Reviewed, UniProtKB/Swiss-Prot P33401 (PGM1_YEAST)

Names and origin

Protein names

Recommended name:
    Phosphoglucomutase-1
      Short name=PGM 1
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase 1

Gene names

Name:	PGM1
Ordered Locus Names:	YKL127W

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	570 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 9820 molecules/cell in log phase SD medium. Ref.3
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
Gene Ontology (GO)
Biological process	UDP-glucose metabolic process Inferred from genetic interaction. Source: SGD galactose catabolic process Ref.1 Inferred from genetic interaction. Source: SGD glucose 1-phosphate utilization Ref.1 Inferred from genetic interaction. Source: SGD glycogen biosynthetic process Inferred from genetic interaction. Source: SGD trehalose biosynthetic process Inferred from genetic interaction. Source: SGD
Cellular component	cytoplasm Inferred from direct assay. Source: SGD
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Ref.1 Inferred from genetic interaction. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
MGM1	P32266	1	EBI-13289,EBI-10865

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 570	570	Phosphoglucomutase-1		PRO_0000147796
Sites
	Active site	120	1	Phosphoserine intermediate By similarity
	Metal binding	120	1	Magnesium; via phosphate group By similarity
	Metal binding	291	1	Magnesium By similarity
	Metal binding	293	1	Magnesium By similarity
	Metal binding	295	1	Magnesium By similarity
Amino acid modifications
	Modified residue	118	1	Phosphothreonine Ref.7
	Modified residue	120	1	Phosphoserine Ref.7 Ref.4 Ref.5 Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P33401-1 [UniParc]. Last modified February 1, 1994. Version 1. Checksum: D6C5EA41AC62CE85	FASTA	570	63,112
	10 20 30 40 50 60 MSLLIDSVPT VAYKDQKPGT SGLRKKTKVF MDEPHYTENF IQATMQSIPN GSEGTTLVVG 70 80 90 100 110 120 GDGRFYNDVI MNKIAAVGAA NGVRKLVIGQ GGLLSTPAAS HIIRTYEEKC TGGGIILTAS 130 140 150 160 170 180 HNPGGPENDL GIKYNLPNGG PAPESVTNAI WEASKKLTHY KIIKNFPKLN LNKLGKNQKY 190 200 210 220 230 240 GPLLVDIIDP AKAYVQFLKE IFDFDLIKSF LAKQRKDKGW KLLFDSLNGI TGPYGKAIFV 250 260 270 280 290 300 DEFGLPAEEV LQNWHPLPDF GGLHPDPNLT YARTLVDRVD REKIAFGAAS DGDGDRNMIY 310 320 330 340 350 360 GYGPAFVSPG DSVAIIAEYA PEIPYFAKQG IYGLARSFPT SSAIDRVAAK KGLRCYEVPT 370 380 390 400 410 420 GWKFFCALFD AKKLSICGEE SFGTGSNHIR EKDGLWAIIA WLNILAIYHR RNPEKEASIK 430 440 450 460 470 480 TIQDEFWNEY GRTFFTRYDY EHIECEQAEK VVALLSEFVS RPNVCGSHFP ADESLTVIDC 490 500 510 520 530 540 GDFSYRDLDG SISENQGLFV KFSNGTKFVL RLSGTGSSGA TIRLYVEKYT DKKENYGQTA 550 560 570 DVFLKPVINS IVKFLRFKEI LGTDEPTVRT

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: 8119301] [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: 8196765] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[3]	"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: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[4]	"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: 15665377] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY.
[5]	"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: 17330950] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY.
[6]	"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: 17563356] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120, MASS SPECTROMETRY.
[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: 18407956] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-118 AND SER-120, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X72016 Genomic DNA. Translation: CAA50895.1. Z28127 Genomic DNA. Translation: CAA81968.1.
PIR	S41199.
RefSeq	NP_012795.1.
3D structure databases
HSSP	HSSP built from PDB template 3PMG based on UniProtKB P00949.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:4098N.
IntAct	P33401. 10 interactions.
STRING	P33401.
Proteomic databases
PeptideAtlas	P33401.
PRIDE	P33401.
Genome annotation databases
Ensembl	YKL127W; YKL127W; YKL127W; Saccharomyces cerevisiae. [Genome view]
GeneID	853732.
GenomeReviews	Gene locus YKL127W in contig Y13137_GR.
KEGG	sce:YKL127W.
NMPDR	fig|4932.3.peg.3776.
Organism-specific databases
CYGD	YKL127w.
SGD	S000001610. PGM1.
Phylogenomic databases
HOGENOM	P33401.
OMA	KIELYET.
Enzyme and pathway databases
BRENDA	5.4.2.2. 250.
Gene expression databases
ArrayExpress	P33401.
Genevestigator	P33401.
GermOnline	YKL127W. Saccharomyces cerevisiae.
Family and domain databases
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. A-D-PHexomutase_N. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	974772.

Entry information

Entry name

PGM1_YEAST

Accession

Primary (citable) accession number: P33401

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	February 1, 1994
Last modified:	November 3, 2009
This is version 85 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)