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Reviewed, UniProtKB/Swiss-Prot P39671 (PGM_RHIRD)

Last modified September 22, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoglucomutase
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase
Gene names
Name: pgm
Synonyms: exoC, pscA
OrganismRhizobium radiobacter (Agrobacterium tumefaciens) (Agrobacterium radiobacter)
Taxonomic identifier358 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesRhizobiaceaeRhizobium/Agrobacterium groupAgrobacterium

Protein attributes

Sequence length542 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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 processCarbohydrate metabolism
Glucose metabolism
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processglucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglucomutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 542542Phosphoglucomutase
PRO_0000147808

Sites

Active site1121Phosphoserine intermediate By similarity
Metal binding1121Magnesium; via phosphate group By similarity
Metal binding2761Magnesium By similarity
Metal binding2781Magnesium By similarity
Metal binding2801Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P39671-1 [UniParc].

Last modified February 1, 1995. Version 1.
Checksum: F40AD8ED482E905D

FASTA54257,802
        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 

« Hide

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.

Cross-references

Sequence databases

AF033856 Genomic DNA. Translation: AAD03475.1.

3D structure databases

HSSPHSSP built from PDB template 3PMG based on UniProtKB P00949.
ModBaseSearch...

Enzyme and pathway databases

BRENDA5.4.2.2. 2199.

Family and domain databases

InterProIPR005844. 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]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 2 hits.
PfamPF02878. 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]
PRINTSPR00509. PGMPMM.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGM_RHIRD
AccessionPrimary (citable) accession number: P39671
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 22, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents