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Protein

Phosphoglucomutase-2

Gene

Pgm2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the conversion of the nucleoside breakdown products ribose-1-phosphate and deoxyribose-1-phosphate to the corresponding 5-phosphopentoses. May also catalyze the interconversion of glucose-1-phosphate and glucose-6-phosphate. Has low glucose 1,6-bisphosphate synthase activity (By similarity).By similarity

Catalytic activityi

Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Alpha-D-ribose 1-phosphate = D-ribose 5-phosphate.
2-deoxy-alpha-D-ribose 1-phosphate = 2-deoxy-alpha-D-ribose 5-phosphate.

Cofactori

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

Pathwayi: 2-deoxy-D-ribose 1-phosphate degradation

This protein is involved in step 1 of the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Phosphoglucomutase-2 (Pgm2)
  2. Deoxyribose-phosphate aldolase (Dera)
This subpathway is part of the pathway 2-deoxy-D-ribose 1-phosphate degradation, which is itself part of Carbohydrate degradation.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate, the pathway 2-deoxy-D-ribose 1-phosphate degradation and in Carbohydrate degradation.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei67SubstrateBy similarity1
Binding sitei71SubstrateBy similarity1
Active sitei173Phosphoserine intermediateBy similarity1
Metal bindingi173Magnesium; via phosphate groupBy similarity1
Metal bindingi330MagnesiumBy similarity1
Metal bindingi332MagnesiumBy similarity1
Metal bindingi334MagnesiumBy similarity1
Binding sitei408SubstrateBy similarity1
Binding sitei446SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • deoxyribose phosphate catabolic process Source: UniProtKB-UniPathway
  • glucose metabolic process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiR-MMU-3322077. Glycogen synthesis.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-70221. Glycogen breakdown (glycogenolysis).
R-MMU-70370. Galactose catabolism.
R-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).
UniPathwayiUPA00002; UER00467.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase-2 (EC:5.4.2.2)
Short name:
PGM 2
Alternative name(s):
Glucose phosphomutase 2
Phosphodeoxyribomutase
Phosphoglucomutase-1
Phosphopentomutase (EC:5.4.2.7)
Gene namesi
Name:Pgm2
Synonyms:Pgm1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:97564. Pgm1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001477821 – 620Phosphoglucomutase-2Add BLAST620

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei173PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ7TSV4.
MaxQBiQ7TSV4.
PaxDbiQ7TSV4.
PeptideAtlasiQ7TSV4.
PRIDEiQ7TSV4.

PTM databases

iPTMnetiQ7TSV4.
PhosphoSitePlusiQ7TSV4.

Expressioni

Tissue specificityi

Highly expressed in lung, spleen and thymus. Expressed at lower levels in liver, brain, kidney, skeletal muscle, testis and heart.1 Publication

Gene expression databases

BgeeiENSMUSG00000029171.
ExpressionAtlasiQ7TSV4. baseline and differential.
GenevisibleiQ7TSV4. MM.

Interactioni

Protein-protein interaction databases

IntActiQ7TSV4. 1 interactor.
MINTiMINT-4116798.
STRINGi10090.ENSMUSP00000084582.

Structurei

3D structure databases

ProteinModelPortaliQ7TSV4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni173 – 174Substrate bindingBy similarity2
Regioni334 – 335Substrate bindingBy similarity2
Regioni432 – 434Substrate bindingBy similarity3

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ7TSV4.
KOiK15779.
OMAiPLLHDPY.
OrthoDBiEOG091G040C.
PhylomeDBiQ7TSV4.
TreeFamiTF300692.

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.
IPR016066. A-D-PHexomutase_CS.
[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]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7TSV4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAATPTETP APEGSGLGMD ARLDQETAQW LRWDQNPLTS ESVKQLIAGG
60 70 80 90 100
NKEELRKCFG ARMEFGTAGL RAPMGAGISR MNDLTIIQTT QGFCRYLEKQ
110 120 130 140 150
FSDLKQRGVV ISFDARAHPA SGGSSRRFAR LAATAFITQG VPVYLFSDIT
160 170 180 190 200
PTPFVPYTVS HLKLCAGIMI TASHNPKQDN GYKVYWDNGA QIISPHDRGI
210 220 230 240 250
SQAIEENLEP WPQAWEESLV DSSPLLHNPS ASIGNDYFED LKKYCFHRTV
260 270 280 290 300
NKESKVKFVH TSVHGVGHEF VQLAFKAFDL APPEAVPQQK DPDPEFPTVK
310 320 330 340 350
YPNPEEGKGV LTLSFALADK IKAKIVLAND PDADRLAVAE KQDSGEWRVF
360 370 380 390 400
SGNELGALLG WWLFTSWKEK NQDQSNLKDT YMLSSTVSSK ILRAIALKEG
410 420 430 440 450
FHFEETLTGF KWMGNRAQQL GDQGKTVLFA FEEAIGYMCC PFVLDKDGVS
460 470 480 490 500
AAVICAELAS FLATKNLSLS QQLNAIYVEY GYHITTASYF ICHDQGTIQN
510 520 530 540 550
LFGNLRNYDG KNNYPKMCGK FEISAIRDLT TGYDDSQPDK KAVLPTSKSS
560 570 580 590 600
QMITFTFANG GVATMRTSGT EPKIKYYAEL CAPPGNSDPE HLKKELDELV
610 620
GAIEEHFFQP QKYNLQPKAE
Length:620
Mass (Da):68,748
Last modified:October 1, 2003 - v1
Checksum:iF2535A3F700EFD50
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC030869 mRNA. Translation: AAH30869.1.
BC052762 mRNA. Translation: AAH52762.1.
AK014332 mRNA. Translation: BAB29278.1.
CCDSiCCDS19300.1.
RefSeqiNP_079976.1. NM_025700.2.
UniGeneiMm.2325.

Genome annotation databases

EnsembliENSMUST00000087324; ENSMUSP00000084582; ENSMUSG00000029171.
GeneIDi66681.
KEGGimmu:66681.
UCSCiuc008xmi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC030869 mRNA. Translation: AAH30869.1.
BC052762 mRNA. Translation: AAH52762.1.
AK014332 mRNA. Translation: BAB29278.1.
CCDSiCCDS19300.1.
RefSeqiNP_079976.1. NM_025700.2.
UniGeneiMm.2325.

3D structure databases

ProteinModelPortaliQ7TSV4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ7TSV4. 1 interactor.
MINTiMINT-4116798.
STRINGi10090.ENSMUSP00000084582.

PTM databases

iPTMnetiQ7TSV4.
PhosphoSitePlusiQ7TSV4.

Proteomic databases

EPDiQ7TSV4.
MaxQBiQ7TSV4.
PaxDbiQ7TSV4.
PeptideAtlasiQ7TSV4.
PRIDEiQ7TSV4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000087324; ENSMUSP00000084582; ENSMUSG00000029171.
GeneIDi66681.
KEGGimmu:66681.
UCSCiuc008xmi.1. mouse.

Organism-specific databases

CTDi5236.
MGIiMGI:97564. Pgm1.

Phylogenomic databases

eggNOGiKOG1220. Eukaryota.
COG1109. LUCA.
GeneTreeiENSGT00390000017247.
HOGENOMiHOG000268676.
HOVERGENiHBG056917.
InParanoidiQ7TSV4.
KOiK15779.
OMAiPLLHDPY.
OrthoDBiEOG091G040C.
PhylomeDBiQ7TSV4.
TreeFamiTF300692.

Enzyme and pathway databases

UniPathwayiUPA00002; UER00467.
ReactomeiR-MMU-3322077. Glycogen synthesis.
R-MMU-6798695. Neutrophil degranulation.
R-MMU-70221. Glycogen breakdown (glycogenolysis).
R-MMU-70370. Galactose catabolism.
R-MMU-71336. Pentose phosphate pathway (hexose monophosphate shunt).

Miscellaneous databases

ChiTaRSiPgm2. mouse.
PROiQ7TSV4.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000029171.
ExpressionAtlasiQ7TSV4. baseline and differential.
GenevisibleiQ7TSV4. MM.

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.
IPR016066. A-D-PHexomutase_CS.
[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]
SUPFAMiSSF53738. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPGM2_MOUSE
AccessioniPrimary (citable) accession number: Q7TSV4
Secondary accession number(s): Q8K0P7, Q9CRS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 1, 2003
Last modified: November 30, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

There is a known reversal of the Pgm1 and Pgm2 nomenclature applied to mouse versus other vertebrates. The official name of this gene in mouse is Pgm1 but it is the ortholog of other vertebrate PGM2 genes.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.