HXK4_ARATH
ID HXK4_ARATH Reviewed; 502 AA.
AC Q56XE8; Q9LJZ7;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Hexokinase-4;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:P93834};
GN OrderedLocusNames=At3g20040; ORFNames=MAL21.4;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10907853; DOI=10.1093/dnares/7.3.217;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 3. II. Sequence
RT features of the 4,251,695 bp regions covered by 90 P1, TAC and BAC
RT clones.";
RL DNA Res. 7:217-221(2000).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-502.
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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).
CC -!- FUNCTION: Fructose and glucose phosphorylating enzyme (By similarity).
CC May be involved in the phosphorylation of glucose during the export
CC from mitochondrion to cytosol (By similarity).
CC {ECO:0000250|UniProtKB:P93834}.
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:0000250|UniProtKB:P93834};
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:0000250|UniProtKB:P93834};
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:0000250|UniProtKB:P93834};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:P93834}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000250|UniProtKB:P93834}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:14671022}; Single-pass membrane protein
CC {ECO:0000269|PubMed:14671022}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD93730.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AP000383; BAB01861.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE76323.1; -; Genomic_DNA.
DR EMBL; AK221726; BAD93730.1; ALT_INIT; mRNA.
DR RefSeq; NP_188639.2; NM_112895.3.
DR AlphaFoldDB; Q56XE8; -.
DR SMR; Q56XE8; -.
DR BioGRID; 6875; 1.
DR STRING; 3702.AT3G20040.1; -.
DR PaxDb; Q56XE8; -.
DR PRIDE; Q56XE8; -.
DR ProteomicsDB; 232205; -.
DR EnsemblPlants; AT3G20040.1; AT3G20040.1; AT3G20040.
DR GeneID; 821543; -.
DR Gramene; AT3G20040.1; AT3G20040.1; AT3G20040.
DR KEGG; ath:AT3G20040; -.
DR Araport; AT3G20040; -.
DR TAIR; locus:2087590; AT3G20040.
DR eggNOG; KOG1369; Eukaryota.
DR HOGENOM; CLU_014393_5_1_1; -.
DR InParanoid; Q56XE8; -.
DR OMA; EILHDDC; -.
DR OrthoDB; 1153545at2759; -.
DR PhylomeDB; Q56XE8; -.
DR BioCyc; ARA:AT3G20040-MON; -.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR PRO; PR:Q56XE8; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q56XE8; baseline and differential.
DR Genevisible; Q56XE8; AT.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0031307; C:integral component of mitochondrial outer membrane; IDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; IDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0004396; F:hexokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0001678; P:cellular glucose homeostasis; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR001312; Hexokinase.
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; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Glycolysis; Kinase; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleotide-binding; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..502
FT /note="Hexokinase-4"
FT /id="PRO_0000259632"
FT TRANSMEM 4..24
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 35..491
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 171..197
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 229..480
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT BINDING 101..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 502
FT /note="V -> I (in Ref. 3; BAD93730)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 502 AA; 54955 MW; 354D46773BA91199 CRC64;
MGKVLVMLTA AAAVVACSVA TVMVRRRMKG RRKWRRVVGL LKDLEEACET PLGRLRQMVD
AIAVEMQAGL VSEGGSKLKM LLTFVDDLPN GSETGTYYAL HLGGSYFRII KVHLGGQRSS
LEVQDVERHS IPTSLMNSTS EVLFDFLASS LQRFIEKEGN DFSLSQPLKR ELAFTFSFPV
KQTSISSGVL IKWTKGFAIS EMAGEDIAEC LQGALNKRGL DIRVAALVND TVGALSFGHF
HDPDTIAAVV FGTGSNACYL ERTDAIIKCQ NPRTTSGSMV VNMEWGNFWS SRLPRTSYDL
ELDAESMNSN DMGFEKMIGG MYLGDIVRRV ILRMSQESDI FGPISSILST PFVLRTNSVS
AMHEDDTSEL QEVARILKDL GVSEVPMKVR KLVVKICDVV TRRAARLAAA GIAGILKKVG
RDGSGGGRRS DKQIMRRTVV AVEGGLYLNY RMFREYMDEA LRDILGEDVA QHVVVKAMED
GSSIGSALLL ASSQSVQTIP SV
