UniProtKB - P37012 (PGM2_YEAST)
Protein
Phosphoglucomutase 2
Gene
PGM2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Functioni
Major phosphoglucomutase isozyme that catalyzes the reversible interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:5784209). Constitutes about 80-90% of the phosphoglucomutase activity in the cell (PubMed:14264884, PubMed:5231755). Key enzyme in hexose metabolism. The forward reaction is an essential step in the energy metabolism of galactose since the product of the galactose pathway enzymes in yeast is glucose 1-phosphate. The reverse reaction is an essential step for biosynthesis when carbon sources other than galactose are the energy source 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 (PubMed:14264884).2 Publications
Miscellaneous
Present with 3790 molecules/cell in log phase SD medium.1 Publication
Catalytic activityi
- EC:5.4.2.23 Publications
Cofactori
Mg2+2 Publications, Zn2+2 PublicationsNote: Binds 1 magnesium ion per subunit. Can also use Zn2+ as cofactor.2 Publications
Kineticsi
- KM=2.24 µM for alpha-D-glucose 1,6-diphosphate1 Publication
- KM=23.4 µM for alpha-D-glucose 1-phosphate1 Publication
- KM=26 µM for alpha-D-glucose 1-phosphate1 Publication
- KM=530 µM for D-ribose 1-phosphate1 Publication
- Vmax=33.7 µmol/min/mg enzyme for alpha-D-glucose 1-phosphate1 Publication
- Vmax=0.32 µmol/min/mg enzyme for D-ribose 1-phosphate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 20 | SubstrateBy similarity | 1 | |
Binding sitei | 24 | SubstrateBy similarity | 1 | |
Active sitei | 119 | Phosphoserine intermediateBy similarity | 1 | |
Metal bindingi | 119 | Magnesium; via phosphate groupBy similarity | 1 | |
Binding sitei | 132 | SubstrateBy similarity | 1 | |
Metal bindingi | 290 | MagnesiumBy similarity | 1 | |
Metal bindingi | 292 | MagnesiumBy similarity | 1 | |
Metal bindingi | 294 | MagnesiumBy similarity | 1 | |
Binding sitei | 359 | SubstrateBy similarity | 1 | |
Binding sitei | 391 | SubstrateBy similarity | 1 | |
Binding sitei | 522 | SubstrateBy similarity | 1 |
GO - Molecular functioni
- magnesium ion binding Source: InterPro
- phosphoglucomutase activity Source: SGD
GO - Biological processi
- carbohydrate metabolic process Source: GO_Central
- cellular calcium ion homeostasis Source: SGD
- cellular cation homeostasis Source: SGD
- galactose catabolic process Source: SGD
- glucose 1-phosphate metabolic process Source: SGD
- glucose 6-phosphate metabolic process Source: SGD
- glucose metabolic process Source: UniProtKB-KW
- glycogen biosynthetic process Source: SGD
- trehalose biosynthetic process Source: SGD
- UDP-glucose metabolic process Source: SGD
Keywordsi
Molecular function | Isomerase |
Biological process | Carbohydrate metabolism, Glucose metabolism |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BioCyci | MetaCyc:YMR105C-MONOMER |
Reactomei | R-SCE-3322077, Glycogen synthesis R-SCE-6798695, Neutrophil degranulation |
SABIO-RKi | P37012 |
Names & Taxonomyi
Protein namesi | Recommended name: Phosphoglucomutase 21 Publication (EC:5.4.2.23 Publications)Short name: PGM 21 Publication Alternative name(s): D-glucose-1,6-diphosphate:D-glucose-1-phosphate phosphotransferase1 Publication Glucose phosphomutase 2 |
Gene namesi | Ordered Locus Names:YMR105CImported ORF Names:YM9718.04C |
Organismi | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
Taxonomic identifieri | 559292 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › |
Proteomesi |
|
Organism-specific databases
EuPathDBi | FungiDB:YMR105C |
SGDi | S000004711, PGM2 |
Pathology & Biotechi
Disruption phenotypei
Blocks galactose utilization, but does not impair growth on glucose.1 Publication
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | RemovedCombined sources | |||
ChainiPRO_0000147797 | 2 – 569 | Phosphoglucomutase 2Add BLAST | 568 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserineCombined sources | 1 | |
Modified residuei | 111 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 117 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 119 | PhosphoserineCombined sources | 1 |
Post-translational modificationi
O-glycosylated with mannose residues (By similarity). Substrate of UDP-glucose--glycoprotein glucose phosphotransferase, linking glucose in a phosphodiester linkage to O-linked mannose (PubMed:8385141, PubMed:7929458).By similarity2 Publications
Keywords - PTMi
Acetylation, Glycoprotein, PhosphoproteinProteomic databases
MaxQBi | P37012 |
PaxDbi | P37012 |
PRIDEi | P37012 |
PTM databases
iPTMneti | P37012 |
Expressioni
Inductioni
Induced in response to galactose and severely repressed in response to glucose.1 Publication
Interactioni
Subunit structurei
Monomer.
1 PublicationProtein-protein interaction databases
BioGRIDi | 35280, 122 interactors |
DIPi | DIP-6499N |
IntActi | P37012, 28 interactors |
MINTi | P37012 |
STRINGi | 4932.YMR105C |
Miscellaneous databases
RNActi | P37012, protein |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 119 – 120 | Substrate bindingBy similarity | 2 | |
Regioni | 294 – 295 | Substrate bindingBy similarity | 2 | |
Regioni | 378 – 380 | Substrate bindingBy similarity | 3 |
Sequence similaritiesi
Belongs to the phosphohexose mutase family.Curated
Phylogenomic databases
eggNOGi | KOG0625, Eukaryota |
GeneTreei | ENSGT00940000173602 |
HOGENOMi | CLU_009330_0_1_1 |
InParanoidi | P37012 |
OMAi | DIYKIYA |
Family and domain databases
InterProi | View protein in InterPro IPR005844, 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 IPR036900, A-D-PHexomutase_C_sf IPR016066, A-D-PHexomutase_CS IPR005841, Alpha-D-phosphohexomutase_SF |
Pfami | View protein in Pfam PF02878, PGM_PMM_I, 1 hit PF02879, PGM_PMM_II, 1 hit PF02880, PGM_PMM_III, 1 hit PF00408, PGM_PMM_IV, 1 hit |
PRINTSi | PR00509, PGMPMM |
SUPFAMi | SSF53738, SSF53738, 3 hits SSF55957, SSF55957, 1 hit |
PROSITEi | View protein in PROSITE PS00710, PGM_PMM, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P37012-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE
60 70 80 90 100
GSKGATLVVG GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS
110 120 130 140 150
HIMRTYEEKC TGGIILTASH NPGGPENDMG IKYNLSNGGP APESVTNAIW
160 170 180 190 200
EISKKLTSYK IIKDFPELDL GTIGKNKKYG PLLVDIIDIT KDYVNFLKEI
210 220 230 240 250
FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD EFGLPADEVL
260 270 280 290 300
QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG
310 320 330 340 350
YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH
360 370 380 390 400
GLNCYEVPTG WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW
410 420 430 440 450
LNILAIYNKH HPENEASIKT IQNEFWAKYG RTFFTRYDFE KVETEKANKI
460 470 480 490 500
VDQLRAYVTK SGVVNSAFPA DESLKVTDCG DFSYTDLDGS VSDHQGLYVK
510 520 530 540 550
LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE EYLKPIINSV
560
IKFLNFKQVL GTEEPTVRT
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 27 | T → G AA sequence (PubMed:8385141).Curated | 1 | |
Sequence conflicti | 32 | D → G AA sequence (PubMed:8385141).Curated | 1 | |
Sequence conflicti | 272 | S → A AA sequence (PubMed:8385141).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X74823 Genomic DNA Translation: CAA52820.1 U09499 Genomic DNA Translation: AAA91282.1 Z49702 Genomic DNA Translation: CAA89741.1 AY723853 Genomic DNA Translation: AAU09770.1 BK006946 Genomic DNA Translation: DAA10001.1 |
PIRi | S41200 |
RefSeqi | NP_013823.1, NM_001182605.1 |
Genome annotation databases
EnsemblFungii | YMR105C_mRNA; YMR105C; YMR105C |
GeneIDi | 855131 |
KEGGi | sce:YMR105C |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X74823 Genomic DNA Translation: CAA52820.1 U09499 Genomic DNA Translation: AAA91282.1 Z49702 Genomic DNA Translation: CAA89741.1 AY723853 Genomic DNA Translation: AAU09770.1 BK006946 Genomic DNA Translation: DAA10001.1 |
PIRi | S41200 |
RefSeqi | NP_013823.1, NM_001182605.1 |
3D structure databases
SMRi | P37012 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 35280, 122 interactors |
DIPi | DIP-6499N |
IntActi | P37012, 28 interactors |
MINTi | P37012 |
STRINGi | 4932.YMR105C |
PTM databases
iPTMneti | P37012 |
Proteomic databases
MaxQBi | P37012 |
PaxDbi | P37012 |
PRIDEi | P37012 |
Genome annotation databases
EnsemblFungii | YMR105C_mRNA; YMR105C; YMR105C |
GeneIDi | 855131 |
KEGGi | sce:YMR105C |
Organism-specific databases
EuPathDBi | FungiDB:YMR105C |
SGDi | S000004711, PGM2 |
Phylogenomic databases
eggNOGi | KOG0625, Eukaryota |
GeneTreei | ENSGT00940000173602 |
HOGENOMi | CLU_009330_0_1_1 |
InParanoidi | P37012 |
OMAi | DIYKIYA |
Enzyme and pathway databases
BioCyci | MetaCyc:YMR105C-MONOMER |
Reactomei | R-SCE-3322077, Glycogen synthesis R-SCE-6798695, Neutrophil degranulation |
SABIO-RKi | P37012 |
Miscellaneous databases
PROi | PR:P37012 |
RNActi | P37012, protein |
Family and domain databases
InterProi | View protein in InterPro IPR005844, 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 IPR036900, A-D-PHexomutase_C_sf IPR016066, A-D-PHexomutase_CS IPR005841, Alpha-D-phosphohexomutase_SF |
Pfami | View protein in Pfam PF02878, PGM_PMM_I, 1 hit PF02879, PGM_PMM_II, 1 hit PF02880, PGM_PMM_III, 1 hit PF00408, PGM_PMM_IV, 1 hit |
PRINTSi | PR00509, PGMPMM |
SUPFAMi | SSF53738, SSF53738, 3 hits SSF55957, SSF55957, 1 hit |
PROSITEi | View protein in PROSITE PS00710, PGM_PMM, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PGM2_YEAST | |
Accessioni | P37012Primary (citable) accession number: P37012 Secondary accession number(s): D6VZS7 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 1, 1994 |
Last sequence update: | June 1, 1994 | |
Last modified: | December 2, 2020 | |
This is version 182 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- Yeast chromosome XIII
Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names - SIMILARITY comments
Index of protein domains and families - Yeast
Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD