YMY9_YEAST
ID YMY9_YEAST Reviewed; 297 AA.
AC Q03161; D6VZS2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Glucose-6-phosphate 1-epimerase {ECO:0000305};
DE EC=5.1.3.15 {ECO:0000269|PubMed:16857670};
DE AltName: Full=D-hexose-6-phosphate mutarotase {ECO:0000303|PubMed:16857670};
GN OrderedLocusNames=YMR099C; ORFNames=YM6543.06C;
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=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(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 IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=14690591; DOI=10.1016/s1097-2765(03)00476-3;
RA Hazbun T.R., Malmstroem L., Anderson S., Graczyk B.J., Fox B., Riffle M.,
RA Sundin B.A., Aranda J.D., McDonald W.H., Chiu C.-H., Snydsman B.E.,
RA Bradley P., Muller E.G.D., Fields S., Baker D., Yates J.R. III, Davis T.N.;
RT "Assigning function to yeast proteins by integration of technologies.";
RL Mol. Cell 12:1353-1365(2003).
RN [4]
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).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) ALONE AND IN COMPLEX WITH GLC6P AND
RP GAL6P, FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
RX PubMed=16857670; DOI=10.1074/jbc.m604443200;
RA Graille M., Baltaze J.P., Leulliot N., Liger D., Quevillon-Cheruel S.,
RA van Tilbeurgh H.;
RT "Structure-based functional annotation: yeast ymr099c codes for a D-hexose-
RT 6-phosphate mutarotase.";
RL J. Biol. Chem. 281:30175-30185(2006).
CC -!- FUNCTION: Catalyzes the interconversion between the alpha and beta
CC anomers from at least three hexose 6-phosphate sugars (Glc6P, Gal6P,
CC and Man6P). {ECO:0000269|PubMed:16857670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:16249, ChEBI:CHEBI:58225, ChEBI:CHEBI:58247;
CC EC=5.1.3.15; Evidence={ECO:0000269|PubMed:16857670};
CC -!- MISCELLANEOUS: Present with 8580 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the glucose-6-phosphate 1-epimerase family.
CC {ECO:0000305}.
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DR EMBL; Z49807; CAA89900.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09996.1; -; Genomic_DNA.
DR PIR; S55085; S55085.
DR RefSeq; NP_013817.1; NM_001182599.1.
DR PDB; 2CIQ; X-ray; 1.70 A; A=1-297.
DR PDB; 2CIR; X-ray; 1.60 A; A=1-297.
DR PDB; 2CIS; X-ray; 1.62 A; A=1-297.
DR PDBsum; 2CIQ; -.
DR PDBsum; 2CIR; -.
DR PDBsum; 2CIS; -.
DR AlphaFoldDB; Q03161; -.
DR SMR; Q03161; -.
DR BioGRID; 35275; 87.
DR IntAct; Q03161; 12.
DR MINT; Q03161; -.
DR STRING; 4932.YMR099C; -.
DR iPTMnet; Q03161; -.
DR MaxQB; Q03161; -.
DR PaxDb; Q03161; -.
DR PRIDE; Q03161; -.
DR EnsemblFungi; YMR099C_mRNA; YMR099C; YMR099C.
DR GeneID; 855125; -.
DR KEGG; sce:YMR099C; -.
DR SGD; S000004705; YMR099C.
DR VEuPathDB; FungiDB:YMR099C; -.
DR eggNOG; KOG1594; Eukaryota.
DR GeneTree; ENSGT00390000015166; -.
DR HOGENOM; CLU_048345_2_0_1; -.
DR InParanoid; Q03161; -.
DR OMA; TQALHSY; -.
DR BioCyc; MetaCyc:G3O-32799-MON; -.
DR BioCyc; YEAST:G3O-32799-MON; -.
DR BRENDA; 5.3.3.3; 1455.
DR EvolutionaryTrace; Q03161; -.
DR PRO; PR:Q03161; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03161; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005634; C:nucleus; HDA:SGD.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0047938; F:glucose-6-phosphate 1-epimerase activity; IDA:SGD.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IC:SGD.
DR CDD; cd09020; D-hex-6-P-epi_like; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008183; Aldose_1/G6P_1-epimerase.
DR InterPro; IPR025532; G6P_1-epimerase.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR Pfam; PF01263; Aldose_epim; 1.
DR PIRSF; PIRSF016020; PHexose_mutarotase; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isomerase; Phosphoprotein; Reference proteome.
FT CHAIN 1..297
FT /note="Glucose-6-phosphate 1-epimerase"
FT /id="PRO_0000213035"
FT ACT_SITE 159
FT /evidence="ECO:0000269|PubMed:16857670"
FT ACT_SITE 264
FT /evidence="ECO:0000269|PubMed:16857670"
FT BINDING 57
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16857670"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16857670"
FT BINDING 86
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16857670"
FT BINDING 203
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:16857670"
FT MOD_RES 88
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 7..14
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 17..25
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 30..36
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 51..54
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 62..65
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:2CIR"
FT TURN 98..101
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 114..119
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 125..132
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 134..144
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 152..158
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 167..169
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 179..182
FT /evidence="ECO:0007829|PDB:2CIR"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 187..190
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 202..206
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:2CIR"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 260..274
FT /evidence="ECO:0007829|PDB:2CIR"
FT STRAND 279..287
FT /evidence="ECO:0007829|PDB:2CIR"
SQ SEQUENCE 297 AA; 33956 MW; 122BDC460BB9A32B CRC64;
MPIKETDKEV VLTHPADETT SVHILKYGAT VYSWKLKSEE QLWLSTAAKL DGSKPVRGGI
PLVFPVFGKN STDEHLSKLP QHGLARNSTW EFLGQTKENP PTVQFGLKPE IANPELTKLW
PMDYLLILTV ELGSDYLKTA IEVENTSSSK ELKFNWLFHT YFRIEDIEGT MVSNLAGMKL
YDQLLKESYV DKHPVVTFNQ ETDVIYQNVS AERAIQIVDK GVQIHTLKRY NLPDTVVWNP
WIEKSQGMAD FEPKTGYQQM ICIEPGHVHD FISLAPGKKW NAYQLLCKEE LKYQAIQ
