ID Q19440_CAEEL Unreviewed; 500 AA.
AC Q19440;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 24-JAN-2024, entry version 171.
DE RecName: Full=Phosphotransferase {ECO:0000256|RuleBase:RU362007};
DE EC=2.7.1.- {ECO:0000256|RuleBase:RU362007};
GN Name=hxk-1 {ECO:0000313|EMBL:CAA99826.1,
GN ECO:0000313|WormBase:F14B4.2a};
GN ORFNames=CELE_F14B4.2 {ECO:0000313|EMBL:CAA99826.1}, F14B4.2
GN {ECO:0000313|WormBase:F14B4.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000313|EMBL:CAA99826.1, ECO:0000313|Proteomes:UP000001940};
RN [1] {ECO:0000313|EMBL:CAA99826.1, ECO:0000313|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000313|EMBL:CAA99826.1,
RC ECO:0000313|Proteomes:UP000001940};
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RA Sulson J.E., Waterston R.;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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:0000256|ARBA:ARBA00001397};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000256|ARBA:ARBA00001397};
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:0000256|ARBA:ARBA00000435};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000256|ARBA:ARBA00000435};
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:0000256|ARBA:ARBA00000417};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000256|ARBA:ARBA00000417};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000256|ARBA:ARBA00004888}.
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000256|ARBA:ARBA00005028}.
CC -!- SIMILARITY: Belongs to the hexokinase family.
CC {ECO:0000256|ARBA:ARBA00009225, ECO:0000256|RuleBase:RU362007}.
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DR EMBL; BX284601; CAA99826.1; -; Genomic_DNA.
DR PIR; T20869; T20869.
DR RefSeq; NP_001021106.1; NM_001025935.2.
DR AlphaFoldDB; Q19440; -.
DR SMR; Q19440; -.
DR DIP; DIP-26887N; -.
DR IntAct; Q19440; 1.
DR STRING; 6239.F14B4.2a.2; -.
DR EPD; Q19440; -.
DR PaxDb; 6239-F14B4-2a; -.
DR PeptideAtlas; Q19440; -.
DR EnsemblMetazoa; F14B4.2a.1; F14B4.2a.1; WBGene00008780.
DR GeneID; 172751; -.
DR UCSC; F14B4.2b; c. elegans.
DR AGR; WB:WBGene00008780; -.
DR WormBase; F14B4.2a; CE05628; WBGene00008780; hxk-1.
DR eggNOG; KOG1369; Eukaryota.
DR InParanoid; Q19440; -.
DR OMA; YPNFEGY; -.
DR OrthoDB; 5481886at2759; -.
DR PhylomeDB; Q19440; -.
DR Reactome; R-CEL-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-70171; Glycolysis.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR Proteomes; UP000001940; Chromosome I.
DR Bgee; WBGene00008780; Expressed in pharyngeal muscle cell (C elegans) and 4 other cell types or tissues.
DR ExpressionAtlas; Q19440; baseline and differential.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0008865; F:fructokinase activity; IBA:GO_Central.
DR GO; GO:0004340; F:glucokinase activity; IBA:GO_Central.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IBA:GO_Central.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central.
DR GO; GO:0001678; P:intracellular glucose homeostasis; IBA:GO_Central.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
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; HEXOKINASE; 1.
DR PANTHER; PTHR19443:SF16; HEXOKINASE TYPE 1-RELATED; 1.
DR Pfam; PF00349; Hexokinase_1; 1.
DR Pfam; PF03727; Hexokinase_2; 1.
DR PRINTS; PR00475; HEXOKINASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00378; HEXOKINASE_1; 1.
DR PROSITE; PS51748; HEXOKINASE_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362007};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU362007};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|RuleBase:RU362007};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362007};
KW Proteomics identification {ECO:0007829|EPD:Q19440,
KW ECO:0007829|PeptideAtlas:Q19440};
KW Reference proteome {ECO:0000313|Proteomes:UP000001940};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362007}.
FT DOMAIN 39..233
FT /note="Hexokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00349"
FT DOMAIN 239..480
FT /note="Hexokinase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF03727"
SQ SEQUENCE 500 AA; 54670 MW; 446EF1799DFAFEC2 CRC64;
MSSIVCHPIL DSQNGIATDA VIKKQRPPPL VLSRPKDLIQ EACQRLVLSD QQLRRIMQSM
EKSMEQGLAT STKKVAVKML PTYVDSVPNG TESGDFLALD LGGTNFRVLH IKLQGKETKM
TGKIFRVPES IMRGTGEALF DHIAGCMAKF MGENDLKDAQ KLPLGFTFSF PCEQEGLTKG
KLVTWTKGFK ASGVEGVDVV TLLHEACHRR KDIDIDVVAL LNDTVGTLMA CAFQENSCQI
GVIVGTGTNA CYMERLDRIP KLAGYVDEHG VTPEEMIINT EWGAFGDDGA LDFLRTEWDE
VVDRESINPG QHLYEKMISG MYMGECARVV LEDLAKQGLL FGGNSDAISV PHCFPTKFVS
EIDSDLLEDD DRTFQKTYQI LEDIGVEMIT ANDCANVAYV CSLISTRAAH LTAAGIAMLL
NRMNKKHVTV GVDGSVYRFH PTYPTLLDAK IGELIVGDIE YKLMLSEDGS GRGAALVAAV
ATRLKEEKLA ASLSSSSSNQ
//