HXK1_ARATH
ID HXK1_ARATH Reviewed; 496 AA.
AC Q42525; Q42535;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Hexokinase-1 {ECO:0000303|PubMed:9014361};
DE EC=2.7.1.1 {ECO:0000255|PROSITE-ProRule:PRU01084, ECO:0000269|PubMed:7610198};
DE AltName: Full=Protein GLUCOSE INSENSITIVE 2 {ECO:0000303|PubMed:16920781};
GN Name=HXK1 {ECO:0000303|PubMed:9014361};
GN Synonyms=GIN2 {ECO:0000303|PubMed:16920781};
GN OrderedLocusNames=At4g29130 {ECO:0000312|Araport:AT4G29130};
GN ORFNames=F19B15.160 {ECO:0000312|EMBL:CAB43927.1};
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=7610198; DOI=10.1104/pp.108.2.879;
RA Dai N., Schaffer A.A., Petreikov M., Granot D.;
RT "Arabidopsis thaliana hexokinase cDNA isolated by complementation of yeast
RT cells.";
RL Plant Physiol. 108:879-880(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=9014361; DOI=10.2307/3870367;
RA Jang J.-C., Leon P., Zhou L., Sheen J.;
RT "Hexokinase as a sugar sensor in higher plants.";
RL Plant Cell 9:5-19(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [6]
RP FUNCTION, MUTAGENESIS OF GLY-104; SER-177 AND GLY-416, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=12690200; DOI=10.1126/science.1080585;
RA Moore B., Zhou L., Rolland F., Hall Q., Cheng W.-H., Liu Y.-X., Hwang I.,
RA Jones T., Sheen J.;
RT "Role of the Arabidopsis glucose sensor HXK1 in nutrient, light, and
RT hormonal signaling.";
RL Science 300:332-336(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC STRAIN=cv. Landsberg erecta;
RX PubMed=14671022; DOI=10.1105/tpc.016055;
RA Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J.,
RA Millar A.H.;
RT "Experimental analysis of the Arabidopsis mitochondrial proteome highlights
RT signaling and regulatory components, provides assessment of targeting
RT prediction programs, and indicates plant-specific mitochondrial proteins.";
RL Plant Cell 16:241-256(2004).
RN [8]
RP INTERACTION WITH RPT5B, AND SUBCELLULAR LOCATION.
RX PubMed=17081979; DOI=10.1016/j.cell.2006.09.028;
RA Cho Y.H., Yoo S.D., Sheen J.;
RT "Regulatory functions of nuclear hexokinase1 complex in glucose
RT signaling.";
RL Cell 127:579-589(2006).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16920781; DOI=10.1105/tpc.106.041509;
RA Kim M., Lim J.-H., Ahn C.S., Park K., Kim G.T., Kim W.T., Pai H.-S.;
RT "Mitochondria-associated hexokinases play a role in the control of
RT programmed cell death in Nicotiana benthamiana.";
RL Plant Cell 18:2341-2355(2006).
RN [10]
RP FUNCTION, DISRUPTION PHENOTYPE, AND INTERACTION WITH RHIP1.
RX PubMed=26528314; DOI=10.3389/fpls.2015.00851;
RA Huang J.-P., Tunc-Ozdemir M., Chang Y., Jones A.M.;
RT "Cooperative control between AtRGS1 and AtHXK1 in a WD40-repeat protein
RT pathway in Arabidopsis thaliana.";
RL Front. Plant Sci. 6:851-851(2015).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 30-496 IN COMPLEX WITH GLUCOSE.
RX PubMed=25664748; DOI=10.1107/s1399004714026091;
RA Feng J., Zhao S., Chen X., Wang W., Dong W., Chen J., Shen J.R., Liu L.,
RA Kuang T.;
RT "Biochemical and structural study of Arabidopsis hexokinase 1.";
RL Acta Crystallogr. D 71:367-375(2015).
CC -!- FUNCTION: Fructose and glucose phosphorylating enzyme (PubMed:7610198).
CC May be involved in the phosphorylation of glucose during the export
CC from mitochondrion to cytosol (PubMed:16920781). Acts as sugar sensor
CC which may regulate sugar-dependent gene repression or activation
CC (PubMed:9014361, PubMed:12690200, PubMed:26528314). Mediates the
CC effects of sugar on plant growth and development independently of its
CC catalytic activity or the sugar metabolism (PubMed:9014361,
CC PubMed:12690200). May regulate the execution of program cell death in
CC plant cells (PubMed:16920781). Promotes roots and leaves growth
CC (PubMed:26528314). {ECO:0000269|PubMed:12690200,
CC ECO:0000269|PubMed:16920781, ECO:0000269|PubMed:26528314,
CC ECO:0000269|PubMed:7610198, ECO:0000269|PubMed:9014361}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-hexose = ADP + D-hexose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61567, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01084,
CC ECO:0000269|PubMed:7610198};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000269|PubMed:7610198};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-fructose = ADP + D-fructose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:16125, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:37721, ChEBI:CHEBI:61527, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:7610198};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000269|PubMed:7610198};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC Evidence={ECO:0000269|PubMed:7610198};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000269|PubMed:7610198};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for glucose {ECO:0000269|PubMed:7610198};
CC KM=17 mM for fructose {ECO:0000269|PubMed:7610198};
CC Note=Measured in yeast lacking glucose and hexose kinase activity.
CC {ECO:0000269|PubMed:7610198};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000305|PubMed:7610198}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000305|PubMed:7610198}.
CC -!- SUBUNIT: Interacts with RPT5B in nucleus. Interacts with RHIP1
CC (PubMed:26528314). {ECO:0000269|PubMed:17081979,
CC ECO:0000269|PubMed:26528314}.
CC -!- INTERACTION:
CC Q42525; Q96292: ACT2; NbExp=2; IntAct=EBI-1644489, EBI-1644538;
CC Q42525; Q9SRH5: VDAC1; NbExp=2; IntAct=EBI-1644489, EBI-1644501;
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane; Single-pass
CC membrane protein. Nucleus {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers and siliques, at
CC intermediate levels in roots and stems, and at lower levels in rosette
CC and cauline leaves. {ECO:0000269|PubMed:9014361}.
CC -!- DISRUPTION PHENOTYPE: Plants display a glucose-insensitive phenotype
CC which allows them to grow on high glucose concentration medium (>6%
CC glucose) (PubMed:12690200, PubMed:26528314). Dwarf plants with reduced
CC roots and leaves growth (PubMed:26528314).
CC {ECO:0000269|PubMed:12690200, ECO:0000269|PubMed:26528314}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60333.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18754; AAA60333.1; ALT_INIT; mRNA.
DR EMBL; U28214; AAB49908.1; -; mRNA.
DR EMBL; AL078470; CAB43927.1; -; Genomic_DNA.
DR EMBL; AL161574; CAB79671.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE85590.1; -; Genomic_DNA.
DR EMBL; AY075658; AAL77665.1; -; mRNA.
DR EMBL; AY124809; AAM70518.1; -; mRNA.
DR PIR; S71205; S71205.
DR RefSeq; NP_194642.1; NM_119057.4.
DR PDB; 4QS7; X-ray; 2.00 A; A=30-496.
DR PDB; 4QS8; X-ray; 1.80 A; A=30-496.
DR PDB; 4QS9; X-ray; 2.10 A; A=30-496.
DR PDBsum; 4QS7; -.
DR PDBsum; 4QS8; -.
DR PDBsum; 4QS9; -.
DR AlphaFoldDB; Q42525; -.
DR SMR; Q42525; -.
DR BioGRID; 14321; 12.
DR IntAct; Q42525; 3.
DR STRING; 3702.AT4G29130.1; -.
DR MoonProt; Q42525; -.
DR iPTMnet; Q42525; -.
DR SwissPalm; Q42525; -.
DR PaxDb; Q42525; -.
DR PRIDE; Q42525; -.
DR ProteomicsDB; 228861; -.
DR EnsemblPlants; AT4G29130.1; AT4G29130.1; AT4G29130.
DR GeneID; 829034; -.
DR Gramene; AT4G29130.1; AT4G29130.1; AT4G29130.
DR KEGG; ath:AT4G29130; -.
DR Araport; AT4G29130; -.
DR TAIR; locus:2119931; AT4G29130.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_5_1_1; -.
DR InParanoid; Q42525; -.
DR OMA; VATECED; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; Q42525; -.
DR BioCyc; ARA:AT4G29130-MON; -.
DR BioCyc; MetaCyc:AT4G29130-MON; -.
DR BRENDA; 2.7.1.1; 399.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR PRO; PR:Q42525; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q42525; baseline and differential.
DR Genevisible; Q42525; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005741; C:mitochondrial outer membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
DR GO; GO:0032991; C:protein-containing complex; IMP:CAFA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0001046; F:core promoter sequence-specific DNA binding; IMP:CAFA.
DR GO; GO:0008865; F:fructokinase activity; IDA:TAIR.
DR GO; GO:0004340; F:glucokinase activity; IDA:TAIR.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; IDA:TAIR.
DR GO; GO:0008270; F:zinc ion binding; HDA:TAIR.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0001678; P:cellular glucose homeostasis; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0010255; P:glucose mediated signaling pathway; IMP:CAFA.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0019320; P:hexose catabolic process; IDA:TAIR.
DR GO; GO:0012501; P:programmed cell death; IMP:TAIR.
DR GO; GO:2000032; P:regulation of secondary shoot formation; IMP:TAIR.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:CAFA.
DR GO; GO:0090332; P:stomatal closure; IMP:TAIR.
DR GO; GO:0010182; P:sugar mediated signaling pathway; TAS:TAIR.
DR GO; GO:0010148; P:transpiration; IMP:TAIR.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
DR InterPro; IPR019807; Hexokinase_BS.
DR InterPro; IPR022673; Hexokinase_C.
DR InterPro; IPR022672; Hexokinase_N.
DR PANTHER; PTHR19443; PTHR19443; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycolysis; Kinase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Nucleus;
KW Reference proteome; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..496
FT /note="Hexokinase-1"
FT /id="PRO_0000197612"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..487
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 90..228
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 229..476
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 25..26
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 101..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 101..105
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 177..178
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 194..195
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25664748,
FT ECO:0007744|PDB:4QS7, ECO:0007744|PDB:4QS9"
FT BINDING 229..230
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25664748,
FT ECO:0007744|PDB:4QS7, ECO:0007744|PDB:4QS9"
FT BINDING 230
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 253
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 253
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 255..256
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25664748,
FT ECO:0007744|PDB:4QS7, ECO:0007744|PDB:4QS9"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25664748,
FT ECO:0007744|PDB:4QS7, ECO:0007744|PDB:4QS9"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:25664748,
FT ECO:0007744|PDB:4QS7, ECO:0007744|PDB:4QS9"
FT BINDING 320..321
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 357..361
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 439..441
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 441..445
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT BINDING 478
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P19367"
FT MUTAGEN 104
FT /note="G->A: Abolishes glucose phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:12690200"
FT MUTAGEN 177
FT /note="S->D: Abolishes glucose phosphorylation activity."
FT /evidence="ECO:0000269|PubMed:12690200"
FT MUTAGEN 416
FT /note="G->A: In gin2-2; insensitive to glucose."
FT /evidence="ECO:0000269|PubMed:12690200"
FT HELIX 34..48
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 52..71
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 94..115
FT /evidence="ECO:0007829|PDB:4QS8"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 121..130
FT /evidence="ECO:0007829|PDB:4QS8"
FT TURN 133..136
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:4QS7"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 207..216
FT /evidence="ECO:0007829|PDB:4QS8"
FT TURN 217..219
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 222..228
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 230..241
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 245..262
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 285..287
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 320..338
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 342..344
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 347..350
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 357..364
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 369..371
FT /evidence="ECO:0007829|PDB:4QS9"
FT HELIX 372..382
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 389..420
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 434..440
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 441..444
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 447..466
FT /evidence="ECO:0007829|PDB:4QS8"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:4QS8"
FT TURN 477..479
FT /evidence="ECO:0007829|PDB:4QS8"
FT HELIX 480..488
FT /evidence="ECO:0007829|PDB:4QS8"
SQ SEQUENCE 496 AA; 53707 MW; 6DC81CE114E0B52B CRC64;
MGKVAVGATV VCTAAVCAVA VLVVRRRMQS SGKWGRVLAI LKAFEEDCAT PISKLRQVAD
AMTVEMHAGL ASDGGSKLKM LISYVDNLPS GDEKGLFYAL DLGGTNFRVM RVLLGGKQER
VVKQEFEEVS IPPHLMTGGS DELFNFIAEA LAKFVATECE DFHLPEGRQR ELGFTFSFPV
KQTSLSSGSL IKWTKGFSIE EAVGQDVVGA LNKALERVGL DMRIAALVND TVGTLAGGRY
YNPDVVAAVI LGTGTNAAYV ERATAIPKWH GLLPKSGEMV INMEWGNFRS SHLPLTEFDH
TLDFESLNPG EQILEKIISG MYLGEILRRV LLKMAEDAAF FGDTVPSKLR IPFIIRTPHM
SAMHNDTSPD LKIVGSKIKD ILEVPTTSLK MRKVVISLCN IIATRGARLS AAGIYGILKK
LGRDTTKDEE VQKSVIAMDG GLFEHYTQFS ECMESSLKEL LGDEASGSVE VTHSNDGSGI
GAALLAASHS LYLEDS
