NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Stock 51;
PubMed=9173895 [NCBI, ExPASy, EBI, Israel, Japan]
Hauser K., Kissmehl R., Linder J., Schultz J.E., Lottspeich F., Plattner H.;
"Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity.";
Biochem. J. 323:289-296(1997).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Stock d4-2;
DOI=10.1038/nature05230; PubMed=17086204 [NCBI, ExPASy, EBI, Israel, Japan]
Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M., Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A., Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R., Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F., Le Mouel A., Lepere G., Malinsky S., Nowacki M., Nowak J.K., Plattner H., Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M., Weissenbach J., Scarpelli C., Schaechter V., Sperling L., Meyer E., Cohen J., Wincker P.;
"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia.";
Nature 444:171-178(2006).

Comments

FUNCTION: May be involved in membrane fusion in exocytosis (By similarity).
CATALYTIC ACTIVITY: Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
PTM: Phosphorylated via a calcium-dependent protein kinase (By similarity).
SIMILARITY: Belongs to the phosphohexose mutase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

Y09970; CAA71089.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
CT868096; CAK70916.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

XP_001438313.1; -.

3D structure databases

HSSP

P47244; 1KFQ. [HSSP ENTRY / PDB]

SMR

O02606; 3-572.

ModBase

O02606.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from InterPro).
GO:0004614;	Molecular function: phosphoglucomutase activity (inferred from electronic annotation from EC).
GO:0005975;	Biological process: carbohydrate metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR005844; A-D-PHexomutase_a/b/a-I.
IPR016055; A-D-PHexomutase_a/b/a-I/II/III.
IPR005845; A-D-PHexomutase_a/b/a-II.
IPR005846; A-D-PHexomutase_a/b/a-III.
IPR005843; A-D-PHexomutase_C.
IPR016066; A-D-PHexomutase_CS.
IPR005841; A-D-PHexomutase_N.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.120.10; A-D-PHexomutase_a/b/a-I/II/III; 2.

Pfam

PF02878; PGM_PMM_I; 1.
PF02879; PGM_PMM_II; 1.
PF02880; PGM_PMM_III; 1.
PF00408; PGM_PMM_IV; 1.
Pfam graphical view of domain structure.

PRINTS

PR00509; PGMPMM.

PROSITE

PS00710; PGM_PMM; 1.

Genome annotation databases

GeneID

5024098; -.

KEGG

ptm:GSPATT00000627001; -.

Other

ProtoNet

O02606.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Cytoplasm; Isomerase; Magnesium; Metal-binding; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 572`	`572`	`Phosphoglucomutase-2.`	`PRO_0000307834`
`ACT_SITE`	`126 126`		`Phosphoserine intermediate (By similarity).`
`METAL`	`126 126`		`Magnesium; via phosphate group (By similarity).`
`METAL`	`308 308`		`Magnesium (By similarity).`
`METAL`	`310 310`		`Magnesium (By similarity).`
`METAL`	`312 312`		`Magnesium (By similarity).`

Sequence information

Length: 572 AA [This is the length of the unprocessed precursor]

Molecular weight: 63718 Da [This is the MW of the unprocessed precursor]

CRC64: A2489D239595D5B8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MQQVIPAPRV QVTQPYAGQK PGTSGLRKKV TEATQPHYLE NFVQSIFNTL RKDELKPKNV 

        70         80         90        100        110        120 
LFVGGDGRYF NRQAIFSIIR LAYANDISEV HVGQAGLMST PASSHYIRKV NEEVGNCIGG 

       130        140        150        160        170        180 
IILTASHNPG GKEHGDFGIK FNVRTGAPAP EDFTDQIYTH TTKIKEYLTV DYEFEKHINL 

       190        200        210        220        230        240 
DQIGVYKFEG TRLEKSHFEV KVVDTVQDYT SLMQKLFDFD LLKGLFSNKD FTFSFDGMHG 

       250        260        270        280        290        300 
VAGPYAKHIF GTLLGCSKES LLNCDPSEDF GGGHPDPNLT YAHDLVELLD IHKKKDVGAV 

       310        320        330        340        350        360 
PQFGAACDGD ADRNMILGRQ FFVTPSDSLA VIAANANLIF KNGLLGAARS MPTSGALDKV 

       370        380        390        400        410        420 
AAKNGIKLFE TPTGWKFFGN LMDAGLINLC GEESFGTGSN HIREKDGIWA VLAWLTILAH 

       430        440        450        460        470        480 
KNKNTDHFVT VEEIVTQYWQ QFGRNYYSRY DYEQVDSAGA NKMMEHLKTK FQYFEQLKQG 

       490        500        510        520        530        540 
NKADIYDYVD PVDQSVSKNQ GVRFVFGDGS RIIFRLSGTG SVGATIRIYF EQFEQQEIQH 

       550        560        570 
ETATALANII KLGLEISDIA QFTGRNEPTV IT

O02606 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools