Phosphoglucomutase-2 - Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

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P37012 (PGM2_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 123. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Phosphoglucomutase-2
Short name=PGM 2
EC=5.4.2.2

Alternative name(s):
Glucose phosphomutase 2

Gene names

Name:	PGM2
Synonyms:	GAL5
Ordered Locus Names:	YMR105C
ORF Names:	YM9718.04C

Organism

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›

Protein attributes

Sequence length	569 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	This enzyme participates in both the breakdown and synthesis of glucose. Can also act on mannose.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subunit structure	Monomer By similarity.
Subcellular location	Cytoplasm.
Miscellaneous	Present with 3790 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	UDP-glucose metabolic process Inferred from genetic interaction PubMed 9252577. Source: SGD cellular calcium ion homeostasis Inferred from mutant phenotype PubMed 10681519 PubMed 15252028. Source: SGD galactose catabolic process Inferred from mutant phenotype PubMed 13887540 PubMed 14264884 Ref.1. Source: SGD glucose 1-phosphate metabolic process Inferred from mutant phenotype PubMed 10681519 Ref.1. Source: SGD glucose 6-phosphate metabolic process Inferred from sequence or structural similarity Ref.1. Source: SGD glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW glycogen biosynthetic process Inferred from genetic interaction PubMed 9252577. Source: SGD trehalose biosynthetic process Inferred from genetic interaction PubMed 9252577. Source: SGD
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase activity Inferred from mutant phenotype PubMed 13887540 PubMed 2138705 Ref.1. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 569

569

Phosphoglucomutase-2

PRO_0000147797

Sites

Active site

119

Phosphoserine intermediate By similarity

Metal binding

119

Magnesium; via phosphate group By similarity

Metal binding

290

Magnesium By similarity

Metal binding

292

Magnesium By similarity

Metal binding

294

Magnesium By similarity

Amino acid modifications

Modified residue

117

Phosphothreonine Ref.9

Modified residue

119

Phosphoserine Ref.7 Ref.8 Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

P37012 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 45B78AFF8197645E
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FASTA

569

63,089

        10         20         30         40         50         60 
MSFQIETVPT KPYEDQKPGT SGLRKKTKVF KDEPNYTENF IQSIMEAIPE GSKGATLVVG 

        70         80         90        100        110        120 
GDGRYYNDVI LHKIAAIGAA NGIKKLVIGQ HGLLSTPAAS HIMRTYEEKC TGGIILTASH 

       130        140        150        160        170        180 
NPGGPENDMG IKYNLSNGGP APESVTNAIW EISKKLTSYK IIKDFPELDL GTIGKNKKYG 

       190        200        210        220        230        240 
PLLVDIIDIT KDYVNFLKEI FDFDLIKKFI DNQRSTKNWK LLFDSMNGVT GPYGKAIFVD 

       250        260        270        280        290        300 
EFGLPADEVL QNWHPSPDFG GMHPDPNLTY ASSLVKRVDR EKIEFGAASD GDGDRNMIYG 

       310        320        330        340        350        360 
YGPSFVSPGD SVAIIAEYAA EIPYFAKQGI YGLARSFPTS GAIDRVAKAH GLNCYEVPTG 

       370        380        390        400        410        420 
WKFFCALFDA KKLSICGEES FGTGSNHVRE KDGVWAIMAW LNILAIYNKH HPENEASIKT 

       430        440        450        460        470        480 
IQNEFWAKYG RTFFTRYDFE KVETEKANKI VDQLRAYVTK SGVVNSAFPA DESLKVTDCG 

       490        500        510        520        530        540 
DFSYTDLDGS VSDHQGLYVK LSNGARFVLR LSGTGSSGAT IRLYIEKYCD DKSQYQKTAE 

       550        560 
EYLKPIINSV IKFLNFKQVL GTEEPTVRT

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Fu L., Bounelis P., Dey N., Browne B.L., Marchase R.B., Bedwell D.M. Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII." Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T., Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K., Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P. Barrell B.G. Nature 387:90-93(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 204511 / S288c / AB972.
[4]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[5]	"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae." Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J. LaBaer J. Genome Res. 17:536-543(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 204508 / S288c.
[6]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[7]	"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N. Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, MASS SPECTROMETRY. Strain: YAL6B.
[8]	"Proteome-wide identification of in vivo targets of DNA damage checkpoint kinases." Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H. Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-119, MASS SPECTROMETRY.
[9]	"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 THR-117 AND SER-119, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S41200.
RefSeq	NP_013823.1. NM_001182605.1.
3D structure databases
ProteinModelPortal	P37012.
SMR	P37012. Positions 4-569.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-6499N.
IntAct	P37012. 27 interactions.
MINT	MINT-705119.
STRING	4932.YMR105C.
Proteomic databases
PaxDb	P37012.
PeptideAtlas	P37012.
PRIDE	P37012.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR105C; YMR105C; YMR105C.
GeneID	855131.
KEGG	sce:YMR105C.
Organism-specific databases
CYGD	YMR105c.
SGD	S000004711. PGM2.
Phylogenomic databases
eggNOG	COG0033.
GeneTree	ENSGT00390000011831.
HOGENOM	HOG000009550.
KO	K01835.
OMA	YLEAIPY.
OrthoDB	EOG4D82F2.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-17136. YEAST:YMR105C-MONOMER.
Gene expression databases
ArrayExpress	P37012.
Genevestigator	P37012.
GermOnline	YMR105C. Saccharomyces cerevisiae.
Family and domain databases
Gene3D	3.40.120.10. 3 hits.
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. IPR016066. A-D-PHexomutase_CS. IPR005841. Alpha-D-phosphohexomutase_SF. [Graphical view]
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. [Graphical view]
PRINTS	PR00509. PGMPMM.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	978502.

Entry information

Entry name

PGM2_YEAST

Accession

Primary (citable) accession number: P37012
Secondary accession number(s): D6VZS7

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	June 1, 1994
Last modified:	May 29, 2013
This is version 123 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

Yeast chromosome XIII

Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents