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Protein

Phosphoglucomutase

Gene

SPBC32F12.10

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate. Key enzyme in hexose metabolism. The reverse reaction is an essential step for biosynthesis because glucose 1-phosphate is the starting point for the synthesis of UDP-glucose, which acts as a precursor for the synthesis of oligosaccharides and trehalose.By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-SPO-3322077. Glycogen synthesis.
R-SPO-70221. Glycogen breakdown (glycogenolysis).
R-SPO-70370. Galactose catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
PhosphoglucomutaseBy similarity (EC:5.4.2.2By similarity)
Short name:
PGMBy similarity
Alternative name(s):
Glucose phosphomutase
Gene namesi
ORF Names:SPBC32F12.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC32F12.10.
PomBaseiSPBC32F12.10.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 554554PhosphoglucomutasePRO_0000147795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei111 – 1111Phosphothreonine1 Publication
Modified residuei113 – 1131Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO74374.
PRIDEiO74374.

PTM databases

iPTMnetiO74374.

Interactioni

Protein-protein interaction databases

BioGridi276785. 1 interaction.
MINTiMINT-4678553.

Structurei

3D structure databases

ProteinModelPortaliO74374.
SMRiO74374. Positions 2-554.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

HOGENOMiHOG000009550.
InParanoidiO74374.
KOiK01835.
OMAiPAYSKGI.
OrthoDBiEOG70S7FF.
PhylomeDBiO74374.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.

Sequencei

Sequence statusi: Complete.

O74374-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MIETIPTKPY EGQRPGTSGL RKKVTVFEQP NYVENFVQAT MDVVEPSAKG
60 70 80 90 100
AHLVVGGDGR YFNFHAIQVI AAIAAGNGVE KIIVGTNGYL STPAASHIIR
110 120 130 140 150
KYKLTGGIIL TASHNAGGPK NDFGIKYNLG NGGPAPESVT EKIYSITKTI
160 170 180 190 200
SEYKMVKIPP LDLTTTGVRR YGPLTVEVID PVKDYVQLMK EIFDFDLIRS
210 220 230 240 250
FLSKNPDFTF VFDALHGITG PYGEALFCKE LGMPSSVCQN CKPLPDFGGG
260 270 280 290 300
HPDPNLTYAK SLVARVDRDN IVMGAASDGD GDRNMIYGAN AFVTPSDSVA
310 320 330 340 350
IIAHHAELIP YFRDGGVHGF ARSMPTSGAI DRVGKYKGKN VYEVPTGWKF
360 370 380 390 400
FCNLFDAKRL SICGEESFGT GSDHIREKDG VWGILCWLNI LAGLNAQNPK
410 420 430 440 450
IKTLIDVKKD FYNIYGRTFY SRYDYEELEN EAAGKVMDRM RAIADDKSKV
460 470 480 490 500
GEAVLPGFVV SEAGDFEYHD PIDGSESKHQ GLYIKFENGS RIVTRLSGTG
510 520 530 540 550
SSGATLRLYM EKHESDSSKF DLDAQVALKP VVHAALEILA LEELTGRKEP

TVIT
Length:554
Mass (Da):60,599
Last modified:November 1, 1998 - v1
Checksum:i5B064562A22A1358
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19371.1.
PIRiT40234.
RefSeqiNP_596153.1. NM_001022072.2.

Genome annotation databases

EnsemblFungiiSPBC32F12.10.1; SPBC32F12.10.1:pep; SPBC32F12.10.
GeneIDi2540254.
KEGGispo:SPBC32F12.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAA19371.1.
PIRiT40234.
RefSeqiNP_596153.1. NM_001022072.2.

3D structure databases

ProteinModelPortaliO74374.
SMRiO74374. Positions 2-554.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276785. 1 interaction.
MINTiMINT-4678553.

PTM databases

iPTMnetiO74374.

Proteomic databases

MaxQBiO74374.
PRIDEiO74374.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC32F12.10.1; SPBC32F12.10.1:pep; SPBC32F12.10.
GeneIDi2540254.
KEGGispo:SPBC32F12.10.

Organism-specific databases

EuPathDBiFungiDB:SPBC32F12.10.
PomBaseiSPBC32F12.10.

Phylogenomic databases

HOGENOMiHOG000009550.
InParanoidiO74374.
KOiK01835.
OMAiPAYSKGI.
OrthoDBiEOG70S7FF.
PhylomeDBiO74374.

Enzyme and pathway databases

ReactomeiR-SPO-3322077. Glycogen synthesis.
R-SPO-70221. Glycogen breakdown (glycogenolysis).
R-SPO-70370. Galactose catabolism.

Miscellaneous databases

PROiO74374.

Family and domain databases

Gene3Di3.30.310.50. 1 hit.
3.40.120.10. 3 hits.
InterProiIPR005844. 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]
PfamiPF02878. 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]
PRINTSiPR00509. PGMPMM.
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-111 AND SER-113, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiPGM_SCHPO
AccessioniPrimary (citable) accession number: O74374
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.