GLPK_YEAST
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 03-AUG-2022, entry version 181.
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=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
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 -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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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; 52.
DR DIP; DIP-6761N; -.
DR IntAct; P32190; 2.
DR MINT; P32190; -.
DR STRING; 4932.YHL032C; -.
DR iPTMnet; P32190; -.
DR MaxQB; P32190; -.
DR PaxDb; P32190; -.
DR PRIDE; P32190; -.
DR EnsemblFungi; YHL032C_mRNA; YHL032C; YHL032C.
DR GeneID; 856353; -.
DR KEGG; sce:YHL032C; -.
DR SGD; S000001024; GUT1.
DR VEuPathDB; FungiDB:YHL032C; -.
DR eggNOG; KOG2517; Eukaryota.
DR GeneTree; ENSGT01000000214434; -.
DR HOGENOM; CLU_009281_2_2_1; -.
DR InParanoid; P32190; -.
DR OMA; PESGWHE; -.
DR BioCyc; YEAST:YHL032C-MON; -.
DR Reactome; R-SCE-75109; Triglyceride biosynthesis.
DR UniPathway; UPA00618; UER00672.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004370; F:glycerol kinase activity; IMP:SGD.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IBA:GO_Central.
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:0016310; P:phosphorylation; IBA:GO_Central.
DR GO; GO:0006641; P:triglyceride metabolic process; IBA:GO_Central.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
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
