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Reviewed, UniProtKB/Swiss-Prot O02606 (PGM2_PARTE)

Last modified June 16, 2009. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucomutase-2
      Short name=PGM 2
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase 2
    Parafusin-2
      Short name=Pf-2
Gene names
Name: pp63-2
ORF Names: GSPATT00000627001
OrganismParamecium tetraurelia
Taxonomic identifier5888 [NCBI]
Taxonomic lineageEukaryotaAlveolataCiliophoraIntramacronucleataOligohymenophoreaPeniculidaParameciidaeParamecium

Protein attributes

Sequence length572 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript level.

General annotation (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.

Post-translational modification

Phosphorylated via a calcium-dependent protein kinase By similarity.

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglucomutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Phosphoglucomutase-2
PRO_0000307834

Sites

Active site1261Phosphoserine intermediate By similarity
Metal binding1261Magnesium; via phosphate group By similarity
Metal binding3081Magnesium By similarity
Metal binding3101Magnesium By similarity
Metal binding3121Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
O02606-1 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: A2489D239595D5B8

FASTA57263,718
        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 

« Hide

References

« Hide 'large scale' references
[1]"Identification of isoforms of the exocytosis-sensitive phosphoprotein PP63/parafusin in Paramecium tetraurelia and demonstration of phosphoglucomutase activity."
Hauser K., Kissmehl R., Linder J., Schultz J.E., Lottspeich F., Plattner H.
Biochem. J. 323:289-296(1997) [PubMed: 9173895] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Stock 51.
[2]"Global trends of whole-genome duplications revealed by the ciliate Paramecium tetraurelia."
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. expand/collapse author list , 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.
Nature 444:171-178(2006) [PubMed: 17086204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Stock d4-2.

Cross-references

Sequence databases

Y09970 mRNA. Translation: CAA71089.1.
CT868096 Genomic DNA. Translation: CAK70916.1.
RefSeqXP_001438313.1.
UniGenePte.8242

3D structure databases

HSSPHSSP built from PDB template 1KFQ based on UniProtKB P47244.
SMRO02606. Positions 3-572.
ModBaseSearch...

Genome annotation databases

GeneID5024098.
KEGGptm:GSPATT00000627001.

Enzyme and pathway databases

BRENDA5.4.2.2. 21526.

Family and domain databases

InterProIPR005844. 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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
PfamPF02878. PGM_PMM_I. 1 hit.
PF02879. PGM_PMM_II. 1 hit.
PF02880. PGM_PMM_III. 1 hit.
PF00408. PGM_PMM_IV. 1 hit.
[Graphical view]
PRINTSPR00509. PGMPMM.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGM2_PARTE
AccessionPrimary (citable) accession number: O02606
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: July 1, 1997
Last modified: June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents