DOG1_YEAST
ID DOG1_YEAST Reviewed; 246 AA.
AC P38774; D3DKZ2; P38923;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=2-deoxyglucose-6-phosphate phosphatase 1 {ECO:0000303|PubMed:8553694};
DE Short=2-DOG-6-P 1 {ECO:0000303|PubMed:8553694};
DE Short=2-deoxyglucose-6-phosphatase 1 {ECO:0000303|PubMed:8553694};
DE EC=3.1.3.68 {ECO:0000269|PubMed:8553694};
GN Name=DOG1 {ECO:0000303|PubMed:8553694}; OrderedLocusNames=YHR044C;
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].
RX PubMed=7754708; DOI=10.1002/yea.320100907;
RA Sanz P., Randez-Gil F., Prieto J.A.;
RT "Molecular characterization of a gene that confers 2-deoxyglucose
RT resistance in yeast.";
RL Yeast 10:1195-1202(1994).
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).
RN [4]
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).
RN [5]
RP N, FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=8553694; DOI=10.1002/yea.320111303;
RA Randez-Gil F., Blasco A., Prieto J.A., Sanz P.;
RT "DOGR1 and DOGR2: two genes from Saccharomyces cerevisiae that confer 2-
RT deoxyglucose resistance when overexpressed.";
RL Yeast 11:1233-1240(1995).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
CC -!- FUNCTION: Phosphatase that is active on 2-deoxy-D-glucose 6-phosphate
CC (2-DOG-6P), as well as on fructose-1-P. {ECO:0000269|PubMed:8553694}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-deoxy-D-glucose 6-phosphate + H2O = 2-deoxy-D-glucose +
CC phosphate; Xref=Rhea:RHEA:22236, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:84755, ChEBI:CHEBI:84760; EC=3.1.3.68;
CC Evidence={ECO:0000269|PubMed:8553694};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q94K71};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=17 mM for 2-deoxy-D-glucose 6-phosphate
CC {ECO:0000269|PubMed:8553694};
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:8553694};
CC Temperature dependence:
CC Optimum temperature is 30 degrees Celsius.
CC {ECO:0000269|PubMed:8553694};
CC -!- MISCELLANEOUS: Present with 752 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. DOG/GPP
CC family. {ECO:0000305}.
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DR EMBL; U03107; AAC48923.1; -; Genomic_DNA.
DR EMBL; U00062; AAB68917.1; -; Genomic_DNA.
DR EMBL; AY558516; AAS56842.1; -; Genomic_DNA.
DR EMBL; BK006934; DAA06736.1; -; Genomic_DNA.
DR PIR; S46604; S46604.
DR RefSeq; NP_011910.1; NM_001179174.1.
DR AlphaFoldDB; P38774; -.
DR SMR; P38774; -.
DR BioGRID; 36476; 64.
DR DIP; DIP-6336N; -.
DR IntAct; P38774; 5.
DR STRING; 4932.YHR044C; -.
DR MaxQB; P38774; -.
DR PaxDb; P38774; -.
DR PRIDE; P38774; -.
DR EnsemblFungi; YHR044C_mRNA; YHR044C; YHR044C.
DR GeneID; 856440; -.
DR KEGG; sce:YHR044C; -.
DR SGD; S000001086; DOG1.
DR VEuPathDB; FungiDB:YHR044C; -.
DR eggNOG; KOG2914; Eukaryota.
DR GeneTree; ENSGT00940000176801; -.
DR HOGENOM; CLU_045011_13_4_1; -.
DR InParanoid; P38774; -.
DR OMA; DPQCYIL; -.
DR BioCyc; YEAST:YHR044C-MON; -.
DR BRENDA; 3.1.3.68; 984.
DR PRO; PR:P38774; -.
DR Proteomes; UP000002311; Chromosome VIII.
DR RNAct; P38774; protein.
DR GO; GO:0003850; F:2-deoxyglucose-6-phosphatase activity; IDA:SGD.
DR GO; GO:0008801; F:beta-phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050308; F:sugar-phosphatase activity; IBA:GO_Central.
DR GO; GO:0006006; P:glucose metabolic process; IDA:SGD.
DR Gene3D; 1.10.150.240; -; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006439; HAD-SF_hydro_IA.
DR InterPro; IPR041492; HAD_2.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR023198; PGP-like_dom2.
DR Pfam; PF13419; HAD_2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT CHAIN 1..246
FT /note="2-deoxyglucose-6-phosphate phosphatase 1"
FT /id="PRO_0000079974"
FT ACT_SITE 83
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT BINDING 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
FT BINDING 83
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 146..149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P95649"
FT BINDING 183
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:Q94K71"
SQ SEQUENCE 246 AA; 27100 MW; 0682527802373EAD CRC64;
MAEFSADLCL FDLDGTIVST TVAAEKAWTK LCYEYGVDPS ELFKHSHGAR TQEVLRRFFP
KLDDTDNKGV LALEKDIAHS YLDTVSLIPG AENLLLSLDV DTETQKKLPE RKWAIVTSGS
PYLAFSWFET ILKNVGKPKV FITGFDVKNG KPDPEGYSRA RDLLRQDLQL TGKQDLKYVV
FEDAPVGIKA GKAMGAITVG ITSSYDKSVL FDAGADYVVC DLTQVSVVKN NENGIVIQVN
NPLTRA
