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B0RB78 (GLMM_CLAMS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:CMS0322
OrganismClavibacter michiganensis subsp. sepedonicus (strain ATCC 33113 / JCM 9667) [Complete proteome] [HAMAP]
Taxonomic identifier31964 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrobacteriaceaeClavibacter

Protein attributes

Sequence length449 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 – 449449Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000087760

Sites

Active site1051Phosphoserine intermediate By similarity
Metal binding1051Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1051Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B0RB78 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: C1A6EEE7F0A17900

FASTA44946,957
        10         20         30         40         50         60 
MPRLFGTDGV RGLANGETIT ADLALRLAQA AAHVLGQDAR DAGRRPVAVV ARDPRVSGEF 

        70         80         90        100        110        120 
IAAAVAAGLA SSGVDVFDAG VIPTPATAYL IADFDADFGV MISASHNPAP DNGIKFFAAG 

       130        140        150        160        170        180 
GRKLADELED RIEAQLSQPV LLPTGADVGR IRRFADAEDR YVLHLLGTLQ HRLDGIHVVL 

       190        200        210        220        230        240 
DCAHGAAAGI SPEVSTDAGA RVTVIGNDPD GMNINDRVGS THLDLLAEAV LGHGADVGIA 

       250        260        270        280        290        300 
YDGDADRCLA VDHTGAIIDG DQIMAVLALS MARRGLLVER TLVATVMSNL GLRIAMAEND 

       310        320        330        340        350        360 
ITVLQTRVGD RYVLEAMNEG GYSLGGEQSG HLVIAEHATT GDGILTGIQL LGEMAATGRS 

       370        380        390        400        410        420 
LHELASVMTV YPQVMINVRG VDRERVSDDA ELNAAVARAE AELGDTGRIL MRASGTEPMI 

       430        440 
RVMVEAADQA TAERHAQELA ALVTERLAI 

« Hide

References

[1]"Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. sepedonicus suggests recent niche adaptation."
Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., Parkhill J., Ishimaru C.A.
J. Bacteriol. 190:2150-2160(2008) [PubMed: 18192393] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 33113 / JCM 9667.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM849034 Genomic DNA. Translation: CAQ00443.1.
RefSeqYP_001709104.1. NC_010407.1.

3D structure databases

ProteinModelPortalB0RB78.
ModBaseSearch...

Protein-protein interaction databases

STRINGB0RB78.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6156293.
GenomeReviewsGene locus CMS0322 in contig AM849034_GR.
KEGGcms:CMS_0322.
PATRIC21457618. VBIClaMic4666_0382.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycCMIC31964:CMS0322-MONOMER.

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. 2 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CLAMS
AccessionPrimary (citable) accession number: B0RB78
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: April 8, 2008
Last modified: January 25, 2012
This is version 27 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