Reviewed, UniProtKB/Swiss-Prot O15820 (PGM_ENTHI)

Names and origin

Protein names

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

Gene names

Name:

pgm

Organism

Entamoeba histolytica

Taxonomic identifier

5759 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Archamoebae › Entamoebidae › Entamoeba

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript 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
Cellular component	Cytoplasm
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro signal transduction Inferred from electronic annotation. Source: InterPro
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 – 553	553	Phosphoglucomutase		PRO_0000147792
Sites
	Active site	117	1	Phosphoserine intermediate By similarity
	Metal binding	117	1	Magnesium; via phosphate group By similarity
	Metal binding	289	1	Magnesium By similarity
	Metal binding	291	1	Magnesium By similarity
	Metal binding	293	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	O15820-1 [UniParc]. Last modified January 1, 1998. Version 1. Checksum: 2312137FC0A0865A	FASTA	553	60,788
	10 20 30 40 50 60 MQATIKRYPT SPISGQTLGT SGLRKRASEV ENTPNYLENF VNAMFNAASN LQKPGKIIIG 70 80 90 100 110 120 GDGRYLNLKA LDIIIRVALS RGFTDIVVGK SGFMSTPAES ATIIRRKAEA GFIMTASHNP 130 140 150 160 170 180 AGKEHGDFGL KLNMSNGGPA PIEVTSKIEE SARNIKEIVI AELNKPLNID SVGDIEIECE 190 200 210 220 230 240 GKKAVVHVID PLEDYIAYLH ECFDFENLKQ FVSKYHLKVQ VDGFNAVTGI YNKKVFCELL 250 260 270 280 290 300 GLPESSLKNA IPMPDFGGKH PDPNLTYAAE LVHAVIPEDS PYDIGFAFDG DGDRNLIVGR 310 320 330 340 350 360 GAFVSPSDSL AILSTKYNDI PFFVKNGFKG VARSMPTSAA VDHVTSITET PTGWKFFGNL 370 380 390 400 410 420 MDSGKISLCG EESFGTGCCG IREKDGIWAA LCWVSILAAE SERAQRLVGV KEILESHWAK 430 440 450 460 470 480 YGRNYYQRYD FDEVDKKAAE DMMQMMRDNA KTVKCDLNGV PLKFCDDFEY HDSVDGSVTS 490 500 510 520 530 540 KQGIRFVFED GSRIIFRLSG TGSVGATIRV YFDKYSKDYK ADQTKVLADM VTVAYAVSQI 550 TKFTGREKPS VVT

References

[1]

"Molecular and biochemical characterization of phosphoglucomutases from Entamoeba histolytica and Entomoeba dispar." Ortner S., Binder M., Scheiner O., Wiedermann G., Duchene M. Mol. Biochem. Parasitol. 90:121-129(1997) [PubMed: 9497037] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: SFL-3.

Cross-references

Sequence databases
EMBLGenBankDDBJ	Y14444 mRNA. Translation: CAA74796.1.
3D structure databases
HSSP	HSSP built from PDB template 1KFI based on UniProtKB P47244.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.4.2.2. 323.
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. IPR001610. PAC. [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.
SMART	SM00086. PAC. 1 hit. [Graphical view]
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGM_ENTHI

Accession

Primary (citable) accession number: O15820

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 25, 2005
Last sequence update:	January 1, 1998
Last modified:	June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)