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Reviewed, UniProtKB/Swiss-Prot P38569 (PGM_ACEXY)

Last modified June 16, 2009. Version 53. 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: celB
OrganismAcetobacter xylinus (Gluconacetobacter xylinus)
Taxonomic identifier28448 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhodospirillalesAcetobacteraceaeGluconacetobacter

Protein attributes

Sequence length555 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred 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 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 – 555555Phosphoglucomutase
PRO_0000147807

Sites

Active site1481Phosphoserine intermediate By similarity
Metal binding1481Magnesium; via phosphate group By similarity
Metal binding3061Magnesium By similarity
Metal binding3081Magnesium By similarity
Metal binding3101Magnesium By similarity

Sequences

Sequence LengthMass (Da)Tools
P38569-1 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: C67D1475AD4A9E8D

FASTA55559,634
        10         20         30         40         50         60 
MPSISPFAGK PVDPDRLVNI DALLDAYYTR KPDPAIATQR VAFGTSGHRG SSLTTSFNEN 

        70         80         90        100        110        120 
HILSISQAIA DYRKGAGITG PLFIGIDTHA LSRPALKSAL EVFAANGVEV RIDAQDGYTP 

       130        140        150        160        170        180 
TPVISHAILT YNRDRSSDLA DGVVITPSHN PPEDGGYKYN PPHGGPADTD ITKVVETAAN 

       190        200        210        220        230        240 
DYMAKKMEGV KRVSFEDALK APTTKRHDYI TPYVDDLAAV VDMDVIRESG VSIGIDPLGG 

       250        260        270        280        290        300 
AAVDYWQPII DKYGINATIV SKEVDPTFRF MTADWDGQIR MDCSSPYAMA RLVGMKDKFD 

       310        320        330        340        350        360 
IAFANDTDAD RHGIVSGKYG LMNPNHYLAV AIEYLFNNRE NWNASAGVGK TVVSSSMIDR 

       370        380        390        400        410        420 
VAKEIGRKLV EVPVGFKWFV DGLYNGTLGF GGEESAGASF LRRAGTVWST DKDGIILGLL 

       430        440        450        460        470        480 
AAEITARTKR TPGAAYEDMT RRLGTPYYAR IDAPADPEQK AILKNLSPEQ IGMTELAGEP 

       490        500        510        520        530        540 
ILSTLTNAPG NGAAIGGLKV SAKDGWFAAR PSGTENVYKI YAESFKSAAH LKAIQTEAQD 

       550 
AISALFAKAA QKNAG 

« Hide

References

[1]"Nucleotide sequence and expression analysis of the Acetobacter xylinum phosphoglucomutase gene."
Brautaset T., Standal R., Fjaervik E., Valla S.
Microbiology 140:1183-1188(1994) [PubMed: 8025683] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 23768 / NCIB 7029.

Cross-references

Sequence databases

L24077 Genomic DNA. Translation: AAA21561.1.
PIRI39487.

3D structure databases

ModBaseSearch...

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.
IPR005852. PGlcMutase_a-D-Glc-sp.
[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]
TIGRFAMsTIGR01132. pgm. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePGM_ACEXY
AccessionPrimary (citable) accession number: P38569
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: June 16, 2009
This is version 53 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