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O74374 (PGM_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 85. Feed History...

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

Names and origin

Protein namesRecommended name:
Probable phosphoglucomutase
Short name=PGM
EC=5.4.2.2
Alternative name(s):
Glucose phosphomutase
Gene names
ORF Names:SPBC32F12.10
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length554 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.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the phosphohexose mutase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 554554Probable phosphoglucomutase
PRO_0000147795

Sites

Active site1131Phosphoserine intermediate By similarity
Metal binding1131Magnesium; via phosphate group By similarity
Metal binding2781Magnesium By similarity
Metal binding2801Magnesium By similarity
Metal binding2821Magnesium By similarity

Amino acid modifications

Modified residue1111Phosphothreonine Ref.2
Modified residue1131Phosphoserine Ref.2

Sequences

Sequence LengthMass (Da)Tools
O74374 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 5B064562A22A1358

FASTA55460,599
        10         20         30         40         50         60 
MIETIPTKPY EGQRPGTSGL RKKVTVFEQP NYVENFVQAT MDVVEPSAKG AHLVVGGDGR 

        70         80         90        100        110        120 
YFNFHAIQVI AAIAAGNGVE KIIVGTNGYL STPAASHIIR KYKLTGGIIL TASHNAGGPK 

       130        140        150        160        170        180 
NDFGIKYNLG NGGPAPESVT EKIYSITKTI SEYKMVKIPP LDLTTTGVRR YGPLTVEVID 

       190        200        210        220        230        240 
PVKDYVQLMK EIFDFDLIRS FLSKNPDFTF VFDALHGITG PYGEALFCKE LGMPSSVCQN 

       250        260        270        280        290        300 
CKPLPDFGGG HPDPNLTYAK SLVARVDRDN IVMGAASDGD GDRNMIYGAN AFVTPSDSVA 

       310        320        330        340        350        360 
IIAHHAELIP YFRDGGVHGF ARSMPTSGAI DRVGKYKGKN VYEVPTGWKF FCNLFDAKRL 

       370        380        390        400        410        420 
SICGEESFGT GSDHIREKDG VWGILCWLNI LAGLNAQNPK IKTLIDVKKD FYNIYGRTFY 

       430        440        450        460        470        480 
SRYDYEELEN EAAGKVMDRM RAIADDKSKV GEAVLPGFVV SEAGDFEYHD PIDGSESKHQ 

       490        500        510        520        530        540 
GLYIKFENGS RIVTRLSGTG SSGATLRLYM EKHESDSSKF DLDAQVALKP VVHAALEILA 

       550 
LEELTGRKEP TVIT

« 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]"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 THR-111 AND SER-113, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA19371.1.
PIRT40234.
RefSeqNP_596153.1. NM_001022072.1.

3D structure databases

ProteinModelPortalO74374.
SMRO74374. Positions 2-554.
ModBaseSearch...

Protein-protein interaction databases

STRINGO74374.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC32F12.10.1; SPBC32F12.10.1:pep; SPBC32F12.10.
GeneID2540254.
KEGGspo:SPBC32F12.10.
NMPDRfig|4896.1.peg.2019.

Organism-specific databases

GeneDB_SpombeSPBC32F12.10.

Phylogenomic databases

eggNOGfuNOG05018.
GeneTreeEFGT00050000004522.
HOGENOMHBG286308.
OMASIFFSID.
OrthoDBEOG4D82F2.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-004189-MONOMER.

Gene expression databases

ArrayExpressO74374.

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.
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. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGM_SCHPO
AccessionPrimary (citable) accession number: O74374
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: December 14, 2011
This is version 85 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