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Q24NW7 (GLMM_DESHY) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:DSY4486
OrganismDesulfitobacterium hafniense (strain Y51) [Complete proteome] [HAMAP]
Taxonomic identifier138119 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesPeptococcaceaeDesulfitobacterium

Protein attributes

Sequence length445 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: UniProtKB-HAMAP

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 445445Phosphoglucosamine mutase HAMAP-Rule MF_01554
PRO_0000305637

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2391Magnesium By similarity
Metal binding2411Magnesium By similarity
Metal binding2431Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q24NW7 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: 3B731F6341DA9396

FASTA44547,887
        10         20         30         40         50         60 
MGKLFGTDGV RGVANKELTP DLAFRLGQAG AYVLSKEHPH PRIVIGKDTR ISGDMLEAAL 

        70         80         90        100        110        120 
IAGICSVGAD VLRVGVLPTP GIAYLTRTLK ASAGVVISAS HNPVQDNGIK FFSSTGYKLP 

       130        140        150        160        170        180 
DAVEEEIEDL VHSHEKPWAI PVGSEIGRVI EIQDAQRRYM DFLKGTVGSL AGIKVVYDGS 

       190        200        210        220        230        240 
NGAASHVGPQ VLRELGVEVI PLSVTPDGIN INAGCGSTHP EVLQQAVIEH KADLGLANDG 

       250        260        270        280        290        300 
DADRLIAVDE NGEIVDGDFI MVICALALKA KGQLMEDSVV VTVMSNLGLH IALKEAGIRV 

       310        320        330        340        350        360 
YETQVGDRYV MEELLKTGAR LGGEQSGHII FLDHNTTGDG LLTALQLLAV LKEQGKPISK 

       370        380        390        400        410        420 
LAAKMQRLPQ VLINVRVKDK KKAMENPYVF QKVEEVKRFL GERGRVLVRS SGTESLVRVM 

       430        440 
VEGQDHEQLM GLAQSVVDII KREEL 

« Hide

References

[1]"Complete genome sequence of the dehalorespiring bacterium Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides ethenogenes 195."
Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K., Inatomi K., Furukawa K., Inui M., Yukawa H.
J. Bacteriol. 188:2262-2274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Y51.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008230 Genomic DNA. Translation: BAE86275.1.
RefSeqYP_520719.1. NC_007907.1.

3D structure databases

ProteinModelPortalQ24NW7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING138119.DSY4486.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAE86275; BAE86275; DSY4486.
GeneID3957441.
KEGGdsy:DSY4486.
PATRIC21678150. VBIDesHaf65307_5004.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
HOGENOMHOG000268678.
KOK03431.
OMAHTTGDGI.
OrthoDBEOG6TN467.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycDHAF138119:GHT5-4560-MONOMER.

Family and domain databases

Gene3D3.30.310.50. 1 hit.
3.40.120.10. 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. SSF53738. 3 hits.
SSF55957. SSF55957. 1 hit.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_DESHY
AccessionPrimary (citable) accession number: Q24NW7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 2, 2007
Last sequence update: April 18, 2006
Last modified: April 16, 2014
This is version 56 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