIGR01135; glmS; 1.
DR PROSITE; PS51278; GATASE_TYPE_2; 1.
DR PROSITE; PS51464; SIS; 2.
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
