Reviewed, UniProtKB/Swiss-Prot Q54UQ2 (PGM2_DICDI)

Names and origin

Protein names

Recommended name:
    Probable phosphoglucomutase-2
      Short name=PGM 2
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase 2

Gene names

Name:	pgmB
ORF Names:	DDB_G0280897

Organism

Dictyostelium discoideum (Slime mold) [Complete proteome]

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	603 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

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	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
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 – 603	603	Probable phosphoglucomutase-2		PRO_0000328516
Sites
	Active site	149	1	Phosphoserine intermediate By similarity
	Metal binding	149	1	Magnesium; via phosphate group By similarity
	Metal binding	310	1	Magnesium By similarity
	Metal binding	312	1	Magnesium By similarity
	Metal binding	314	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q54UQ2-1 [UniParc]. Last modified May 24, 2005. Version 1. Checksum: D2E413FEC3995117	FASTA	603	67,535
	10 20 30 40 50 60 MTDKINNLIN QWLKWDKNEI TRKEIEQLKE NNNEKELLVR LEERIQFGTA GLRGAMRAGF 70 80 90 100 110 120 SCMNDLTVTQ ASQGLCEYVI ETIEQSKSKG IVIGYDGRHN SYIFAKITAA TFKSKGFKVY 130 140 150 160 170 180 LFSHIVPTPY VSFAVPNLKA AIGVMITASH NPKNDNGYKV YWETGCQINT PHDKGISKKI 190 200 210 220 230 240 DENLEPWSNV DATSDIKYGN GDDGESMIDP LSVITELYNK NIKEYSVGSK IELANEPIVY 250 260 270 280 290 300 TAMHGVGGVY AKKAFETFQL KPFIPVAQQI EPDAEFPTVT YPNPEEGKGA LKLSIETAEA 310 320 330 340 350 360 NNSRLILAND PDADRLAVAE KLADGSWKVF NGNEIGVLLA DWAWTNRSTL TKGGSTLENN 370 380 390 400 410 420 KYFMINTAVS SAMLKTMSEK EGFIHQECLT GFKWIGNAAY NAINNNDGTT FLFGYEEAIG 430 440 450 460 470 480 FQYGDVSFDK DGVRAAAIFA EFALSLYKKG SSVQDHLESM YKRYGYHISK NRYFFCYEPS 490 500 510 520 530 540 KMVSIFNKIR NDGKYLTKLG DDDDEQFTIT RIRDLTTGYD NGYPDCKARL PVSSSTQMIT 550 560 570 580 590 600 FYFKNGGIAT LRGSGTEPKL KYYVEMIGEV KSNVESTLTK AVELVINQLL KPIENQLEPP KDD

References

[1]

"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AAFI02000039 Genomic DNA. Translation: EAL66990.1.
RefSeq	XP_640969.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q54UQ2.
Genome annotation databases
GeneID	3392061.
GenomeReviews	Gene locus pgmB in contig CM000152_GR.
KEGG	ddi:DDB_0238765.
Organism-specific databases
dictyBase	DDB_G0280897. pgmB.
Phylogenomic databases
OMA	IGEDVDM.
Enzyme and pathway databases
BRENDA	5.4.2.2. 424.
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. 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. [Graphical view]
PRINTS	PR00509. PGMPMM.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGM2_DICDI

Accession

Primary (citable) accession number: Q54UQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 8, 2008
Last sequence update:	May 24, 2005
Last modified:	November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)