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Reviewed, UniProtKB/Swiss-Prot P47244 (PGM1_PARTE)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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Names and origin

Protein namesRecommended name:
    Phosphoglucomutase-1
      Short name=PGM 1
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase 1
    Parafusin
      Short name=Pf
    pp63
Gene names
Name: pp63-1
ORF Names: GSPATT00032405001
OrganismParamecium tetraurelia
Taxonomic identifier5888 [NCBI]
Taxonomic lineageEukaryota › Alveolata › Ciliophora › Intramacronucleata › Oligohymenophorea › Peniculida › Parameciidae › Paramecium

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Protein attributes

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

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General annotation (Comments)

Function

May be involved in membrane fusion in exocytosis.

Catalytic activity

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate. Ref.3

Cofactor

Binds 1 magnesium ion per subunit.

Subcellular location

Cytoplasm.

Post-translational modification

Phosphorylated via a calcium-dependent protein kinase. Very rapidly (within 80 ms) dephosphorylated during triggered trichocyst exocytosis.

O-glycosylated with a short chain of mannose residues.

Sequence similarities

Belongs to the phosphohexose mutase family.

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Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMGlycoprotein
Phosphoprotein
   Technical term3D-structure
Direct protein sequencing
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 572572Phosphoglucomutase-1
PRO_0000147813

Sites

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

Experimental info

Sequence conflict1 – 66MQQVIP → MVLFLLPLRLGHNLWRIE in AAB05649. Ref.1
Sequence conflict1 – 66MQQVIP → MVLFLLPLRLGHNLWRIE in AAX93766. Ref.3

Secondary structure

1 ............................................................................................................. 572
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P47244-1 [UniParc].

Last modified October 23, 2007. Version 4.
Checksum: AB0C31BEF01A930A

FASTA57263,806
        10         20         30         40         50         60 
MQQVIPAPRV QVTQPYAGQK PGTSGLRKKV SEATQPNYLE 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 QLMQKLFDFD LLKGLFSNKD FSFRFDGMHG 

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

       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 EQFEQQQIQH 

       550        560        570 
ETATALANII KLGLEISDIA QFTGRNEPTV IT

« Hide

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References

« Hide 'large scale' references
[1]"Cloning and sequencing of parafusin, a calcium-dependent exocytosis-related phosphoglycoprotein."
Subramanian S.V., Wyroba E., Andersen A.P., Satir B.H.
Proc. Natl. Acad. Sci. U.S.A. 91:9832-9836(1994) [PubMed: 7937900] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: Stock 51.
[2]Satir B.H.
Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 57-58.
[3]"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], PARTIAL PROTEIN SEQUENCE, CATALYTIC ACTIVITY.
Strain: Stock 51.
[4]Satir B.H.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Stock 51.
[5]"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.
[6]"Carbohydrate cycling in signal transduction: parafusin, a phosphoglycoprotein and possible Ca(2+)-dependent transducer molecule in exocytosis in Paramecium."
Subramanian S.V., Satir B.H.
Proc. Natl. Acad. Sci. U.S.A. 89:11297-11301(1992) [PubMed: 1333606] [Abstract]
Cited for: CHARACTERIZATION.
[7]"Crystal structure analysis of the exocytosis-sensitive phosphoprotein, pp63/parafusin (phosphoglucomutase), from Paramecium reveals significant conformational variability."
Mueller S., Diederichs K., Breed J., Kissmehl R., Hauser K., Plattner H., Welte W.
J. Mol. Biol. 315:141-153(2002) [PubMed: 11779235] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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Cross-references

Sequence databases

L12471 mRNA. Translation: AAB05649.2.
Y09969 mRNA. Translation: CAA71088.1.
AY970820 Genomic DNA. Translation: AAX93766.1.
CT868018 Genomic DNA. Translation: CAK62173.1.
RefSeqXP_001429571.1.
UniGenePte.18051

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1KFIX-ray2.40A/B1-572[»]
1KFQX-ray2.40A/B1-572[»]
SMRP47244. Positions 17-584.
ModBaseSearch...

Genome annotation databases

GeneID5015355.
KEGGptm:GSPATT00032405001.

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. 3 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...

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Entry information

Entry namePGM1_PARTE
AccessionPrimary (citable) accession number: P47244
Secondary accession number(s): O02605, Q52S71
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: October 23, 2007
Last modified: June 16, 2009
This is version 70 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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