Q42525 (HXK1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Hexokinase-1
EC=2.7.1.1

Alternative name(s):
Protein GLUCOSE INSENSITIVE 2

Gene names

Name:	HXK1
Synonyms:	GIN2
Ordered Locus Names:	At4g29130
ORF Names:	F19B15.160

Organism

Arabidopsis thaliana (Mouse-ear cress) [Reference proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Fructose and glucose phosphorylating enzyme. May be involved in the phosphorylation of glucose during the export from mitochondrion to cytosol. Acts as sugar sensor which may regulate sugar-dependent gene repression or activation. Mediates the effects of sugar on plant growth and development independently of its catalytic activity or the sugar metabolism. May regulate the execution of program cell death in plant cells. Ref.2 Ref.6 Ref.9
Catalytic activity	ATP + D-hexose = ADP + D-hexose 6-phosphate.
Subunit structure	Interacts with RPT5B in nucleus. Ref.8
Subcellular location	Mitochondrion outer membrane; Single-pass membrane protein. Nucleus Ref.8 Ref.9.
Tissue specificity	Highly expressed in flowers and siliques, at intermediate levels in roots and stems, and at lower levels in rosette and cauline leaves. Ref.2
Disruption phenotype	Plants display a glucose-insensitive phenotype which allows them to grow on high glucose concentration medium (>6% glucose). Ref.6
Sequence similarities	Belongs to the hexokinase family.
Biophysicochemical properties	Kinetic parameters: Measured in yeast lacking glucose and hexose kinase activity. KM=44 µM for glucose Ref.1 KM=17 mM for fructose
Sequence caution	The sequence AAA60333.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Glycolysis
Cellular component	Membrane Mitochondrion Mitochondrion outer membrane Nucleus
Domain	Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucose mediated signaling pathway Inferred from mutant phenotype Ref.6. Source: TAIR glycolysis Inferred from electronic annotation. Source: UniProtKB-KW hexose catabolic process Inferred from direct assay PubMed 10402427. Source: TAIR programmed cell death Inferred from mutant phenotype Ref.9. Source: TAIR stomatal closure Inferred from mutant phenotype PubMed 22451715. Source: TAIR transpiration Inferred from mutant phenotype PubMed 22451715. Source: TAIR
Cellular_component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW mitochondrial outer membrane Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from direct assay Ref.7PubMed 16618929PubMed 18481082PubMed 22923678. Source: TAIR nucleus Inferred from direct assay Ref.8. Source: TAIR plastid Inferred from direct assay PubMed 16618929. Source: TAIR vacuolar membrane Inferred from direct assay PubMed 17151019. Source: TAIR
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fructokinase activity Inferred from direct assay PubMed 10402427. Source: TAIR glucokinase activity Inferred from direct assay PubMed 10402427PubMed 11851922. Source: TAIR zinc ion binding Inferred from direct assay PubMed 20018591. Source: TAIR
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ACT2	Q96292	2	EBI-1644489,EBI-1644538
VDAC1	Q9SRH5	2	EBI-1644489,EBI-1644501

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 496	496	Hexokinase-1		PRO_0000197612
Regions
	Transmembrane	4 – 24	21	Helical; Potential
	Nucleotide binding	101 – 106	6	ATP Potential
	Region	171 – 197	27	Glucose-binding Potential
Experimental info
	Mutagenesis	104	1	G → A: Abolishes glucose phosphorylation activity. Ref.6
	Mutagenesis	177	1	S → D: Abolishes glucose phosphorylation activity. Ref.6
	Mutagenesis	416	1	G → A in gin2-2; insensitive to glucose. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q42525 [UniParc]. Last modified December 1, 2000. Version 2. Checksum: 6DC81CE114E0B52B	FASTA	496	53,707
	10 20 30 40 50 60 MGKVAVGATV VCTAAVCAVA VLVVRRRMQS SGKWGRVLAI LKAFEEDCAT PISKLRQVAD 70 80 90 100 110 120 AMTVEMHAGL ASDGGSKLKM LISYVDNLPS GDEKGLFYAL DLGGTNFRVM RVLLGGKQER 130 140 150 160 170 180 VVKQEFEEVS IPPHLMTGGS DELFNFIAEA LAKFVATECE DFHLPEGRQR ELGFTFSFPV 190 200 210 220 230 240 KQTSLSSGSL IKWTKGFSIE EAVGQDVVGA LNKALERVGL DMRIAALVND TVGTLAGGRY 250 260 270 280 290 300 YNPDVVAAVI LGTGTNAAYV ERATAIPKWH GLLPKSGEMV INMEWGNFRS SHLPLTEFDH 310 320 330 340 350 360 TLDFESLNPG EQILEKIISG MYLGEILRRV LLKMAEDAAF FGDTVPSKLR IPFIIRTPHM 370 380 390 400 410 420 SAMHNDTSPD LKIVGSKIKD ILEVPTTSLK MRKVVISLCN IIATRGARLS AAGIYGILKK 430 440 450 460 470 480 LGRDTTKDEE VQKSVIAMDG GLFEHYTQFS ECMESSLKEL LGDEASGSVE VTHSNDGSGI 490 GAALLAASHS LYLEDS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Arabidopsis thaliana hexokinase cDNA isolated by complementation of yeast cells." Dai N., Schaffer A.A., Petreikov M., Granot D. Plant Physiol. 108:879-880(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], BIOPHYSICOCHEMICAL PROPERTIES. Strain: cv. Landsberg erecta.
[2]	"Hexokinase as a sugar sensor in higher plants." Jang J.-C., Leon P., Zhou L., Sheen J. Plant Cell 9:5-19(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY. Strain: cv. Landsberg erecta.
[3]	"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana." Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B. , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R. Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[5]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[6]	"Role of the Arabidopsis glucose sensor HXK1 in nutrient, light, and hormonal signaling." Moore B., Zhou L., Rolland F., Hall Q., Cheng W.-H., Liu Y.-X., Hwang I., Jones T., Sheen J. Science 300:332-336(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF GLY-104; SER-177 AND GLY-416, DISRUPTION PHENOTYPE. Strain: cv. Landsberg erecta.
[7]	"Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins." Heazlewood J.L., Tonti-Filippini J.S., Gout A.M., Day D.A., Whelan J., Millar A.H. Plant Cell 16:241-256(2004) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Strain: cv. Landsberg erecta.
[8]	"Regulatory functions of nuclear hexokinase1 complex in glucose signaling." Cho Y.H., Yoo S.D., Sheen J. Cell 127:579-589(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RPT5B, SUBCELLULAR LOCATION.
[9]	"Mitochondria-associated hexokinases play a role in the control of programmed cell death in Nicotiana benthamiana." Kim M., Lim J.-H., Ahn C.S., Park K., Kim G.T., Kim W.T., Pai H.-S. Plant Cell 18:2341-2355(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U18754 mRNA. Translation: AAA60333.1. Different initiation. U28214 mRNA. Translation: AAB49908.1. AL078470 Genomic DNA. Translation: CAB43927.1. AL161574 Genomic DNA. Translation: CAB79671.1. CP002687 Genomic DNA. Translation: AEE85590.1. AY075658 mRNA. Translation: AAL77665.1. AY124809 mRNA. Translation: AAM70518.1.
IPI	IPI00542953.
PIR	S71205.
RefSeq	NP_194642.1. NM_119057.3.
UniGene	At.24726. At.70249.
3D structure databases
ProteinModelPortal	Q42525.
SMR	Q42525. Positions 54-486.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q42525. 3 interactions.
Proteomic databases
PaxDb	Q42525.
PRIDE	Q42525.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT4G29130.1; AT4G29130.1; AT4G29130.
GeneID	829034.
KEGG	ath:AT4G29130.
Organism-specific databases
GeneFarm	4274. 430.
TAIR	At4g29130.
Phylogenomic databases
eggNOG	COG5026.
HOGENOM	HOG000162670.
InParanoid	Q42525.
KO	K00844.
OMA	ANDCANV.
PhylomeDB	Q42525.
ProtClustDB	PLN02405.
Enzyme and pathway databases
BioCyc	ARA:AT4G29130-MONOMER. MetaCyc:AT4G29130-MONOMER.
BRENDA	2.7.1.1. 399.
Gene expression databases
ArrayExpress	Q42525.
Genevestigator	Q42525.
GermOnline	AT4G29130. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR001312. Hexokinase. IPR022673. Hexokinase_C. IPR019807. Hexokinase_CS. IPR022672. Hexokinase_N. [Graphical view]
PANTHER	PTHR19443. PTHR19443. 1 hit.
Pfam	PF00349. Hexokinase_1. 1 hit. PF03727. Hexokinase_2. 1 hit. [Graphical view]
PRINTS	PR00475. HEXOKINASE.
PROSITE	PS00378. HEXOKINASES. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

HXK1_ARATH

Accession

Primary (citable) accession number: Q42525
Secondary accession number(s): Q42535

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program