ID   GLPK_YEAST              Reviewed;         709 AA.
AC   P32190; D3DKT6;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   02-SEP-2026, entry version 198.
DE   RecName: Full=Glycerol kinase;
DE            Short=GK;
DE            Short=Glycerokinase;
DE            EC=2.7.1.30 {ECO:0000305|PubMed:8358828};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase;
GN   Name=GUT1; OrderedLocusNames=YHL032C;
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 [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC 204511 / S288c / AB972;
RX   PubMed=8358828; DOI=10.1007/bf00324660;
RA   Pavlik P., Simon M., Schuster T., Ruis H.;
RT   "The glycerol kinase (GUT1) gene of Saccharomyces cerevisiae: cloning and
RT   characterization.";
RL   Curr. Genet. 24:21-25(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=8091229; DOI=10.1126/science.8091229;
RA   Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Dover J., Du Z.,
RA   Favello A., Fulton L., Gattung S., Geisel C., Kirsten J., Kucaba T.,
RA   Hillier L.W., Jier M., Johnston L., Langston Y., Latreille P., Louis E.J.,
RA   Macri C., Mardis E., Menezes S., Mouser L., Nhan M., Rifkin L., Riles L.,
RA   St Peter H., Trevaskis E., Vaughan K., Vignati D., Wilcox L., Wohldman P.,
RA   Waterston R., Wilson R., Vaudin M.;
RT   "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome
RT   VIII.";
RL   Science 265:2077-2082(1994).
RN   [3]
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).
CC   -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC       metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
CC       glycerol 3-phosphate. {ECO:0000305|PubMed:8358828}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycerol + ATP = sn-glycerol 3-phosphate + ADP + H(+);
CC         Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC         EC=2.7.1.30; Evidence={ECO:0000305|PubMed:8358828};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21645;
CC         Evidence={ECO:0000305|PubMed:8358828};
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC       pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000305|PubMed:8358828}.
CC   -!- INTERACTION:
CC       P32190; P40106: GPP2; NbExp=2; IntAct=EBI-7694, EBI-7836;
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X69049; CAA48791.1; -; Genomic_DNA.
DR   EMBL; U11583; AAB65044.1; -; Genomic_DNA.
DR   EMBL; BK006934; DAA06653.1; -; Genomic_DNA.
DR   PIR; S33907; S33907.
DR   RefSeq; NP_011831.1; NM_001179112.1.
DR   AlphaFoldDB; P32190; -.
DR   SMR; P32190; -.
DR   BioGRID; 36390; 56.
DR   DIP; DIP-6761N; -.
DR   FunCoup; P32190; 449.
DR   IntAct; P32190; 3.
DR   MINT; P32190; -.
DR   STRING; 4932.YHL032C; -.
DR   GlyGen; P32190; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; P32190; -.
DR   PaxDb; 4932-YHL032C; -.
DR   PeptideAtlas; P32190; -.
DR   EnsemblFungi; YHL032C_mRNA; YHL032C; YHL032C.
DR   GeneID; 856353; -.
DR   KEGG; sce:YHL032C; -.
DR   AGR; SGD:S000001024; -.
DR   SGD; S000001024; GUT1.
DR   VEuPathDB; FungiDB:YHL032C; -.
DR   eggNOG; KOG2517; Eukaryota.
DR   HOGENOM; CLU_009281_2_2_1; -.
DR   InParanoid; P32190; -.
DR   OMA; FMLMNIG; -.
DR   OrthoDB; 5422795at2759; -.
DR   BioCyc; YEAST:YHL032C-MONOMER; -.
DR   Reactome; R-SCE-75109; Triglyceride biosynthesis.
DR   UniPathway; UPA00618; UER00672.
DR   BioGRID-ORCS; 856353; 7 hits in 10 CRISPR screens.
DR   PRO; PR:P32190; -.
DR   Proteomes; UP000002311; Chromosome VIII.
DR   RNAct; P32190; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR   GO; GO:0004370; F:glycerol kinase activity; IMP:SGD.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006071; P:glycerol metabolic process; IMP:SGD.
DR   GO; GO:0046167; P:glycerol-3-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR   CDD; cd07792; ASKHA_NBD_FGGY_GK1-3-like; 1.
DR   FunFam; 3.30.420.40:FF:000086; Glycerol kinase; 1.
DR   FunFam; 3.30.420.40:FF:000108; Glycerol kinase, glycosomal; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   InterPro; IPR042018; GK1-3_metazoan-type.
DR   InterPro; IPR005999; Glycerol_kin.
DR   NCBIfam; TIGR01311; glycerol_kin; 1.
DR   PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..709
FT                   /note="Glycerol kinase"
FT                   /id="PRO_0000059542"
FT   REGION          86..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         56
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         258
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         408
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         463
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         584..588
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   709 AA;  79824 MW;  12B42C4DABE49FF6 CRC64;
     MFPSLFRLVV FSKRYIFRSS QRLYTSLKQE QSRMSKIMED LRSDYVPLIA SIDVGTTSSR
     CILFNRWGQD VSKHQIEYST SASKGKIGVS GLRRPSTAPA RETPNAGDIK TSGKPIFSAE
     GYAIQETKFL KIEELDLDFH NEPTLKFPKP GWVECHPQKL LVNVVQCLAS SLLSLQTINS
     ERVANGLPPY KVICMGIANM RETTILWSRR TGKPIVNYGI VWNDTRTIKI VRDKWQNTSV
     DRQLQLRQKT GLPLLSTYFS CSKLRWFLDN EPLCTKAYEE NDLMFGTVDT WLIYQLTKQK
     AFVSDVTNAS RTGFMNLSTL KYDNELLEFW GIDKNLIHMP EIVSSSQYYG DFGIPDWIME
     KLHDSPKTVL RDLVKRNLPI QGCLGDQSAS MVGQLAYKPG AAKCTYGTGC FLLYNTGTKK
     LISQHGALTT LAFWFPHLQE YGGQKPELSK PHFALEGSVA VAGAVVQWLR DNLRLIDKSE
     DVGPIASTVP DSGGVVFVPA FSGLFAPYWD PDARATIMGM SQFTTASHIA RAAVEGVCFQ
     ARAILKAMSS DAFGEGSKDR DFLEEISDVT YEKSPLSVLA VDGGMSRSNE VMQIQADILG
     PCVKVRRSPT AECTALGAAI AANMAFKDVN ERPLWKDLHD VKKWVFYNGM EKNEQISPEA
     HPNLKIFRSE SDDAERRKHW KYWEVAVERS KGWLKDIEGE HEQVLENFQ
//