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Q83NS5 (GLMM_TROW8) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Phosphoglucosamine mutase

EC=5.4.2.10
Gene names
Name:glmM
Ordered Locus Names:TW155
OrganismTropheryma whipplei (strain TW08/27) (Whipple's bacillus) [Complete proteome] [HAMAP]
Taxonomic identifier218496 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeTropheryma

Protein attributes

Sequence length453 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-Rule MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_01554

Post-translational modification

Activated by phosphorylation By similarity. HAMAP-Rule MF_01554

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: HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 453453Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000147994

Sites

Active site1101Phosphoserine intermediate By similarity
Metal binding1101Magnesium; via phosphate group By similarity
Metal binding2471Magnesium By similarity
Metal binding2491Magnesium By similarity
Metal binding2511Magnesium By similarity

Amino acid modifications

Modified residue1101Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q83NS5 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 220D71FD59A240BC

FASTA45348,455
        10         20         30         40         50         60 
MARLFGTDGI RALANGDLLT PELAMAVARA AAVVFTHGRV AKRRQVLGKR PVAIVARDPR 

        70         80         90        100        110        120 
ISGDFLVAAI SAGLASSGVD VLDAGVIPTP AVAFLVKNAN ADFGFMISAS HNPGYDNGVK 

       130        140        150        160        170        180 
IFAHGGVKLP DVVEDRIEYF LDKQKLSPIG SKVGRITRFV DAEDRYQMHL LSTLFTRIDG 

       190        200        210        220        230        240 
VKVVIDCANG AASGVSPDVF KSAGAAVKVI CADPNGVNIN DGVGSAYPER LRAEVIRNSA 

       250        260        270        280        290        300 
TLGLAFDGDA DRCIAVDSNG NTVDGDQIMA ILARSMQQRG TLRNKTLVTT IMSNIGLDRA 

       310        320        330        340        350        360 
MKKLGINLKR TQVGDRYVIE AMTQGGFNIG GEQSGHIILS DYSTAGDGIL AGLHLCAEII 

       370        380        390        400        410        420 
RTGKSLTDLA SIMEIVPQVT ANIETDDPTT LLNNKKIRHE ISRIEKSLKG RVVIRPSGTE 

       430        440        450 
PLIRIMVEDL NPEKAERACS HLADFFKQEI QKS 

« Hide

References

[1]"Sequencing and analysis of the genome of the Whipple's disease bacterium Tropheryma whipplei."
Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G., Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A., Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J., Relman D.A.
Lancet 361:637-644(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TW08/27.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX251410 Genomic DNA. Translation: CAD66835.1.
RefSeqNP_789098.1. NC_004551.1.

3D structure databases

ProteinModelPortalQ83NS5.
ModBaseSearch...

Protein-protein interaction databases

STRING218496.TW155.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAD66835; CAD66835; TW155.
GeneID1064450.
KEGGtws:TW155.
PATRIC23998701. VBITroWhi42739_0195.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK14318.

Family and domain databases

Gene3D3.40.120.10. 3 hits.
HAMAPMF_01554_B. GlmM_B.
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]
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. 2 hits.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_TROW8
AccessionPrimary (citable) accession number: Q83NS5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 60 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