P39671 (PGM_RHIRD) Reviewed, UniProtKB/Swiss-Prot

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
Synonyms:	exoC, pscA

Organism

Rhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)

Taxonomic identifier

358 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Rhizobium/Agrobacterium group › Agrobacterium

Protein attributes

Sequence length	542 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. Required for the synthesis of capsular polysaccharide and normal lipopolysaccharide.
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: InterPro 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 – 542	542	Phosphoglucomutase		PRO_0000147808
Sites
	Active site	112	1	Phosphoserine intermediate By similarity
	Metal binding	112	1	Magnesium; via phosphate group By similarity
	Metal binding	276	1	Magnesium By similarity
	Metal binding	278	1	Magnesium By similarity
	Metal binding	280	1	Magnesium By similarity

Sequences

	Sequence		Length	Mass (Da)
	P39671 [UniParc]. Last modified February 1, 1995. Version 1. Checksum: F40AD8ED482E905D	FASTA	542	57,802
	10 20 30 40 50 60 MIKTIKTTPY QDQKPGTSGL RKKVPVFAQE NYAENFIQSI FDALEGFEGQ TLVIGGDGRY 70 80 90 100 110 120 YNREVIQKAI KMAAAAGFGK VLVGQGGILS TPAASNVIRK YKAFGGIVLS ASHNPGGPTE 130 140 150 160 170 180 DFGIKYNIGN GGPAPEKITD AIYARSKVID SYKISDAADI DLDKIGSFKV DELTVDVIDP 190 200 210 220 230 240 VADYAALMEE LFDFGAIRSL IAGGFKVVVD SMSAVTGPYA VEILEKRLGA PKGSVRNATP 250 260 270 280 290 300 LPDFGGHHPD PNLVHAKELY DDVMSPEGPD FGAASDGDGD RNMVVGKGMF VTPSDSLAII 310 320 330 340 350 360 AANAKLAPGY AAGISGIARS MPTSAAADRV AEKLGLGMYE TPTGWKFFGN LMDAGKVTIC 370 380 390 400 410 420 GEESFGTGSN HVREKDGLWA VLYWLNIVAA RKESVKDIVT KHWAEYGRNY YSRHDYEEVD 430 440 450 460 470 480 SDAANTLVAI LREKLATLPG TSYGNLKVAA ADDFAYHDPV DQSVSKNQGI RILFEGGSRI 490 500 510 520 530 540 VLRLSGTGTA GATLRLYVER YEPDAARHGI ETQSALADLI SVADTIAGIK AHTADSEPTV IT

References

[1]	"A chromosomal cluster of genes encoding ADP-glucose synthetase, glycogen synthase and phosphoglucomutase in Agrobacterium tumefaciens." Uttaro A.D., Ugalde R.A. Gene 150:117-122(1994) [PubMed: 7959036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A348.
[2]	"Biochemical characterization of avirulent exoC mutants of Agrobacterium tumefaciens." Uttaro A.D., Cangelosi G.A., Geremia R.A., Nester E.W., Ugalde R.A. J. Bacteriol. 172:1640-1646(1990) [PubMed: 2307661] [Abstract] Cited for: CHARACTERIZATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF033856 Genomic DNA. Translation: AAD03475.1.
3D structure databases
ProteinModelPortal	P39671.
SMR	P39671. Positions 2-542.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
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. Alpha-D-phosphohexomutase_SF. [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.
SUPFAM	SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PGM_RHIRD

Accession

Primary (citable) accession number: P39671

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	February 1, 1995
Last modified:	May 31, 2011
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program