Skip Header

Contribute Send feedback
Read comments (?) or add your own

O74478 (PGM2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucomutase-2
Short name=PGM 2
EC=5.4.2.2
Alternative name(s):
Glucose phosphomutase 2
Gene names
ORF Names:SPCC1840.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme participates in both the breakdown and synthesis of glucose By similarity.

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Subunit structure

Monomer By similarity.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentCytoplasm
Nucleus
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processglucose 1-phosphate metabolic process

Inferred from sequence or structural similarity. Source: RefGenome

   Cellular componentcytosol

Inferred from direct assay. Source: GeneDB_Spombe

nucleus

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglucomutase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 587587Phosphoglucomutase-2
PRO_0000315630

Sites

Active site1491Phosphoserine intermediate By similarity
Metal binding1491Magnesium; via phosphate group By similarity
Metal binding3061Magnesium By similarity
Metal binding3081Magnesium By similarity
Metal binding3101Magnesium By similarity

Amino acid modifications

Modified residue1491Phosphoserine Ref.3

Sequences

Sequence LengthMass (Da)Tools
O74478 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 3A818C1C02CD5845

FASTA58765,494
        10         20         30         40         50         60 
MDPILQELVD EWFKLDQDET TRNEVSQLIK AEDYATLKQI MHPRIGFGTS GLRAEIGAGF 

        70         80         90        100        110        120 
ARMNCLTVIQ ASQGFAEYLL QTVPSAAKLG VVIGHDHRHK SNTFARLTAA VFLQKGFKTY 

       130        140        150        160        170        180 
FFDHLVHTPL VPFAVKTLGT AAGVMITASH NPAAYNGYKV YWGNGCAIIP PHDKGIAACI 

       190        200        210        220        230        240 
EKNLTPITWD KNLVENHKLA DRDFAVGLLK NYWSQLHEFH SENNFSLEMK SLKFVYTPIH 

       250        260        270        280        290        300 
GVGLPFVTSA LHLFGEQGDM ISVPLQDSPN PDFPTVKFPN PEEEGALDLA YEQADANGIS 

       310        320        330        340        350        360 
YVLATDPDAD RFAFAEKING AWRRFTGDEV GCILAYFIFQ EYKNVGKPID DFYVLSTTVS 

       370        380        390        400        410        420 
SAMVKSMAKV EGFHHVETLT GFKWLGNKAL ELEKQGKFIG LAYEEALGYM VGSIVRDKDG 

       430        440        450        460        470        480 
VNALITFLHL LKRLQLQNLS ITEVFEQMSK KYGYYTTQNS YFLSRDTPKL RALVDALRHY 

       490        500        510        520        530        540 
DTKSGYPATL GSKKITNVRD LTTGYDSSST DGKATLPVSK SSDNVTFELE NGEVIMTIRT 

       550        560        570        580 
SGTEPKLKFY ICARGHSLED SIKNATEVKQ AIKSEWFHPQ QNGLEEP

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[2]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]"Phosphoproteome analysis of fission yeast."
Wilson-Grady J.T., Villen J., Gygi S.P.
J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329672 Genomic DNA. Translation: CAA20128.1.
PIRT41173.
RefSeqNP_588504.1. NM_001023494.1.

3D structure databases

ProteinModelPortalO74478.
ModBaseSearch...

Protein-protein interaction databases

STRINGO74478.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPCC1840.05c.1; SPCC1840.05c.1:pep; SPCC1840.05c.
GeneID2538920.
KEGGspo:SPCC1840.05c.
NMPDRfig|4896.1.peg.842.

Organism-specific databases

GeneDB_SpombeSPCC1840.05c.

Phylogenomic databases

eggNOGfuNOG05584.
GeneTreeEFGT00050000004521.
HOGENOMHBG571743.
OMAIYKEFGY.
OrthoDBEOG4N605B.

Gene expression databases

ArrayExpressO74478.

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. Alpha-D-phosphohexomutase_SF.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK01835.
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.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGM2_SCHPO
AccessionPrimary (citable) accession number: O74478
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 1, 1998
Last modified: December 14, 2011
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents