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Protein

Phosphoglucomutase 1

Gene

PGM1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Minor phosphoglucomutase isozyme that catalyzes the interconversion of glucose 1-phosphate and glucose 6-phosphate (PubMed:5784209). Constitutes about 10-20% 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).3 Publications

Catalytic activityi

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

Cofactori

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

Kineticsi

  1. KM=60 µM for alpha-D-glucose 1-phosphate1 Publication
  1. Vmax=0.24 µmol/min/mg enzyme for alpha-D-glucose 1-phosphate1 Publication
  2. Vmax=0.06 µmol/min/mg enzyme for D-ribose 1-phosphate1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei20 – 201SubstrateBy similarity
Binding sitei24 – 241SubstrateBy similarity
Active sitei120 – 1201Phosphoserine intermediateBy similarity
Metal bindingi120 – 1201Magnesium; via phosphate groupBy similarity
Binding sitei133 – 1331SubstrateBy similarity
Metal bindingi291 – 2911MagnesiumBy similarity
Metal bindingi293 – 2931MagnesiumBy similarity
Metal bindingi295 – 2951MagnesiumBy similarity
Binding sitei360 – 3601SubstrateBy similarity
Binding sitei392 – 3921SubstrateBy similarity
Binding sitei523 – 5231SubstrateBy similarity

GO - Molecular functioni

  • magnesium ion binding Source: InterPro
  • phosphoglucomutase activity Source: SGD

GO - Biological processi

  • 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
Complete GO annotation...

Keywords - Molecular functioni

Isomerase

Keywords - Biological processi

Carbohydrate metabolism, Glucose metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17137.
YEAST:YKL127W-MONOMER.
ReactomeiR-SCE-3322077. Glycogen synthesis.
R-SCE-70221. Glycogen breakdown (glycogenolysis).
R-SCE-70370. Galactose catabolism.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoglucomutase 11 Publication (EC:5.4.2.21 Publication)
Short name:
PGM 11 Publication
Alternative name(s):
Glucose phosphomutase 1
Gene namesi
Name:PGM11 Publication
Ordered Locus Names:YKL127WImported
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL127W.
SGDiS000001610. PGM1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 570569Phosphoglucomutase 1PRO_0000147796Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources
Modified residuei120 – 1201PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP33401.
PeptideAtlasiP33401.
PRIDEiP33401.

PTM databases

iPTMnetiP33401.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

BioGridi34009. 79 interactions.
DIPiDIP-4098N.
IntActiP33401. 6 interactions.
MINTiMINT-492216.

Structurei

3D structure databases

ProteinModelPortaliP33401.
SMRiP33401. Positions 5-570.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni120 – 1212Substrate bindingBy similarity
Regioni295 – 2962Substrate bindingBy similarity
Regioni379 – 3813Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the phosphohexose mutase family.Curated

Phylogenomic databases

HOGENOMiHOG000009550.
InParanoidiP33401.
KOiK01835.
OMAiVEDICVE.
OrthoDBiEOG70S7FF.

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.
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.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33401-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSLLIDSVPT VAYKDQKPGT SGLRKKTKVF MDEPHYTENF IQATMQSIPN
60 70 80 90 100
GSEGTTLVVG GDGRFYNDVI MNKIAAVGAA NGVRKLVIGQ GGLLSTPAAS
110 120 130 140 150
HIIRTYEEKC TGGGIILTAS HNPGGPENDL GIKYNLPNGG PAPESVTNAI
160 170 180 190 200
WEASKKLTHY KIIKNFPKLN LNKLGKNQKY GPLLVDIIDP AKAYVQFLKE
210 220 230 240 250
IFDFDLIKSF LAKQRKDKGW KLLFDSLNGI TGPYGKAIFV DEFGLPAEEV
260 270 280 290 300
LQNWHPLPDF GGLHPDPNLT YARTLVDRVD REKIAFGAAS DGDGDRNMIY
310 320 330 340 350
GYGPAFVSPG DSVAIIAEYA PEIPYFAKQG IYGLARSFPT SSAIDRVAAK
360 370 380 390 400
KGLRCYEVPT GWKFFCALFD AKKLSICGEE SFGTGSNHIR EKDGLWAIIA
410 420 430 440 450
WLNILAIYHR RNPEKEASIK TIQDEFWNEY GRTFFTRYDY EHIECEQAEK
460 470 480 490 500
VVALLSEFVS RPNVCGSHFP ADESLTVIDC GDFSYRDLDG SISENQGLFV
510 520 530 540 550
KFSNGTKFVL RLSGTGSSGA TIRLYVEKYT DKKENYGQTA DVFLKPVINS
560 570
IVKFLRFKEI LGTDEPTVRT
Length:570
Mass (Da):63,112
Last modified:February 1, 1994 - v1
Checksum:iD6C5EA41AC62CE85
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72016 Genomic DNA. Translation: CAA50895.1.
Z28127 Genomic DNA. Translation: CAA81968.1.
BK006944 Genomic DNA. Translation: DAA09034.1.
PIRiS41199.
RefSeqiNP_012795.1. NM_001179693.1.

Genome annotation databases

EnsemblFungiiYKL127W; YKL127W; YKL127W.
GeneIDi853732.
KEGGisce:YKL127W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X72016 Genomic DNA. Translation: CAA50895.1.
Z28127 Genomic DNA. Translation: CAA81968.1.
BK006944 Genomic DNA. Translation: DAA09034.1.
PIRiS41199.
RefSeqiNP_012795.1. NM_001179693.1.

3D structure databases

ProteinModelPortaliP33401.
SMRiP33401. Positions 5-570.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34009. 79 interactions.
DIPiDIP-4098N.
IntActiP33401. 6 interactions.
MINTiMINT-492216.

PTM databases

iPTMnetiP33401.

Proteomic databases

MaxQBiP33401.
PeptideAtlasiP33401.
PRIDEiP33401.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL127W; YKL127W; YKL127W.
GeneIDi853732.
KEGGisce:YKL127W.

Organism-specific databases

EuPathDBiFungiDB:YKL127W.
SGDiS000001610. PGM1.

Phylogenomic databases

HOGENOMiHOG000009550.
InParanoidiP33401.
KOiK01835.
OMAiVEDICVE.
OrthoDBiEOG70S7FF.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17137.
YEAST:YKL127W-MONOMER.
ReactomeiR-SCE-3322077. Glycogen synthesis.
R-SCE-70221. Glycogen breakdown (glycogenolysis).
R-SCE-70370. Galactose catabolism.

Miscellaneous databases

NextBioi974772.
PROiP33401.

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.
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.
PROSITEiPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A family of hexosephosphate mutases in Saccharomyces cerevisiae."
    Boles E., Liebetrau W., Hofmann M., Zimmermann F.K.
    Eur. J. Biochem. 220:83-96(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Complete DNA sequence of yeast chromosome XI."
    Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
    , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
    Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. "The effect of mutation of two forms of phosphoglucomutase in Saccharomyces."
    Tsoi A., Douglas H.C.
    Biochim. Biophys. Acta 92:513-520(1964) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 8050B.
  5. Cited for: FUNCTION.
  6. "Genetic control of phosphoglucomutase variants in Saccharomyces cerevisiae."
    Bevan P., Douglas H.C.
    J. Bacteriol. 98:532-535(1969) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
    Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
    J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Strain: ADR376.
  10. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
    Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
    Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "The PGM3 gene encodes the major phosphoribomutase in the yeast Saccharomyces cerevisiae."
    Walther T., Baylac A., Alkim C., Vax A., Cordier H., Francois J.M.
    FEBS Lett. 586:4114-4118(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPGM1_YEAST
AccessioniPrimary (citable) accession number: P33401
Secondary accession number(s): D6VX68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: May 11, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 9820 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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.