YL446_YEAST
ID YL446_YEAST Reviewed; 433 AA.
AC Q06204; D6VZ80; Q6B2U1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Putative hexokinase YLR446W;
DE EC=2.7.1.1 {ECO:0000250|UniProtKB:P04806};
GN OrderedLocusNames=YLR446W;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169871;
RA Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W.,
RA Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A.,
RA Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K.,
RA Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K., Koetter P., Louis E.J.,
RA Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S.,
RA Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D.,
RA Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M.,
RA Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P.,
RA Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M.,
RA Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K.,
RA Zollner A., Hani J., Hoheisel J.D.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
RL Nature 387:87-90(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
CC -!- FUNCTION: Catalyzes the phosphorylation of hexose, such as D-glucose
CC and D-fructose, to hexose 6-phosphate (D-glucose 6-phosphate and D-
CC fructose 6-phosphate, respectively). Mediates the initial step of
CC glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-
CC phosphate. {ECO:0000250|UniProtKB:P04806}.
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:P04806};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC Evidence={ECO:0000250|UniProtKB:P04806};
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:P04806};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16126;
CC Evidence={ECO:0000250|UniProtKB:P04806};
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:P04806};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC Evidence={ECO:0000250|UniProtKB:P04806};
CC -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC {ECO:0000250|UniProtKB:P04806}.
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 1/4.
CC {ECO:0000250|UniProtKB:P04806}.
CC -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC ProRule:PRU01084, ECO:0000305}.
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DR EMBL; U22382; AAB67530.1; -; Genomic_DNA.
DR EMBL; AY692639; AAT92658.1; -; Genomic_DNA.
DR EMBL; BK006945; DAA09746.1; -; Genomic_DNA.
DR PIR; S55968; S55968.
DR RefSeq; NP_013551.1; NM_001182334.1.
DR AlphaFoldDB; Q06204; -.
DR SMR; Q06204; -.
DR BioGRID; 31704; 24.
DR DIP; DIP-4630N; -.
DR IntAct; Q06204; 3.
DR STRING; 4932.YLR446W; -.
DR MaxQB; Q06204; -.
DR PaxDb; Q06204; -.
DR PRIDE; Q06204; -.
DR EnsemblFungi; YLR446W_mRNA; YLR446W; YLR446W.
DR GeneID; 851167; -.
DR KEGG; sce:YLR446W; -.
DR SGD; S000004438; YLR446W.
DR VEuPathDB; FungiDB:YLR446W; -.
DR eggNOG; KOG1369; Eukaryota.
DR GeneTree; ENSGT00950000182787; -.
DR HOGENOM; CLU_014393_4_1_1; -.
DR InParanoid; Q06204; -.
DR OMA; TICTRLA; -.
DR BioCyc; YEAST:G3O-32501-MON; -.
DR Reactome; R-SCE-170822; Regulation of Glucokinase by Glucokinase Regulatory Protein.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-70171; Glycolysis.
DR UniPathway; UPA00109; UER00180.
DR UniPathway; UPA00242; -.
DR PRO; PR:Q06204; -.
DR Proteomes; UP000002311; Chromosome XII.
DR RNAct; Q06204; protein.
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-KW.
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:0001678; P:cellular glucose homeostasis; 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 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 3: Inferred from homology;
KW ATP-binding; Glycolysis; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..433
FT /note="Putative hexokinase YLR446W"
FT /id="PRO_0000268190"
FT DOMAIN 1..424
FT /note="Hexokinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 51..194
FT /note="Hexokinase small subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT REGION 132..154
FT /note="Glucose-binding"
FT /evidence="ECO:0000255"
FT REGION 195..413
FT /note="Hexokinase large subdomain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT CONFLICT 52
FT /note="K -> E (in Ref. 3; AAT92658)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 433 AA; 48969 MW; 704555676B3DA755 CRC64;
MTIESTLARE LESLILPADS IVNVVDQFQE ELLSRLQTNT ISMLPQCLVP DKRSRWNPED
KILTIDFGGT RLKFAIISLP QIVIEYNDAF ELTYNIVDSN FFNQIIYTIC TRLAANGYIK
KKNESSEASK FFVSVTFSFP LNPEGEVVAM GKGFVMTDTL QGSTVKQLIQ SSFHRIISEN
IEEFFCTMNV CHVINDAIAV SLTSKFICEN DSISLIIGTG TNACFEVPYG YLPPFKRDAL
RETLPSSYNK ETLNFKHVLI NSEIGFIGKN VIALQPFDIH GAISYEMPLE CVTSGKWLPL
SLKNILLQYN IIPKNFPVEF NGELVCQLAE DCTNAWFENE HYALICQIAR LLIKRAAFYV
AAIVQAIDII TGCKNYNFIH IGYVGSFLHN SNFYREQIKY YSSIHIKLQF LNHSNLLGAA
IATYLNKSDN QVQ
