Q03262 (PGM3_YEAST) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Phosphoglucomutase-3
Short name=PGM-3
EC=5.4.2.2

Alternative name(s):
Glucose phosphomutase-3

Gene names

Name:	PGM3
Ordered Locus Names:	YMR278W
ORF Names:	YM8021.04

Organism

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

Taxonomic identifier

559292 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Fungi › Dikarya › Ascomycota › saccharomyceta › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces › Saccharomyces cerevisiae

Protein attributes

Sequence length	622 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. Ref.6
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subcellular location	Cytoplasm. Nucleus Ref.3.
Miscellaneous	Present with 4960 molecules/cell in log phase SD medium.
Sequence similarities	Belongs to the phosphohexose mutase family.
Biophysicochemical properties	Kinetic parameters: KM=2.0 mM for alpha-D-glucose 1-phosphate Ref.6

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Cellular component	Cytoplasm Nucleus
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	glucose 1-phosphate metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Inferred from direct assay Ref.3. Source: SGD
Molecular_function	magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase activity Inferred from direct assay Ref.6. Source: SGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 622	622	Phosphoglucomutase-3		PRO_0000148022
Sites
	Active site	158	1	Phosphoserine intermediate
	Metal binding	158	1	Magnesium; via phosphate group By similarity
	Metal binding	325	1	Magnesium By similarity
	Metal binding	327	1	Magnesium By similarity
	Metal binding	329	1	Magnesium By similarity
Amino acid modifications
	Modified residue	156	1	Phosphothreonine Ref.7
	Modified residue	158	1	Phosphoserine Ref.5 Ref.7
Experimental info
	Mutagenesis	158	1	S → T: Loss of function. Ref.6
	Mutagenesis	326	1	P → G: No effect. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Q03262 [UniParc]. Last modified November 1, 1997. Version 1. Checksum: E402A69551B36CD3	FASTA	622	71,069
	10 20 30 40 50 60 MLQGILETVP SDLKDPISLW FKQDRNPKTI EEVTALCKKS DWNELHKRFD SRIQFGTAGL 70 80 90 100 110 120 RSQMQAGFSR MNTLVVIQAS QGLATYVRQQ FPDNLVAVVG HDHRFHSKEF ARATAAAFLL 130 140 150 160 170 180 KGFKVHYLNP DHEFVHTPLV PFAVDKLKAS VGVMITASHN PKMDNGYKVY YSNGCQIIPP 190 200 210 220 230 240 HDHAISDSID ANLEPWANVW DFDDVLNKAL KQGKLMYSRE EMLKLYLEEV SKNLVEINPL 250 260 270 280 290 300 KLEVKAKPWF VYTPMHGVGF DIFSTIVKKT LCLVEGKDYL CVPEQQNPDP SFPTVGFPNP 310 320 330 340 350 360 EEKGALDIGI NLAEKHDIDL LVANDPDADR FSVAVKDMQS GEWRQLTGNE IGFLFAFYEY 370 380 390 400 410 420 QKYKSMDKEF QHVHPLAMLN STVSSQMIKK MAEIEGFHYE DTLTGFKWIG NRAILLEKKG 430 440 450 460 470 480 YYVPFGFEEA IGYMFPAMEH DKDGISASIV FLQAYCKWKI DHNLDPLNVL ENGFKKYGVF 490 500 510 520 530 540 KEYNGYYVVP NPTVTKDIFD YIRNVYTPEG ASYPSSIGEE IEVLYYRDLT TGYQSDTINH 550 560 570 580 590 600 KPTLPVDPTS QMITVSARPS NGSENEHIRF TIRGSGTEPK LKVYIEACAN EEQRASFLAK 610 620 LTWNVLRREW FRPDEMNIVT KF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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. , Skelton J., Walsh S.V., Whitehead S., 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.
[2]	Saccharomyces Genome Database Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: ATCC 204508 / S288c.
[3]	"Global analysis of protein localization in budding yeast." Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K. Nature 425:686-691(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[4]	"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].
[5]	"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-158, MASS SPECTROMETRY. Strain: YAL6B.
[6]	"Molecular characterization reveals that YMR278w encoded protein is environmental stress response homologue of Saccharomyces cerevisiae PGM2." Tiwari A., Bhat J.P. Biochem. Biophys. Res. Commun. 366:340-345(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF SER-158 AND PRO-326.
[7]	"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-156 AND SER-158, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z49704 Genomic DNA. Translation: CAA89776.1. BK006946 Genomic DNA. Translation: DAA10179.1.
PIR	S54585.
RefSeq	NP_014005.1. NM_001182785.1.
3D structure databases
ProteinModelPortal	Q03262.
SMR	Q03262. Positions 55-333.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-5066N.
MINT	MINT-519611.
STRING	4932.YMR278W.
Proteomic databases
PaxDb	Q03262.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblFungi	YMR278W; YMR278W; YMR278W.
GeneID	855321.
KEGG	sce:YMR278W.
Organism-specific databases
CYGD	YMR278w.
SGD	S000004891. PGM3.
Phylogenomic databases
eggNOG	COG1109.
GeneTree	ENSGT00390000017247.
HOGENOM	HOG000268676.
KO	K01835.
OMA	YDGRHDS.
OrthoDB	EOG4N605B.
Enzyme and pathway databases
SABIO-RK	Q03262.
Gene expression databases
Genevestigator	Q03262.
GermOnline	YMR278W. 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. [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]
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	979026.

Entry information

Entry name

PGM3_YEAST

Accession

Primary (citable) accession number: Q03262
Secondary accession number(s): D6W0A5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 106 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program