Reviewed, UniProtKB/Swiss-Prot O74374 (PGM_SCHPO)

Names and origin

Protein names

Recommended name:
    Probable phosphoglucomutase
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase

Gene names

ORF Names:

SPBC32F12.10

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	554 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 By similarity.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Subcellular location	Cytoplasm By similarity.
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	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: GeneDB_SPombe nucleus 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 – 554	554	Probable phosphoglucomutase		PRO_0000147795
Sites
	Active site	113	1	Phosphoserine intermediate By similarity
	Metal binding	113	1	Magnesium; via phosphate group By similarity
	Metal binding	278	1	Magnesium By similarity
	Metal binding	280	1	Magnesium By similarity
	Metal binding	282	1	Magnesium By similarity
Amino acid modifications
	Modified residue	111	1	Phosphothreonine Ref.2
	Modified residue	113	1	Phosphoserine Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O74374-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 5B064562A22A1358	FASTA	554	60,599
	10 20 30 40 50 60 MIETIPTKPY EGQRPGTSGL RKKVTVFEQP NYVENFVQAT MDVVEPSAKG AHLVVGGDGR 70 80 90 100 110 120 YFNFHAIQVI AAIAAGNGVE KIIVGTNGYL STPAASHIIR KYKLTGGIIL TASHNAGGPK 130 140 150 160 170 180 NDFGIKYNLG NGGPAPESVT EKIYSITKTI SEYKMVKIPP LDLTTTGVRR YGPLTVEVID 190 200 210 220 230 240 PVKDYVQLMK EIFDFDLIRS FLSKNPDFTF VFDALHGITG PYGEALFCKE LGMPSSVCQN 250 260 270 280 290 300 CKPLPDFGGG HPDPNLTYAK SLVARVDRDN IVMGAASDGD GDRNMIYGAN AFVTPSDSVA 310 320 330 340 350 360 IIAHHAELIP YFRDGGVHGF ARSMPTSGAI DRVGKYKGKN VYEVPTGWKF FCNLFDAKRL 370 380 390 400 410 420 SICGEESFGT GSDHIREKDG VWGILCWLNI LAGLNAQNPK IKTLIDVKKD FYNIYGRTFY 430 440 450 460 470 480 SRYDYEELEN EAAGKVMDRM RAIADDKSKV GEAVLPGFVV SEAGDFEYHD PIDGSESKHQ 490 500 510 520 530 540 GLYIKFENGS RIVTRLSGTG SSGATLRLYM EKHESDSSKF DLDAQVALKP VVHAALEILA 550 LEELTGRKEP TVIT

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]

"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 THR-111 AND SER-113, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	CU329671 Genomic DNA. Translation: CAA19371.1.
PIR	T40234.
RefSeq	NP_596153.1.
3D structure databases
HSSP	HSSP built from PDB template 3PMG based on UniProtKB P00949.
ModBase	Search...
Protein-protein interaction databases
STRING	O74374.
Genome annotation databases
GeneID	2540254.
KEGG	spo:SPBC32F12.10.
NMPDR	fig|4896.1.peg.2019.
Organism-specific databases
GeneDB_Spombe	SPBC32F12.10.
Phylogenomic databases
OMA	YMKEAIQ.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-004189-MON.
BRENDA	5.4.2.2. 653.
Gene expression databases
ArrayExpress	O74374.
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. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGM_SCHPO

Accession

Primary (citable) accession number: O74374

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	November 1, 1998
Last modified:	November 3, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)