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Q6NJ50 (GLMM_CORDI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 52. 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:DIP0563
OrganismCorynebacterium diphtheriae [Complete proteome] [HAMAP]
Taxonomic identifier1717 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

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_0000147877

Sites

Active site1041Phosphoserine intermediate By similarity
Metal binding1041Magnesium; via phosphate group By similarity
Metal binding2431Magnesium By similarity
Metal binding2451Magnesium By similarity
Metal binding2471Magnesium By similarity

Amino acid modifications

Modified residue1041Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6NJ50 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: AF2539AC21964956

FASTA44746,672
        10         20         30         40         50         60 
MTRLFGTDGV RGLANRKLTA LLALKLGAAA AEVLTKDNRS TSRRPVAVVG RDPRVSGEML 

        70         80         90        100        110        120 
AAALSAGMAS RGVDVLRVGV LPTPAVAYLT DFYGADMGVV ISASHNPMPD NGIKFFSKGG 

       130        140        150        160        170        180 
HKLPDSVEDE IEKVMETIPD GGPTGHGIGR VIEEAVDAQE TYLKHLKGAV PRSLEGITVV 

       190        200        210        220        230        240 
VDCANGAASE VAPLAYAAAG AKVIPIHNHP NAYNINDSCG STHIDQVQAA VLEHGADLGL 

       250        260        270        280        290        300 
AHDGDADRCL AVDAEGNVVD GDQIMAILAL AMKENGELHK STLVATVMSN LGLRLAMKEA 

       310        320        330        340        350        360 
GIELRTTKVG DRYVLEELNA GGFSLGGEQS GHIVLPDHGT TGDGTLTGLS LMSRMAETGL 

       370        380        390        400        410        420 
SLKVLASAMT VLPQVLINVP VSDKTIIQTH PDVVAAMERA SDELGEDGRV LLRPSGTEEL 

       430        440 
FRVMVEAPSK ETARRIAADL ASVVAKI 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX248355 Genomic DNA. Translation: CAE49075.1.
RefSeqNP_938939.1. NC_002935.2.

3D structure databases

ProteinModelPortalQ6NJ50.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2649509.
GenomeReviewsGene locus DIP0563 in contig BX248353_GR.
KEGGcdi:DIP0563.
NMPDRfig|257309.1.peg.530.
PATRIC21482293. VBICorDip47633_0547.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

Enzyme and pathway databases

BioCycCDIP257309:DIP0563-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. 3 hits.
TIGRFAMsTIGR01455. GlmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLMM_CORDI
AccessionPrimary (citable) accession number: Q6NJ50
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: July 5, 2004
Last modified: January 25, 2012
This is version 52 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