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B2UYH3 (GLMM_CLOBA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 28. 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:CLH_0300
OrganismClostridium botulinum (strain Alaska E43 / Type E3) [Complete proteome] [HAMAP]
Taxonomic identifier508767 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

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_1000201075

Sites

Active site1001Phosphoserine intermediate By similarity
Metal binding1001Magnesium; via phosphate group By similarity
Metal binding2401Magnesium By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity

Amino acid modifications

Modified residue1001Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B2UYH3 [UniParc].

Last modified July 1, 2008. Version 1.
Checksum: BDB2F0308E1CDA9F

FASTA44748,409
        10         20         30         40         50         60 
MDRMFGTDGV RGIANTELTA QMAYNLGRAG AYVLTEGAHK PKILVAKDTR ISGDMLESAL 

        70         80         90        100        110        120 
VAGILSVGAE AVILGVVPTP AVAYLTREYN ADAGVMISAS HNPVEYNGIK FFNNKGYKLS 

       130        140        150        160        170        180 
DELEDGIQKV IESDFEGVPS PIGIDLGRER IEVAALEDYT EFAKQTIPYN LKGMKIALDC 

       190        200        210        220        230        240 
ANGASYKSAV KAFRDLGADV FVINDNPDGT NINKNCGSTH PEELMDYVVK KGCDLGFAFD 

       250        260        270        280        290        300 
GDADRCLAVD ENGKLINGDF ILMLCANYLK EIGKLKDDTL VVTVMSNLGL DIACRGLGIK 

       310        320        330        340        350        360 
LEKTKVGDRY VLEEMTKDNY VLGGEQSGHV IFLDYNTTGD GLVTALQVAS IVKKKEKTLS 

       370        380        390        400        410        420 
ELCSVMKELP QVLVNATVPN DKKNIYLEDA EIVEAIKEIE AKLNGVGRVL IRPSGTEPLV 

       430        440 
RVMLEGENQV EIDEMAHGLA NLILSKI 

« Hide

References

[1]"Complete genome sequence of Clostridium botulinum E3 str. Alaska E43."
Brinkac L.M., Brown J.L., Bruce D., Detter C., Munk C., Smith L.A., Smith T.J., Sutton G., Brettin T.S.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Alaska E43 / Type E3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001078 Genomic DNA. Translation: ACD52376.1.
RefSeqYP_001919735.1. NC_010723.1.

3D structure databases

ProteinModelPortalB2UYH3.
ModBaseSearch...

Protein-protein interaction databases

STRINGB2UYH3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6319707.
GenomeReviewsGene locus CLH_0300 in contig CP001078_GR.
KEGGcbt:CLH_0300.
PATRIC19416870. VBICloBot115804_0266.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMALGLDIAC.
ProtClustDBPRK14316.

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_CLOBA
AccessionPrimary (citable) accession number: B2UYH3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 1, 2008
Last modified: January 25, 2012
This is version 28 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