Reviewed, UniProtKB/Swiss-Prot O74478 (PGM2_SCHPO)

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

ORF Names:

SPCC1840.05c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	587 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 By similarity.
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. Nucleus Ref.2.
Sequence similarities	Belongs to the phosphohexose mutase family.

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
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.2 Inferred from direct assay. Source: GeneDB_SPombe nucleus Ref.2 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucomutase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 587	587	Phosphoglucomutase-2		PRO_0000315630
Sites
	Active site	149	1	Phosphoserine intermediate By similarity
	Metal binding	149	1	Magnesium; via phosphate group By similarity
	Metal binding	306	1	Magnesium By similarity
	Metal binding	308	1	Magnesium By similarity
	Metal binding	310	1	Magnesium By similarity
Amino acid modifications
	Modified residue	149	1	Phosphoserine Ref.3

Sequences

	Sequence		Length	Mass (Da)
	O74478-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 3A818C1C02CD5845	FASTA	587	65,494
	10 20 30 40 50 60 MDPILQELVD EWFKLDQDET TRNEVSQLIK AEDYATLKQI MHPRIGFGTS GLRAEIGAGF 70 80 90 100 110 120 ARMNCLTVIQ ASQGFAEYLL QTVPSAAKLG VVIGHDHRHK SNTFARLTAA VFLQKGFKTY 130 140 150 160 170 180 FFDHLVHTPL VPFAVKTLGT AAGVMITASH NPAAYNGYKV YWGNGCAIIP PHDKGIAACI 190 200 210 220 230 240 EKNLTPITWD KNLVENHKLA DRDFAVGLLK NYWSQLHEFH SENNFSLEMK SLKFVYTPIH 250 260 270 280 290 300 GVGLPFVTSA LHLFGEQGDM ISVPLQDSPN PDFPTVKFPN PEEEGALDLA YEQADANGIS 310 320 330 340 350 360 YVLATDPDAD RFAFAEKING AWRRFTGDEV GCILAYFIFQ EYKNVGKPID DFYVLSTTVS 370 380 390 400 410 420 SAMVKSMAKV EGFHHVETLT GFKWLGNKAL ELEKQGKFIG LAYEEALGYM VGSIVRDKDG 430 440 450 460 470 480 VNALITFLHL LKRLQLQNLS ITEVFEQMSK KYGYYTTQNS YFLSRDTPKL RALVDALRHY 490 500 510 520 530 540 DTKSGYPATL GSKKITNVRD LTTGYDSSST DGKATLPVSK SSDNVTFELE NGEVIMTIRT 550 560 570 580 SGTEPKLKFY ICARGHSLED SIKNATEVKQ AIKSEWFHPQ QNGLEEP

References

[1]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.
[2]	"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe." Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M. Nat. Biotechnol. 24:841-847(2006) [PubMed: 16823372] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[3]	"Phosphoproteome analysis of fission yeast." Wilson-Grady J.T., Villen J., Gygi S.P. J. Proteome Res. 7:1088-1097(2008) [PubMed: 18257517] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-149, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CU329672 Genomic DNA. Translation: CAA20128.1.
PIR	T41173.
RefSeq	NP_588504.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	O74478.
Genome annotation databases
GeneID	2538920.
KEGG	spo:SPCC1840.05c.
NMPDR	fig|4896.1.peg.842.
Organism-specific databases
GeneDB_Spombe	SPCC1840.05c.
Phylogenomic databases
eggNOG	fuNOG05584.
HOGENOM	HBG571743.
OMA	IGEDVDM.
OrthoDB	EOG93FJD2.
PhylomeDB	O74478.
Enzyme and pathway databases
BRENDA	5.4.2.2. 653.
Gene expression databases
ArrayExpress	O74478.
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. 2 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...

Entry information

Entry name

PGM2_SCHPO

Accession

Primary (citable) accession number: O74478

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	November 1, 1998
Last modified:	January 19, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)