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Reviewed, UniProtKB/Swiss-Prot Q9M4G4 (PGMC_SOLTU)

Last modified June 16, 2009. Version 47. 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, cytoplasmic
      Short name=PGM
    EC=5.4.2.2
Alternative name(s):
    Glucose phosphomutase
Gene names
Name: PGM1
Synonyms: PGM I
OrganismSolanum tuberosum (Potato)
Taxonomic identifier4113 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum

Protein attributes

Sequence length583 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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
   Biological processCarbohydrate metabolism
Glucose metabolism
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processglucose metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 – 583583Phosphoglucomutase, cytoplasmic
PRO_0000147806

Sites

Active site1241Phosphoserine intermediate By similarity
Metal binding1241Magnesium; via phosphate group By similarity
Metal binding3001Magnesium By similarity
Metal binding3021Magnesium By similarity
Metal binding3041Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9M4G4-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: DF3E24B9972C7CCA

FASTA58363,470
        10         20         30         40         50         60 
MANFKVSRVE TTPFEGQKPG TSGLRKKVKV FIQPHYLQNF VQATFNALGA DRVEGATLVV 

        70         80         90        100        110        120 
SGDGRYYSKD AIQIITKMAA ANGVRRVWIG QNGLLSTPAV SAVVRERVGA DGSKATGAFI 

       130        140        150        160        170        180 
LTASHNPGGP HEDFGIKYNM ENGGPAPEGI TNKIYENTTT IKEYLIAEGL PDVDISTTGV 

       190        200        210        220        230        240 
SSFEGPKGKF DVDVFDSTSD YLKLLKSIFD FPAIQKLLSS PKFSFCYDAL HGVAGVHAKR 

       250        260        270        280        290        300 
IFVEELGANE SSLVNCVPKE DFGGGHPDPN LTYAKELVAR MGLSKTHSEP NPPEFGAAAD 

       310        320        330        340        350        360 
GDGDRNMVLG KRFFVTPSDS VAIIAANAVQ AIPYFSGGLK GVARSMPTSA ALDIVAKHLN 

       370        380        390        400        410        420 
LKFFEVPTGW KFFGNLMDAG MCSICGEESF GTGSDHIREK DGIWAVLAWL SILAYKNKDN 

       430        440        450        460        470        480 
LGEGNLVSVE DIVRQHWAIY GRHYYTRYDY ENVNADGAKD LMAHLVKLQS SIDEVNKLIK 

       490        500        510        520        530        540 
GIRSDVSNVV HADEFEYKDP VDGSVSKHQG IRYLFEDGSR LVFRLSGTGS EGATIRLYIE 

       550        560        570        580 
QYEKDSSKIG RDSQEALAPL VEVALKLSKM QEYTSRSAPT VIT 

« Hide

References

[1]Tauberger E.
Thesis (1999), Freie Universitaet Berlin, Germany
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Tuber.

Cross-references

Sequence databases

AJ240054 mRNA. Translation: CAB93681.1.

3D structure databases

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

Enzyme and pathway databases

BRENDA5.4.2.2. 296.

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. 3 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 namePGMC_SOLTU
AccessionPrimary (citable) accession number: Q9M4G4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectPPAP (Plant Proteome Annotation Project)

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