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Phosphoglucomutase 2 (PGM 2) (EC 5.4.2.2) (D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase) (Glucose phosphomutase 2)

 PGM2_YEAST              Reviewed;         569 AA.
P37012; D6VZS7;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
22-NOV-2017, entry version 161.
RecName: Full=Phosphoglucomutase 2 {ECO:0000303|PubMed:5784209};
Short=PGM 2 {ECO:0000303|PubMed:5784209};
EC=5.4.2.2 {ECO:0000269|PubMed:1100398, ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:4992300};
AltName: Full=D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase {ECO:0000303|PubMed:14264884};
AltName: Full=Glucose phosphomutase 2;
Name=PGM2 {ECO:0000303|PubMed:5784209};
Synonyms=GA-5 {ECO:0000303|PubMed:13887540},
GAL5 {ECO:0000303|PubMed:2138705};
OrderedLocusNames=YMR105C {ECO:0000312|SGD:S000004711};
ORFNames=YM9718.04C;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8119301; DOI=10.1111/j.1432-1033.1994.tb18601.x;
Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.;
"A family of hexosephosphate mutases in Saccharomyces cerevisiae.";
Eur. J. Biochem. 220:83-96(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Fu L., Bounelis P., Dey N., Browne B.L., Marchase R.B., Bedwell D.M.;
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169872;
Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S.,
Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A.,
Rice P., Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome
XIII.";
Nature 387:90-93(1997).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=17322287; DOI=10.1101/gr.6037607;
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A.,
Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F.,
Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G.,
Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-
encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[6]
PROTEIN SEQUENCE OF 15-32 AND 265-275, SUBCELLULAR LOCATION, AND
GLYCOSYLATION.
PubMed=8385141;
Marchase R.B., Bounelis P., Brumley L.M., Dey N., Browne B., Auger D.,
Fritz T.A., Kulesza P., Bedwell D.M.;
"Phosphoglucomutase in Saccharomyces cerevisiae is a cytoplasmic
glycoprotein and the acceptor for a Glc-phosphotransferase.";
J. Biol. Chem. 268:8341-8349(1993).
[7]
DISRUPTION PHENOTYPE.
PubMed=13887540; DOI=10.1016/0006-3002(61)90924-6;
Douglas H.C.;
"A mutation in Saccharomyces that affects phosphoglucomutase activity
and galactose utilization.";
Biochim. Biophys. Acta 52:209-211(1961).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
STRAIN=8050B;
PubMed=14264884; DOI=10.1016/0926-6569(64)90011-2;
Tsoi A., Douglas H.C.;
"The effect of mutation of two forms of phosphoglucomutase in
Saccharomyces.";
Biochim. Biophys. Acta 92:513-520(1964).
[9]
FUNCTION.
PubMed=5231755; DOI=10.1073/pnas.57.5.1482;
Joshi J.G., Hooper J., Kuwaki T., Sakurada T., Swanson J.R.,
Handler P.;
"Phosphoglucomutase. V. Multiple forms of phosphoglucomutase.";
Proc. Natl. Acad. Sci. U.S.A. 57:1482-1489(1967).
[10]
FUNCTION.
PubMed=5784209;
Bevan P., Douglas H.C.;
"Genetic control of phosphoglucomutase variants in Saccharomyces
cerevisiae.";
J. Bacteriol. 98:532-535(1969).
[11]
CATALYTIC ACTIVITY.
PubMed=4992300;
Hirose M., Sugimoto E., Sasaki R., Chiaa H.;
"Crystallization and reaction mechanism of yeast phosphoglucomutase.";
J. Biochem. 68:449-457(1970).
[12]
COFACTOR.
PubMed=4628805; DOI=10.1016/0005-2744(72)90116-7;
Hirose M., Sugimoto E., Chiba H.;
"Studies on crystalline yeast phosphoglucomutase: the presence of
intrinsic zinc.";
Biochim. Biophys. Acta 289:137-146(1972).
[13]
CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
SUBUNIT.
PubMed=1100398; DOI=10.1111/j.1432-1033.1975.tb02282.x;
Daugherty J.P., Kraemer W.F., Joshi J.G.;
"Purification and properties of phosphoglucomutase from Fleischmann's
yeast.";
Eur. J. Biochem. 57:115-126(1975).
[14]
INDUCTION.
PubMed=2138705; DOI=10.1128/MCB.10.4.1415;
Oh D., Hopper J.E.;
"Transcription of a yeast phosphoglucomutase isozyme gene is galactose
inducible and glucose repressible.";
Mol. Cell. Biol. 10:1415-1422(1990).
[15]
GLYCOSYLATION.
PubMed=7929458;
Dey N.B., Bounelis P., Fritz T.A., Bedwell D.M., Marchase R.B.;
"The glycosylation of phosphoglucomutase is modulated by carbon source
and heat shock in Saccharomyces cerevisiae.";
J. Biol. Chem. 269:27143-27148(1994).
[16]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111; THR-117 AND
SER-119, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[20]
FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=23103740; DOI=10.1016/j.febslet.2012.09.042;
Walther T., Baylac A., Alkim C., Vax A., Cordier H., Francois J.M.;
"The PGM3 gene encodes the major phosphoribomutase in the yeast
Saccharomyces cerevisiae.";
FEBS Lett. 586:4114-4118(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
-!- FUNCTION: Major phosphoglucomutase isozyme that catalyzes the
reversible interconversion of glucose 1-phosphate and glucose 6-
phosphate (PubMed:5784209). Constitutes about 80-90% of the
phosphoglucomutase activity in the cell (PubMed:14264884,
PubMed:5231755). Key enzyme in hexose metabolism. The forward
reaction is an essential step in the energy metabolism of
galactose since the product of the galactose pathway enzymes in
yeast is glucose 1-phosphate. The reverse reaction is an essential
step for biosynthesis when carbon sources other than galactose are
the energy source because glucose 1-phosphate is the starting
point for the synthesis of UDP-glucose, which acts as a precursor
for the synthesis of oligosaccharides and trehalose
(PubMed:14264884). {ECO:0000269|PubMed:14264884,
ECO:0000269|PubMed:5231755}.
-!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
6-phosphate. {ECO:0000269|PubMed:1100398,
ECO:0000269|PubMed:23103740, ECO:0000269|PubMed:4992300}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:1100398,
ECO:0000269|PubMed:4628805};
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000269|PubMed:1100398,
ECO:0000269|PubMed:4628805};
Note=Binds 1 magnesium ion per subunit. Can also use Zn(2+) as
cofactor. {ECO:0000269|PubMed:1100398,
ECO:0000269|PubMed:4628805};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.24 uM for alpha-D-glucose 1,6-diphosphate
{ECO:0000269|PubMed:1100398};
KM=23.4 uM for alpha-D-glucose 1-phosphate
{ECO:0000269|PubMed:1100398};
KM=26 uM for alpha-D-glucose 1-phosphate
{ECO:0000269|PubMed:23103740};
KM=530 uM for D-ribose 1-phosphate
{ECO:0000269|PubMed:23103740};
Vmax=33.7 umol/min/mg enzyme for alpha-D-glucose 1-phosphate
{ECO:0000269|PubMed:23103740};
Vmax=0.32 umol/min/mg enzyme for D-ribose 1-phosphate
{ECO:0000269|PubMed:23103740};
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:1100398}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8385141}.
-!- INDUCTION: Induced in response to galactose and severely repressed
in response to glucose. {ECO:0000269|PubMed:2138705}.
-!- PTM: O-glycosylated with mannose residues (By similarity).
Substrate of UDP-glucose--glycoprotein glucose phosphotransferase,
linking glucose in a phosphodiester linkage to O-linked mannose
(PubMed:8385141, PubMed:7929458). {ECO:0000250|UniProtKB:P47244,
ECO:0000269|PubMed:7929458, ECO:0000269|PubMed:8385141}.
-!- DISRUPTION PHENOTYPE: Blocks galactose utilization, but does not
impair growth on glucose. {ECO:0000269|PubMed:14264884}.
-!- MISCELLANEOUS: Present with 3790 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the phosphohexose mutase family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X74823; CAA52820.1; -; Genomic_DNA.
EMBL; U09499; AAA91282.1; -; Genomic_DNA.
EMBL; Z49702; CAA89741.1; -; Genomic_DNA.
EMBL; AY723853; AAU09770.1; -; Genomic_DNA.
EMBL; BK006946; DAA10001.1; -; Genomic_DNA.
PIR; S41200; S41200.
RefSeq; NP_013823.1; NM_001182605.1.
ProteinModelPortal; P37012; -.
SMR; P37012; -.
BioGrid; 35280; 116.
DIP; DIP-6499N; -.
IntAct; P37012; 28.
MINT; MINT-705119; -.
STRING; 4932.YMR105C; -.
iPTMnet; P37012; -.
MaxQB; P37012; -.
PRIDE; P37012; -.
EnsemblFungi; YMR105C; YMR105C; YMR105C.
GeneID; 855131; -.
KEGG; sce:YMR105C; -.
EuPathDB; FungiDB:YMR105C; -.
SGD; S000004711; PGM2.
GeneTree; ENSGT00390000011831; -.
HOGENOM; HOG000009550; -.
InParanoid; P37012; -.
KO; K01835; -.
OMA; DIYKIYA; -.
OrthoDB; EOG092C1C93; -.
BioCyc; MetaCyc:YMR105C-MONOMER; -.
BioCyc; YEAST:YMR105C-MONOMER; -.
Reactome; R-SCE-3322077; Glycogen synthesis.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-70221; Glycogen breakdown (glycogenolysis).
Reactome; R-SCE-70370; Galactose catabolism.
SABIO-RK; P37012; -.
PRO; PR:P37012; -.
Proteomes; UP000002311; Chromosome XIII.
GO; GO:0005737; C:cytoplasm; IDA:SGD.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
GO; GO:0004614; F:phosphoglucomutase activity; IMP:SGD.
GO; GO:0006874; P:cellular calcium ion homeostasis; IMP:SGD.
GO; GO:0030003; P:cellular cation homeostasis; IMP:SGD.
GO; GO:0019388; P:galactose catabolic process; IMP:SGD.
GO; GO:0019255; P:glucose 1-phosphate metabolic process; IMP:SGD.
GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISS:SGD.
GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
GO; GO:0005978; P:glycogen biosynthetic process; IGI:SGD.
GO; GO:0005992; P:trehalose biosynthetic process; IGI:SGD.
GO; GO:0006011; P:UDP-glucose metabolic process; IGI:SGD.
Gene3D; 3.30.310.50; -; 1.
InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
InterPro; IPR005843; A-D-PHexomutase_C.
InterPro; IPR036900; A-D-PHexomutase_C_sf.
InterPro; IPR016066; A-D-PHexomutase_CS.
InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
Pfam; PF02878; PGM_PMM_I; 1.
Pfam; PF02879; PGM_PMM_II; 1.
Pfam; PF02880; PGM_PMM_III; 1.
Pfam; PF00408; PGM_PMM_IV; 1.
PRINTS; PR00509; PGMPMM.
SUPFAM; SSF53738; SSF53738; 3.
SUPFAM; SSF55957; SSF55957; 1.
PROSITE; PS00710; PGM_PMM; 1.
1: Evidence at protein level;
Acetylation; Carbohydrate metabolism; Complete proteome; Cytoplasm;
Direct protein sequencing; Glucose metabolism; Glycoprotein;
Isomerase; Magnesium; Metal-binding; Phosphoprotein;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 569 Phosphoglucomutase 2.
/FTId=PRO_0000147797.
REGION 119 120 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
REGION 294 295 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
REGION 378 380 Substrate binding.
{ECO:0000250|UniProtKB:P00949}.
ACT_SITE 119 119 Phosphoserine intermediate.
{ECO:0000250|UniProtKB:P00949}.
METAL 119 119 Magnesium; via phosphate group.
{ECO:0000250|UniProtKB:P00949}.
METAL 290 290 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
METAL 292 292 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
METAL 294 294 Magnesium.
{ECO:0000250|UniProtKB:P00949}.
BINDING 20 20 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 24 24 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 132 132 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 359 359 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 391 391 Substrate.
{ECO:0000250|UniProtKB:P00949}.
BINDING 522 522 Substrate.
{ECO:0000250|UniProtKB:P00949}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 111 111 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 117 117 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 119 119 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
CONFLICT 27 27 T -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 32 32 D -> G (in Ref. 6; AA sequence).
{ECO:0000305}.
CONFLICT 272 272 S -> A (in Ref. 6; AA sequence).
{ECO:0000305}.
SEQUENCE 569 AA; 63089 MW; 45B78AFF8197645E CRC64;
MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE GSKGATLVVG
GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS HIMRTYEEKC TGGIILTASH
NPGGPENDMG IKYNLSNGGP APESVTNAIW EISKKLTSYK IIKDFPELDL GTIGKNKKYG
PLLVDIIDIT KDYVNFLKEI FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD
EFGLPADEVL QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG
YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH GLNCYEVPTG
WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW LNILAIYNKH HPENEASIKT
IQNEFWAKYG RTFFTRYDFE KVETEKANKI VDQLRAYVTK SGVVNSAFPA DESLKVTDCG
DFSYTDLDGS VSDHQGLYVK LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE
EYLKPIINSV IKFLNFKQVL GTEEPTVRT


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