ID   HXKG_KLULA              Reviewed;         481 AA.
AC   Q6CUZ3;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   24-JAN-2024, entry version 103.
DE   RecName: Full=Glucokinase-1;
DE            EC=2.7.1.2 {ECO:0000269|PubMed:17573926};
DE   AltName: Full=Glucose kinase 1;
DE            Short=GLK-1;
DE   AltName: Full=Hexokinase GLK1 {ECO:0000305};
DE            EC=2.7.1.1 {ECO:0000269|PubMed:17573926};
GN   Name=GLK1; OrderedLocusNames=KLLA0C01155g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 /
RC   WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17573926; DOI=10.1111/j.1567-1364.2007.00259.x;
RA   Kettner K., Mueller E.-C., Otto A., Roedel G., Breunig K.D., Kriegel T.M.;
RT   "Identification and characterization of a novel glucose-phosphorylating
RT   enzyme in Kluyveromyces lactis.";
RL   FEMS Yeast Res. 7:683-692(2007).
CC   -!- FUNCTION: Glukokinase specific for aldohexoses. Phosphorylates glucose
CC       and mannose, but not fructose. {ECO:0000269|PubMed:17573926}.
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=2.7.1.2;
CC         Evidence={ECO:0000269|PubMed:17573926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17826;
CC         Evidence={ECO:0000269|PubMed:17573926};
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:0000269|PubMed:17573926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22741;
CC         Evidence={ECO:0000269|PubMed:17573926};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-mannose = ADP + D-mannose 6-phosphate + H(+);
CC         Xref=Rhea:RHEA:11028, ChEBI:CHEBI:4208, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58735, ChEBI:CHEBI:456216; EC=2.7.1.1;
CC         Evidence={ECO:0000269|PubMed:17573926};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11029;
CC         Evidence={ECO:0000269|PubMed:17573926};
CC   -!- PATHWAY: Carbohydrate metabolism; hexose metabolism.
CC       {ECO:0000269|PubMed:17573926}.
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 1/4.
CC       {ECO:0000269|PubMed:17573926}.
CC   -!- SIMILARITY: Belongs to the hexokinase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01084, ECO:0000305}.
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DR   EMBL; CR382123; CAH01097.1; -; Genomic_DNA.
DR   RefSeq; XP_452246.1; XM_452246.1.
DR   PDB; 6R2N; X-ray; 2.60 A; A/B/C=2-481.
DR   PDBsum; 6R2N; -.
DR   AlphaFoldDB; Q6CUZ3; -.
DR   SMR; Q6CUZ3; -.
DR   STRING; 284590.Q6CUZ3; -.
DR   PaxDb; 284590-Q6CUZ3; -.
DR   GeneID; 2892353; -.
DR   KEGG; kla:KLLA0_C01155g; -.
DR   eggNOG; KOG1369; Eukaryota.
DR   HOGENOM; CLU_014393_5_0_1; -.
DR   InParanoid; Q6CUZ3; -.
DR   OMA; YPNFEGY; -.
DR   BRENDA; 2.7.1.2; 2825.
DR   UniPathway; UPA00109; UER00180.
DR   UniPathway; UPA00242; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR   GO; GO:0019158; F:mannokinase activity; IEA:RHEA.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019318; P:hexose metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0001678; P:intracellular glucose homeostasis; IEA:InterPro.
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:SF30; GLUCOKINASE-1-RELATED; 1.
DR   PANTHER; PTHR19443; HEXOKINASE; 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   3D-structure; ATP-binding; Glycolysis; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..481
FT                   /note="Glucokinase-1"
FT                   /id="PRO_0000364088"
FT   DOMAIN          4..477
FT                   /note="Hexokinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          64..204
FT                   /note="Hexokinase small subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   REGION          146..172
FT                   /note="Glucose-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          205..466
FT                   /note="Hexokinase large subdomain"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01084"
FT   BINDING         101
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   BINDING         466..471
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
FT   HELIX           4..16
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           21..38
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          68..77
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          79..91
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          94..103
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           106..109
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           117..135
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            137..142
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          146..150
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          155..159
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          162..165
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            176..179
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           182..192
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          198..204
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           206..217
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            223..225
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          226..245
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           246..248
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           254..262
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          267..271
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           274..276
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            277..280
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          282..284
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           288..297
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           305..310
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            312..314
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           315..328
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           348..355
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            359..363
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           364..374
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           380..412
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          415..420
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          422..429
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           430..434
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           438..448
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           452..456
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   STRAND          459..463
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   TURN            467..469
FT                   /evidence="ECO:0007829|PDB:6R2N"
FT   HELIX           470..477
FT                   /evidence="ECO:0007829|PDB:6R2N"
SQ   SEQUENCE   481 AA;  53757 MW;  3894D9AA9FD5BEF5 CRC64;
     MSDPKLTKAV DSICDQFIVT KSKISQLTEY FIDCMEKGLE PCESDISQNK GLPMIPTFVT
     DKPSGQEHGV TMLAADLGGT NFRVCSVELL GNHEFKIEQE KSKIPTFFFQ DDHHVTSKDL
     FQHMALITHQ FLTKHHKDVI QDYKWKMGFT FSYPVDQTSL SSGKLIRWTK GFKIGDTVGQ
     DVVQLFQQEL NDIGLSNVHV VALTNDTTGT LLARCYASSD AARAINEPVI GCIFGTGTNG
     CYMEKLENIH KLDPASREEL LSQGKTHMCI NTEWGSFDNE LNHLPTTSYD IKIDQQFSTN
     PGFHLFEKRV SGLYLGEILR NILLDLEKQE LFDLKESVLK NNPFILTTET LSHIEIDTVE
     NDLQDTRDAL LKAADLETTF EERVLIQKLV RAISRRAAFL AAVPIAAILI KTNALNQSYH
     CQVEVGCDGS VVEHYPGFRS MMRHALALSP IGPEGERDVH LRISKDGSGV GAALCALHAN
     Y
//