KHK_MOUSE
ID KHK_MOUSE Reviewed; 298 AA.
AC P97328; Q91WU8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Ketohexokinase {ECO:0000312|MGI:MGI:1096353};
DE EC=2.7.1.3 {ECO:0000250|UniProtKB:P50053};
DE AltName: Full=Hepatic fructokinase;
GN Name=Khk {ECO:0000312|MGI:MGI:1096353};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Hayward B.E., Bonthron D.T.;
RT "Structure and function of the fructokinase gene.";
RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of the ketose sugar fructose to
CC fructose-1-phosphate. {ECO:0000250|UniProtKB:P50053}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + beta-D-fructose = ADP + beta-D-fructose 1-phosphate +
CC H(+); Xref=Rhea:RHEA:18145, ChEBI:CHEBI:15378, ChEBI:CHEBI:28645,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:138881, ChEBI:CHEBI:456216;
CC EC=2.7.1.3; Evidence={ECO:0000250|UniProtKB:P50053};
CC -!- ACTIVITY REGULATION: Requires potassium. Inhibition by ADP (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Carbohydrate metabolism; fructose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P50053}.
CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family.
CC {ECO:0000305}.
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DR EMBL; Y09335; CAA70515.1; -; mRNA.
DR EMBL; BC013464; AAH13464.1; -; mRNA.
DR CCDS; CCDS39050.1; -.
DR RefSeq; NP_032465.2; NM_008439.4.
DR PDB; 6P2D; X-ray; 1.79 A; A=2-298.
DR PDBsum; 6P2D; -.
DR AlphaFoldDB; P97328; -.
DR SMR; P97328; -.
DR IntAct; P97328; 2.
DR iPTMnet; P97328; -.
DR PhosphoSitePlus; P97328; -.
DR SwissPalm; P97328; -.
DR SWISS-2DPAGE; P97328; -.
DR jPOST; P97328; -.
DR MaxQB; P97328; -.
DR PaxDb; P97328; -.
DR PeptideAtlas; P97328; -.
DR PRIDE; P97328; -.
DR ProteomicsDB; 263597; -.
DR DNASU; 16548; -.
DR GeneID; 16548; -.
DR KEGG; mmu:16548; -.
DR UCSC; uc008wwn.1; mouse.
DR CTD; 3795; -.
DR MGI; MGI:1096353; Khk.
DR eggNOG; KOG2947; Eukaryota.
DR InParanoid; P97328; -.
DR PhylomeDB; P97328; -.
DR TreeFam; TF323942; -.
DR BRENDA; 2.7.1.3; 3474.
DR Reactome; R-MMU-70350; Fructose catabolism.
DR UniPathway; UPA00202; -.
DR BioGRID-ORCS; 16548; 4 hits in 73 CRISPR screens.
DR ChiTaRS; Khk; mouse.
DR PRO; PR:P97328; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P97328; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004454; F:ketohexokinase activity; IDA:MGI.
DR GO; GO:0006001; P:fructose catabolic process; IDA:MGI.
DR GO; GO:0061624; P:fructose catabolic process to hydroxyacetone phosphate and glyceraldehyde-3-phosphate; IMP:MGI.
DR GO; GO:0006000; P:fructose metabolic process; IMP:MGI.
DR GO; GO:0061625; P:glycolytic process through fructose-1-phosphate; IC:MGI.
DR GO; GO:0070873; P:regulation of glycogen metabolic process; IMP:MGI.
DR GO; GO:0009750; P:response to fructose; IBA:GO_Central.
DR GO; GO:0009749; P:response to glucose; ISO:MGI.
DR GO; GO:0032868; P:response to insulin; ISO:MGI.
DR GO; GO:0009744; P:response to sucrose; ISO:MGI.
DR GO; GO:0010043; P:response to zinc ion; ISO:MGI.
DR CDD; cd01939; Ketohexokinase; 1.
DR Gene3D; 3.40.1190.20; -; 1.
DR InterPro; IPR034093; KHK.
DR InterPro; IPR011611; PfkB_dom.
DR InterPro; IPR029056; Ribokinase-like.
DR Pfam; PF00294; PfkB; 1.
DR SUPFAM; SSF53613; SSF53613; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..298
FT /note="Ketohexokinase"
FT /id="PRO_0000080089"
FT BINDING 15
FT /ligand="beta-D-fructose"
FT /ligand_id="ChEBI:CHEBI:28645"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 41
FT /ligand="beta-D-fructose"
FT /ligand_id="ChEBI:CHEBI:28645"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 42
FT /ligand="beta-D-fructose"
FT /ligand_id="ChEBI:CHEBI:28645"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 45
FT /ligand="beta-D-fructose"
FT /ligand_id="ChEBI:CHEBI:28645"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 226..229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 255..258
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT BINDING 258
FT /ligand="beta-D-fructose"
FT /ligand_id="ChEBI:CHEBI:28645"
FT /evidence="ECO:0000250|UniProtKB:P50053"
FT CONFLICT 203
FT /note="P -> S (in Ref. 2; AAH13464)"
FT /evidence="ECO:0000305"
FT STRAND 5..10
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 13..22
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 33..40
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 42..52
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 67..79
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 96..102
FT /evidence="ECO:0007829|PDB:6P2D"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 108..111
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 122..126
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 133..142
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 143..158
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 167..172
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 177..184
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 185..191
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 193..198
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 204..211
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 212..214
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 226..228
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 230..233
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 239..242
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 256..269
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 274..288
FT /evidence="ECO:0007829|PDB:6P2D"
FT STRAND 291..294
FT /evidence="ECO:0007829|PDB:6P2D"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:6P2D"
SQ SEQUENCE 298 AA; 32750 MW; A8181D781A6136D4 CRC64;
MEEKQILCVG LVVLDIINVV DKYPEEDTDR RCLSQRWQRG GNASNSCTVL SLLGARCAFM
GSLAPGHVAD FLVADFRQRG VDVSQVTWQS QGDTPCSCCI VNNSNGSRTI ILYDTNLPDV
SAKDFEKVDL TRFKWIHIEG RNASEQVKML QRIEEHNAKQ PLPQKVRVSV EIEKPREELF
QLFSYGEVVF VSKDVAKHLG FQPAVEALRG LYSRVKKGAT LVCAWAEEGA DALGPDGQLL
HSDAFPPPRV VDTLGAGDTF NASVIFSLSK GNSMQEALRF GCQVAGKKCG LQGFDGIV
