ID   PGM2_PARTE              Reviewed;         572 AA.
AC   O02606;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   16-JUN-2009, entry version 51.
DE   RecName: Full=Phosphoglucomutase-2;
DE            Short=PGM 2;
DE            EC=5.4.2.2;
DE   AltName: Full=Glucose phosphomutase 2;
DE   AltName: Full=Parafusin-2;
DE            Short=Pf-2;
GN   Name=pp63-2; ORFNames=GSPATT00000627001;
OS   Paramecium tetraurelia.
OC   Eukaryota; Alveolata; Ciliophora; Intramacronucleata;
OC   Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX   NCBI_TaxID=5888;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Stock 51;
RX   MEDLINE=97311229; PubMed=9173895;
RA   Hauser K., Kissmehl R., Linder J., Schultz J.E., Lottspeich F.,
RA   Plattner H.;
RT   "Identification of isoforms of the exocytosis-sensitive phosphoprotein
RT   PP63/parafusin in Paramecium tetraurelia and demonstration of
RT   phosphoglucomutase activity.";
RL   Biochem. J. 323:289-296(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Stock d4-2;
RX   PubMed=17086204; DOI=10.1038/nature05230;
RA   Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA   Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA   Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S.,
RA   Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R.,
RA   Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M.,
RA   Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M.,
RA   Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V.,
RA   Sperling L., Meyer E., Cohen J., Wincker P.;
RT   "Global trends of whole-genome duplications revealed by the ciliate
RT   Paramecium tetraurelia.";
RL   Nature 444:171-178(2006).
CC   -!- FUNCTION: May be involved in membrane fusion in exocytosis (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose
CC       6-phosphate.
CC   -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- PTM: Phosphorylated via a calcium-dependent protein kinase (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the phosphohexose mutase family.
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DR   EMBL; Y09970; CAA71089.1; -; mRNA.
DR   EMBL; CT868096; CAK70916.1; -; Genomic_DNA.
DR   RefSeq; XP_001438313.1; -.
DR   UniGene; Pte.8242; -.
DR   HSSP; P47244; 1KFQ.
DR   SMR; O02606; 3-572.
DR   GeneID; 5024098; -.
DR   KEGG; ptm:GSPATT00000627001; -.
DR   BRENDA; 5.4.2.2; 21526.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004614; F:phosphoglucomutase activity; IEA:EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR005843; A-D-PHexomutase_C.
DR   InterPro; IPR016066; A-D-PHexomutase_CS.
DR   InterPro; IPR005841; A-D-PHexomutase_N.
DR   Gene3D; G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 2.
DR   Pfam; PF02878; PGM_PMM_I; 1.
DR   Pfam; PF02879; PGM_PMM_II; 1.
DR   Pfam; PF02880; PGM_PMM_III; 1.
DR   Pfam; PF00408; PGM_PMM_IV; 1.
DR   PRINTS; PR00509; PGMPMM.
DR   PROSITE; PS00710; PGM_PMM; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isomerase; Magnesium; Metal-binding; Phosphoprotein.
FT   CHAIN         1    572       Phosphoglucomutase-2.
FT                                /FTId=PRO_0000307834.
FT   ACT_SITE    126    126       Phosphoserine intermediate (By
FT                                similarity).
FT   METAL       126    126       Magnesium; via phosphate group (By
FT                                similarity).
FT   METAL       308    308       Magnesium (By similarity).
FT   METAL       310    310       Magnesium (By similarity).
FT   METAL       312    312       Magnesium (By similarity).
SQ   SEQUENCE   572 AA;  63718 MW;  A2489D239595D5B8 CRC64;
     MQQVIPAPRV QVTQPYAGQK PGTSGLRKKV TEATQPHYLE NFVQSIFNTL RKDELKPKNV
     LFVGGDGRYF NRQAIFSIIR LAYANDISEV HVGQAGLMST PASSHYIRKV NEEVGNCIGG
     IILTASHNPG GKEHGDFGIK FNVRTGAPAP EDFTDQIYTH TTKIKEYLTV DYEFEKHINL
     DQIGVYKFEG TRLEKSHFEV KVVDTVQDYT SLMQKLFDFD LLKGLFSNKD FTFSFDGMHG
     VAGPYAKHIF GTLLGCSKES LLNCDPSEDF GGGHPDPNLT YAHDLVELLD IHKKKDVGAV
     PQFGAACDGD ADRNMILGRQ FFVTPSDSLA VIAANANLIF KNGLLGAARS MPTSGALDKV
     AAKNGIKLFE TPTGWKFFGN LMDAGLINLC GEESFGTGSN HIREKDGIWA VLAWLTILAH
     KNKNTDHFVT VEEIVTQYWQ QFGRNYYSRY DYEQVDSAGA NKMMEHLKTK FQYFEQLKQG
     NKADIYDYVD PVDQSVSKNQ GVRFVFGDGS RIIFRLSGTG SVGATIRIYF EQFEQQEIQH
     ETATALANII KLGLEISDIA QFTGRNEPTV IT
//