Skip Header

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

C1CWA3 (GLMM_DEIDV) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 30. 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:Deide_15140
OrganismDeinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923) [Complete proteome] [HAMAP]
Taxonomic identifier546414 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus

Protein attributes

Sequence length442 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.

Post-translational modification

Activated by phosphorylation By similarity.

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 – 442442Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_1000215484

Sites

Active site1031Phosphoserine intermediate By similarity
Metal binding1031Magnesium; via phosphate group By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity

Amino acid modifications

Modified residue1031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
C1CWA3 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: CEADCDF0536D1C0C

FASTA44247,197
        10         20         30         40         50         60 
MSERKYFGTD GVRAVAGEFP LTSAWVMSLG AAAGEVLRRV NPHARVVIGK DTRQSGDMLE 

        70         80         90        100        110        120 
AALAAGLTSR GVTVIHVGVL PTPGVSYLTR HLKADAGVVI SASHNPYEDN GIKFFGADGQ 

       130        140        150        160        170        180 
KLSDATELQI EAAIDEVPGF APLTGTAMGS VTNYTEAEHL YTDFLKSHAP DLSGLKIALD 

       190        200        210        220        230        240 
CANGAAYRVA PKVFQAAGAD VFAIYTTPDG RNINRGCGST HMDHLRQIVR EGEYDLGVAF 

       250        260        270        280        290        300 
DGDADRALFV DSRGQVVHGD HMLLLNARAR GEQAVVATIM TNMALEAKLQ DAGIPLERTA 

       310        320        330        340        350        360 
VGDRYVHERL HEKGLSLGGE QSGHVLFLDI SPTGDGVLTA LLTLASMKKL GTTLDALHDD 

       370        380        390        400        410        420 
LVMYPQTLVN VRVQDKKAIA VDQQVQQAVR QAEEQLLGRG RVNLRPSGTE NLIRVMVEGQ 

       430        440 
DAAEIHEVAR VLAGVVEARG QA 

« Hide

References

[1]"Alliance of proteomics and genomics to unravel the specificities of Sahara bacterium Deinococcus deserti."
de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B., Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M., Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.
PLoS Genet. 5:E1000434-E1000434(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VCD115 / DSM 17065 / LMG 22923.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001114 Genomic DNA. Translation: ACO46470.1.
RefSeqYP_002786224.1. NC_012526.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING546414.Deide_15140.

Proteomic databases

PaxDbC1CWA3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACO46470; ACO46470; Deide_15140.
GeneID7738150.
KEGGddr:Deide_15140.
PATRIC21616924. VBIDeiDes121019_1741.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMATLMSNMS.
ProtClustDBPRK14323.

Enzyme and pathway databases

BioCycDDES546414:GHOM-2586-MONOMER.

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_DEIDV
AccessionPrimary (citable) accession number: C1CWA3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 26, 2009
Last modified: May 1, 2013
This is version 30 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