GNPI1_HUMAN
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 03-AUG-2022, entry version 194.
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 6-
CC 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 6-
CC 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};
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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. [P46926-1]
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; 50.
DR IntAct; P46926; 11.
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; P46926; -.
DR PeptideAtlas; P46926; -.
DR PRIDE; P46926; -.
DR ProteomicsDB; 55767; -. [P46926-1]
DR ProteomicsDB; 6552; -.
DR Antibodypedia; 606; 255 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 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; FNEPCSS; -.
DR OrthoDB; 1425290at2759; -.
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 1083 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 211 other tissues.
DR ExpressionAtlas; P46926; baseline and differential.
DR Genevisible; P46926; HS.
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: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 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 PANTHER; PTHR11280; PTHR11280; 1.
DR Pfam; PF01182; Glucosamine_iso; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
DR TIGRFAMs; TIGR00502; nagB; 1.
DR PROSITE; PS01161; GLC_GALNAC_ISOMERASE; 1.
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
