Reviewed, UniProtKB/Swiss-Prot P40390 (PGM_NEIGO)

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

Neisseria gonorrhoeae

Taxonomic identifier

485 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length	460 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.
Catalytic activity	Alpha-D-glucose 1-phosphate = alpha-D-glucose 6-phosphate.
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Biological process	Carbohydrate metabolism Glucose metabolism
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	glucose metabolic process Inferred from electronic annotation. Source: UniProtKB-KW
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 – 460	460	Phosphoglucomutase		PRO_0000147810
Sites
	Active site	103	1	Phosphoserine intermediate By similarity
	Metal binding	103	1	Magnesium; via phosphate group By similarity
	Metal binding	239	1	Magnesium By similarity
	Metal binding	241	1	Magnesium By similarity
	Metal binding	243	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P40390-1 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: 24AB77C7B8AE6391	FASTA	460	49,466
	10 20 30 40 50 60 MASITRDIFK AYDIRGIVGK TLTDDAAYFI GRAIAAKAAE KGIARIALGR DGRLSGPELM 70 80 90 100 110 120 EHIQRGLTDS GISVLNVGMV TTPMLYFAAV NECGGSGVMI TGSHNPPDYN GFKMMLGGDT 130 140 150 160 170 180 LAGEAIQELL AIVEKDGFVA ADKQGSVTEK DISGAYHDHI VGHVKLKRPI NIAIDAGNGV 190 200 210 220 230 240 GGAFAGKLYK GLGNEVTELF CEVDGNFPNH HPDPSKPENL QDLIAALKNG DAEIGLAFDG 250 260 270 280 290 300 DADRLGVVTK DGNIIYPDRQ LMLFAQDVLN RNPGAKVIFD VKSTRLLAPW IKEHGGEAIM 310 320 330 340 350 360 EKTGHSFIKS AMKKTGALVA GEMSGHVFFK ERWFGFDDGL YAGARLLEIL SASDNPSEVL 370 380 390 400 410 420 DNLPQSISTP ELNISLPEGS NGHQVIEELA AKAEFEGATE IITIDGLRVE FPDGFGLMRA 430 440 450 460 SNTTPILVLR FEADTQAAIE RIQNRFKAVI ESNPHLIWPL

References

[1]	"Lipooligosaccharide biosynthesis in pathogenic Neisseria. Cloning, identification, and characterization of the phosphoglucomutase gene." Zhou D., Stephens D.S., Gibson B.W., Engstrom J.J., McAllister C.F., Lee F.K.N., Apicella M.A. J. Biol. Chem. 269:11162-11169(1994) [PubMed: 8157643] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1291.
[2]	"Role of phosphoglucomutase in lipooligosaccharide biosynthesis in Neisseria gonorrhoeae." Sandlin R.C., Stein D.C. J. Bacteriol. 176:2930-2937(1994) [PubMed: 8188595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 1291.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U02489 Genomic DNA. Translation: AAA20588.1. L23426 Unassigned DNA. Translation: AAA20399.1.
PIR	A53614.
3D structure databases
HSSP	HSSP built from PDB template 1K2Y based on UniProtKB P26276.
ModBase	Search...
Enzyme and pathway databases
BRENDA	5.4.2.2. 588.
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...

Entry information

Entry name

PGM_NEIGO

Accession

Primary (citable) accession number: P40390

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)