ID PGM_SCHPO Reviewed; 554 AA.
AC O74374;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 27-MAR-2024, entry version 152.
DE RecName: Full=Phosphoglucomutase {ECO:0000250|UniProtKB:P37012};
DE Short=PGM {ECO:0000250|UniProtKB:P37012};
DE EC=5.4.2.2 {ECO:0000250|UniProtKB:P37012};
DE AltName: Full=Glucose phosphomutase;
GN ORFNames=SPBC32F12.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111 AND SER-113, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalyzes the reversible interconversion of glucose 1-
CC phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The
CC reverse reaction is an essential step for biosynthesis because glucose
CC 1-phosphate is the starting point for the synthesis of UDP-glucose,
CC which acts as a precursor for the synthesis of oligosaccharides and
CC trehalose. {ECO:0000250|UniProtKB:P37012}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate;
CC Xref=Rhea:RHEA:23536, ChEBI:CHEBI:58225, ChEBI:CHEBI:58601;
CC EC=5.4.2.2; Evidence={ECO:0000250|UniProtKB:P37012};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P37012};
CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:P37012};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. {ECO:0000305}.
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DR EMBL; CU329671; CAA19371.1; -; Genomic_DNA.
DR PIR; T40234; T40234.
DR RefSeq; NP_596153.1; NM_001022072.2.
DR AlphaFoldDB; O74374; -.
DR SMR; O74374; -.
DR BioGRID; 276785; 2.
DR STRING; 284812.O74374; -.
DR iPTMnet; O74374; -.
DR MaxQB; O74374; -.
DR PaxDb; 4896-SPBC32F12-10-1; -.
DR EnsemblFungi; SPBC32F12.10.1; SPBC32F12.10.1:pep; SPBC32F12.10.
DR GeneID; 2540254; -.
DR KEGG; spo:SPBC32F12.10; -.
DR PomBase; SPBC32F12.10; -.
DR VEuPathDB; FungiDB:SPBC32F12.10; -.
DR eggNOG; KOG0625; Eukaryota.
DR HOGENOM; CLU_009330_0_1_1; -.
DR InParanoid; O74374; -.
DR OMA; WIQDRAN; -.
DR PhylomeDB; O74374; -.
DR Reactome; R-SPO-3322077; Glycogen synthesis.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-70221; Glycogen breakdown (glycogenolysis).
DR Reactome; R-SPO-70370; Galactose catabolism.
DR PRO; PR:O74374; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004614; F:phosphoglucomutase activity; IBA:GO_Central.
DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
DR GO; GO:0019388; P:galactose catabolic process; ISO:PomBase.
DR GO; GO:0019255; P:glucose 1-phosphate metabolic process; ISO:PomBase.
DR GO; GO:0051156; P:glucose 6-phosphate metabolic process; ISO:PomBase.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005978; P:glycogen biosynthetic process; ISO:PomBase.
DR GO; GO:0005992; P:trehalose biosynthetic process; ISO:PomBase.
DR GO; GO:0006011; P:UDP-glucose metabolic process; ISO:PomBase.
DR CDD; cd03085; PGM1; 1.
DR Gene3D; 3.40.120.10; Alpha-D-Glucose-1,6-Bisphosphate, subunit A, domain 3; 3.
DR Gene3D; 3.30.310.50; Alpha-D-phosphohexomutase, C-terminal domain; 1.
DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I.
DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II.
DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III.
DR InterPro; IPR036900; A-D-PHexomutase_C_sf.
DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF.
DR InterPro; IPR045244; PGM.
DR PANTHER; PTHR22573:SF2; PHOSPHOGLUCOMUTASE; 1.
DR PANTHER; PTHR22573; PHOSPHOHEXOMUTASE FAMILY MEMBER; 1.
DR Pfam; PF02878; PGM_PMM_I; 1.
DR Pfam; PF02879; PGM_PMM_II; 1.
DR Pfam; PF02880; PGM_PMM_III; 1.
DR PRINTS; PR00509; PGMPMM.
DR SUPFAM; SSF55957; Phosphoglucomutase, C-terminal domain; 1.
DR SUPFAM; SSF53738; Phosphoglucomutase, first 3 domains; 3.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Cytoplasm; Glucose metabolism; Isomerase;
KW Magnesium; Metal-binding; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..554
FT /note="Phosphoglucomutase"
FT /id="PRO_0000147795"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 554 AA; 60599 MW; 5B064562A22A1358 CRC64;
MIETIPTKPY EGQRPGTSGL RKKVTVFEQP NYVENFVQAT MDVVEPSAKG AHLVVGGDGR
YFNFHAIQVI AAIAAGNGVE KIIVGTNGYL STPAASHIIR KYKLTGGIIL TASHNAGGPK
NDFGIKYNLG NGGPAPESVT EKIYSITKTI SEYKMVKIPP LDLTTTGVRR YGPLTVEVID
PVKDYVQLMK EIFDFDLIRS FLSKNPDFTF VFDALHGITG PYGEALFCKE LGMPSSVCQN
CKPLPDFGGG HPDPNLTYAK SLVARVDRDN IVMGAASDGD GDRNMIYGAN AFVTPSDSVA
IIAHHAELIP YFRDGGVHGF ARSMPTSGAI DRVGKYKGKN VYEVPTGWKF FCNLFDAKRL
SICGEESFGT GSDHIREKDG VWGILCWLNI LAGLNAQNPK IKTLIDVKKD FYNIYGRTFY
SRYDYEELEN EAAGKVMDRM RAIADDKSKV GEAVLPGFVV SEAGDFEYHD PIDGSESKHQ
GLYIKFENGS RIVTRLSGTG SSGATLRLYM EKHESDSSKF DLDAQVALKP VVHAALEILA
LEELTGRKEP TVIT
//
