Skip Header

Contribute Send feedback
Read comments (?) or add your own

B3R1R9 (GLMM_CUPTR) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 26. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:RALTA_A1976
OrganismCupriavidus taiwanensis (strain R1 / LMG 19424) (Ralstonia taiwanensis (strain LMG 19424)) [Complete proteome] [HAMAP]
Taxonomic identifier164546 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length447 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP MF_01554_B

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554_B

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B

Post-translational modification

Activated by phosphorylation By similarity. HAMAP MF_01554_B

Sequence similarities

Belongs to the phosphohexose mutase family.

Ontologies

Keywords
   LigandMagnesium
Metal-binding
   Molecular functionIsomerase
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcarbohydrate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 447447Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000201082

Sites

Active site1061Phosphoserine intermediate By similarity
Metal binding1061Magnesium; via phosphate group By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity

Amino acid modifications

Modified residue1061Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B3R1R9 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 55FC17433C43B0A2

FASTA44747,417
        10         20         30         40         50         60 
MTRKYFGTDG VRGKVGDAPI TPDFVMRLGH AAGKVLAHGA RTGQGKPTVL IGKDTRISGY 

        70         80         90        100        110        120 
MLEAALEAGF TSAGVHVLLT GPLPTPGIAY LTRALRLSAG VVISASHNPY YDNGIKFFSA 

       130        140        150        160        170        180 
SGDKLPDAVE AAIEAALDEP MVCAPSDDLG RARRIDDAAG RYIEFCKSTF PYEQDLHGLK 

       190        200        210        220        230        240 
LVVDCAHGAA YHIAPPVFHE LGADVVAIGN QPNGRNINAG YGATAPEKLI EAVKANGADL 

       250        260        270        280        290        300 
GLAFDGDADR LQVVDADGRL YNGDELLYLI VRDRQAAGQA VPGAVGTLMT NMAVELALKR 

       310        320        330        340        350        360 
EGVDFVRAKV GDRYVLEELN KRKWTLGGEG SGHLLCLDRH STGDGIVSAL QVLGALRRSG 

       370        380        390        400        410        420 
KTLAQLLDGV KLFPQTLINV RVQKGFDWQT HAGLQAARAA VEPELEGRGR VLIRASGTEP 

       430        440 
VVRVMVEAEQ AEMAERAARK LADALGA 

« Hide

References

[1]"Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and comparative genomics of rhizobia."
Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D., Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V., Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C., Masson-Boivin C.
Genome Res. 18:1472-1483(2008) [PubMed: 18490699] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: R1 / LMG 19424.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU633749 Genomic DNA. Translation: CAQ69917.1.
RefSeqYP_002005980.1. NC_010528.1.

3D structure databases

ProteinModelPortalB3R1R9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB3R1R9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6454934.
GenomeReviewsGene locus RALTA_A1976 in contig CU633749_GR.
KEGGcti:RALTA_A1976.
PATRIC21530574. VBICupTai42494_1937.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAPLEDIQV.
ProtClustDBPRK10887.

Family and domain databases

HAMAPMF_01554_B. GlmM_B.
[Tree]
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. Alpha-D-phosphohexomutase_SF.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
KOK03431.
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.
SUPFAMSSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CUPTR
AccessionPrimary (citable) accession number: B3R1R9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: September 2, 2008
Last modified: January 25, 2012
This is version 26 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families