ID GNPI1_HUMAN Reviewed; 289 AA. AC P46926; B7Z3X4; D3DQE7; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1995, sequence version 1. DT 27-MAR-2024, entry version 203. DE RecName: Full=Glucosamine-6-phosphate isomerase 1; DE EC=3.5.99.6 {ECO:0000269|PubMed:21807125}; DE AltName: Full=Glucosamine-6-phosphate deaminase 1; DE Short=GNPDA 1; DE Short=GlcN6P deaminase 1; DE AltName: Full=Oscillin; GN Name=GNPDA1 {ECO:0000303|PubMed:26887390, ECO:0000312|HGNC:HGNC:4417}; GN Synonyms=GNPI, HLN, KIAA0060; 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 1). RC TISSUE=Brain; RX PubMed=9438414; DOI=10.1096/fasebj.12.1.91; RA Wolosker H., Kline D., Bian Y., Blackshaw S., Cameron A.M., Fralich T.J., RA Schnaar R.L., Snyder S.H.; RT "Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes RT to transporting epithelium and lacks oscillin activity."; RL FASEB J. 12:91-99(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=9714720; DOI=10.1016/s0378-1119(98)00335-7; RA Shevchenko V., Hogben M., Ekong R., Parrington J., Lai F.A.; RT "The human glucosamine-6-phosphate deaminase gene: cDNA cloning and RT expression, genomic organization and chromosomal localization."; RL Gene 216:31-38(1998). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1). RC TISSUE=Testis; RA Hirata S., Koh T., Hoshi K.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., RA Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. The RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Thalamus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Ovary, and Skin; 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 [9] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-64, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [10] 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 [11] RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL RP PROPERTIES, AND MUTAGENESIS OF 268-PRO--ASP-289 AND 275-LYS--ASP-289. RX PubMed=21807125; DOI=10.1016/j.bbapap.2011.07.010; RA Alvarez-Anorve L.I., Alonzo D.A., Mora-Lugo R., Lara-Gonzalez S., RA Bustos-Jaimes I., Plumbridge J., Calcagno M.L.; RT "Allosteric kinetics of the isoform 1 of human glucosamine-6-phosphate RT deaminase."; RL Biochim. Biophys. Acta 1814:1846-1853(2011). RN [12] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. 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 [13] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND SUBUNIT. RX PubMed=12965206; DOI=10.1016/s0014-5793(03)00896-2; RA Arreola R., Valderrama B., Morante M.L., Horjales E.; RT "Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic RT study."; RL FEBS Lett. 551:63-70(2003). CC -!- FUNCTION: Catalyzes the reversible conversion of alpha-D-glucosamine 6- CC phosphate (GlcN-6P) into beta-D-fructose 6-phosphate (Fru-6P) and CC ammonium ion, a regulatory reaction step in de novo uridine CC diphosphate-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc) biosynthesis via CC hexosamine pathway. Deamination is coupled to aldo-keto isomerization CC mediating the metabolic flux from UDP-GlcNAc toward Fru-6P. At high CC ammonium level can drive amination and isomerization of Fru-6P toward CC hexosamines and UDP-GlcNAc synthesis (PubMed:21807125, CC PubMed:26887390). Has a role in fine tuning the metabolic fluctuations CC of cytosolic UDP-GlcNAc and their effects on hyaluronan synthesis that CC occur during tissue remodeling (PubMed:26887390). Seems to trigger CC calcium oscillations in mammalian eggs. These oscillations serve as the CC essential trigger for egg activation and early development of the CC embryo (By similarity). {ECO:0000250|UniProtKB:Q64422, CC ECO:0000269|PubMed:21807125, ECO:0000269|PubMed:26887390}. CC -!- CATALYTIC ACTIVITY: CC Reaction=alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6- CC phosphate + NH4(+); Xref=Rhea:RHEA:12172, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:57634, ChEBI:CHEBI:75989; EC=3.5.99.6; CC Evidence={ECO:0000269|PubMed:21807125}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12173; CC Evidence={ECO:0000305|PubMed:21807125, ECO:0000305|PubMed:26887390}; CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:12174; CC Evidence={ECO:0000305|PubMed:21807125, ECO:0000305|PubMed:26887390}; CC -!- ACTIVITY REGULATION: Allosterically activated by N-acetylglucosamine-6- CC phosphate (GlcNAc6P). {ECO:0000269|PubMed:21807125}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=16.5 mM for alpha-D-glucosamine 6-phosphate (in the presence of CC GlcNAc6P) {ECO:0000269|PubMed:21807125}; CC KM=0.27 mM for alpha-D-glucosamine 6-phosphate (in the absence of CC GlcNAc6P) {ECO:0000269|PubMed:21807125}; CC KM=6.6 mM for beta-D-fructose 6-phosphate (in the presence of CC GlcNAc6P) {ECO:0000269|PubMed:21807125}; CC KM=6.6 mM for NH4(+) (in the presence of GlcNAc6P) CC {ECO:0000269|PubMed:21807125}; CC Note=kcat is 228 sec(-1) for conversion of alpha-D-glucosamine CC 6-phosphate into beta-D-fructose 6-phosphate (in the presence of CC GlcNAc6P). kcat is 0.14 sec(-1) for conversion of alpha-D-glucosamine CC 6-phosphate into beta-D-fructose 6-phosphate (in the absence of CC GlcNAc6P). kcat is 0.84 sec(-1) for conversion of beta-D-fructose CC 6-phosphate into alpha-D-glucosamine 6-phosphate (in the presence of CC GlcNAc6P). {ECO:0000269|PubMed:21807125}; 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:0000305|PubMed:26887390}. CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:12965206}. CC -!- INTERACTION: CC P46926; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-749356, EBI-10178634; CC P46926; Q9NRG1: PRTFDC1; NbExp=3; IntAct=EBI-749356, EBI-739759; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P46926-1; Sequence=Displayed; CC Name=2; CC IsoId=P46926-2; Sequence=VSP_057011; CC -!- SIMILARITY: Belongs to the glucosamine/galactosamine-6-phosphate CC isomerase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA06544.2; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF048826; AAC05123.1; -; mRNA. DR EMBL; AJ002231; CAA05259.1; -; mRNA. DR EMBL; AF029914; AAB84217.1; -; mRNA. DR EMBL; AF035809; AAB88748.1; -; Genomic_DNA. DR EMBL; AF035804; AAB88748.1; JOINED; Genomic_DNA. DR EMBL; AF035805; AAB88748.1; JOINED; Genomic_DNA. DR EMBL; AF035806; AAB88748.1; JOINED; Genomic_DNA. DR EMBL; AF035807; AAB88748.1; JOINED; Genomic_DNA. DR EMBL; AF035808; AAB88748.1; JOINED; Genomic_DNA. DR EMBL; D31766; BAA06544.2; ALT_INIT; mRNA. DR EMBL; AK296452; BAH12360.1; -; mRNA. DR EMBL; AC005740; AAC62119.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61890.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61891.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61892.1; -; Genomic_DNA. DR EMBL; CH471062; EAW61893.1; -; Genomic_DNA. DR EMBL; BC012853; AAH12853.1; -; mRNA. DR EMBL; BC020769; AAH20769.1; -; mRNA. DR EMBL; BC022322; AAH22322.1; -; mRNA. DR CCDS; CCDS4272.1; -. [P46926-1] DR RefSeq; NP_005462.1; NM_005471.4. [P46926-1] DR RefSeq; XP_006714810.1; XM_006714747.2. [P46926-1] DR RefSeq; XP_011535839.1; XM_011537537.1. DR PDB; 1NE7; X-ray; 1.75 A; A/B/C/D/E/F=1-289. DR PDBsum; 1NE7; -. DR AlphaFoldDB; P46926; -. DR SMR; P46926; -. DR BioGRID; 115325; 61. DR IntAct; P46926; 12. DR MINT; P46926; -. DR STRING; 9606.ENSP00000423674; -. DR DrugBank; DB02445; 2-Deoxy-2-Amino Glucitol-6-Phosphate. DR DrugBank; DB02379; Beta-D-Glucose. DR DrugBank; DB03951; N-acetyl-D-glucosamine-6-phosphate. DR GlyGen; P46926; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P46926; -. DR MetOSite; P46926; -. DR PhosphoSitePlus; P46926; -. DR BioMuta; GNPDA1; -. DR EPD; P46926; -. DR jPOST; P46926; -. DR MassIVE; P46926; -. DR MaxQB; P46926; -. DR PaxDb; 9606-ENSP00000423674; -. DR PeptideAtlas; P46926; -. DR ProteomicsDB; 55767; -. [P46926-1] DR ProteomicsDB; 6552; -. DR Pumba; P46926; -. DR Antibodypedia; 606; 271 antibodies from 32 providers. DR DNASU; 10007; -. DR Ensembl; ENST00000311337.11; ENSP00000311876.6; ENSG00000113552.16. [P46926-1] DR Ensembl; ENST00000500692.6; ENSP00000424275.1; ENSG00000113552.16. [P46926-1] DR Ensembl; ENST00000503794.5; ENSP00000423485.1; ENSG00000113552.16. [P46926-1] DR Ensembl; ENST00000508177.5; ENSP00000423674.1; ENSG00000113552.16. [P46926-1] DR GeneID; 10007; -. DR KEGG; hsa:10007; -. DR MANE-Select; ENST00000311337.11; ENSP00000311876.6; NM_005471.5; NP_005462.1. DR UCSC; uc003lmf.5; human. [P46926-1] DR AGR; HGNC:4417; -. DR CTD; 10007; -. DR DisGeNET; 10007; -. DR GeneCards; GNPDA1; -. DR HGNC; HGNC:4417; GNPDA1. DR HPA; ENSG00000113552; Low tissue specificity. DR MIM; 601798; gene. DR neXtProt; NX_P46926; -. DR OpenTargets; ENSG00000113552; -. DR PharmGKB; PA28796; -. DR VEuPathDB; HostDB:ENSG00000113552; -. DR eggNOG; KOG3148; Eukaryota. DR GeneTree; ENSGT00390000014316; -. DR InParanoid; P46926; -. DR OMA; HVITQGI; -. DR OrthoDB; 5475442at2759; -. DR PhylomeDB; P46926; -. DR TreeFam; TF300841; -. DR BRENDA; 3.5.99.6; 2681. DR PathwayCommons; P46926; -. DR Reactome; R-HSA-70171; Glycolysis. DR SABIO-RK; P46926; -. DR SignaLink; P46926; -. DR UniPathway; UPA00113; UER00528. DR BioGRID-ORCS; 10007; 8 hits in 1161 CRISPR screens. DR ChiTaRS; GNPDA1; human. DR EvolutionaryTrace; P46926; -. DR GeneWiki; GNPDA1; -. DR GenomeRNAi; 10007; -. DR Pharos; P46926; Tbio. DR PRO; PR:P46926; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P46926; Protein. DR Bgee; ENSG00000113552; Expressed in type B pancreatic cell and 213 other cell types or tissues. DR ExpressionAtlas; P46926; baseline and differential. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0004342; F:glucosamine-6-phosphate deaminase activity; IDA:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IMP:UniProtKB. DR GO; GO:0006043; P:glucosamine catabolic process; IMP:UniProtKB. DR GO; GO:0006046; P:N-acetylglucosamine catabolic process; IBA:GO_Central. DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IBA:GO_Central. DR GO; GO:0007338; P:single fertilization; TAS:ProtInc. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IMP:UniProtKB. DR CDD; cd01399; GlcN6P_deaminase; 1. DR Gene3D; 3.40.50.1360; -; 1. DR HAMAP; MF_01241; GlcN6P_deamin; 1. DR InterPro; IPR006148; Glc/Gal-6P_isomerase. DR InterPro; IPR004547; Glucosamine6P_isomerase. DR InterPro; IPR018321; Glucosamine6P_isomerase_CS. DR InterPro; IPR037171; NagB/RpiA_transferase-like. DR NCBIfam; TIGR00502; nagB; 1. DR PANTHER; PTHR11280; GLUCOSAMINE-6-PHOSPHATE ISOMERASE; 1. DR PANTHER; PTHR11280:SF8; GLUCOSAMINE-6-PHOSPHATE ISOMERASE 1; 1. DR Pfam; PF01182; Glucosamine_iso; 1. DR SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 1. DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1. DR Genevisible; P46926; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Carbohydrate metabolism; KW Cytoplasm; Hydrolase; Isomerase; Phosphoprotein; Reference proteome. FT CHAIN 1..289 FT /note="Glucosamine-6-phosphate isomerase 1" FT /id="PRO_0000160122" FT ACT_SITE 72 FT /note="Proton acceptor; for enolization step" FT /evidence="ECO:0000250" FT ACT_SITE 141 FT /note="For ring-opening step" FT /evidence="ECO:0000250" FT ACT_SITE 143 FT /note="Proton acceptor; for ring-opening step" FT /evidence="ECO:0000250" FT ACT_SITE 148 FT /note="For ring-opening step" FT /evidence="ECO:0000250" FT MOD_RES 64 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 161 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:O88958" FT VAR_SEQ 69..145 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_057011" FT MUTAGEN 268..289 FT /note="Missing: Decreases hexamer stability and catalytic FT efficiency." FT /evidence="ECO:0000269|PubMed:21807125" FT MUTAGEN 275..289 FT /note="Missing: Decreases catalytic efficiency." FT /evidence="ECO:0000269|PubMed:21807125" FT STRAND 2..8 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 9..27 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 35..39 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 43..57 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 66..74 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 85..92 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 94..96 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 101..103 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 114..127 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 132..136 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 157..161 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 164..170 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 171..173 FT /evidence="ECO:0007829|PDB:1NE7" FT TURN 174..176 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 178..180 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 183..187 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 190..194 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 199..203 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 206..208 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 209..216 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 225..231 FT /evidence="ECO:0007829|PDB:1NE7" FT STRAND 233..240 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 241..244 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 249..257 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 259..262 FT /evidence="ECO:0007829|PDB:1NE7" FT HELIX 263..265 FT /evidence="ECO:0007829|PDB:1NE7" SQ SEQUENCE 289 AA; 32669 MW; 4111F655D574F74F CRC64; MKLIILEHYS QASEWAAKYI RNRIIQFNPG PEKYFTLGLP TGSTPLGCYK KLIEYYKNGD LSFKYVKTFN MDEYVGLPRD HPESYHSFMW NNFFKHIDIH PENTHILDGN AVDLQAECDA FEEKIKAAGG IELFVGGIGP DGHIAFNEPG SSLVSRTRVK TLAMDTILAN ARFFDGELTK VPTMALTVGV GTVMDAREVM ILITGAHKAF ALYKAIEEGV NHMWTVSAFQ QHPRTVFVCD EDATLELKVK TVKYFKGLML VHNKLVDPLY SIKEKETEKS QSSKKPYSD //