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B1VEZ9 (GLMM_CORU7) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 30. 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:cu0378
OrganismCorynebacterium urealyticum (strain ATCC 43042 / DSM 7109) [Complete proteome] [HAMAP]
Taxonomic identifier504474 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length446 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 – 446446Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000201079

Sites

Active site1031Phosphoserine intermediate By similarity
Metal binding1031Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1031Phosphoserine By similarity

Sequences

Sequence LengthMass (Da)Tools
B1VEZ9 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 343B22B6119FA4A8

FASTA44646,797
        10         20         30         40         50         60 
MGRLFGTDGV RGLANEKLTA PLAMRLGAAA ARVLTEKKST DRRPTAIIGR DPRVSGEMLT 

        70         80         90        100        110        120 
AALSAGLASQ GVDVLDVGVL PTPAVAFLTD DYGSDMGVMV SASHNPMPDN GIKFFAIGGR 

       130        140        150        160        170        180 
KLEDWIEDEI EQEMGKLPEE GPTGAAIGRV FDQSHSALDR YLHHLQQAVH TRLDGIKVVV 

       190        200        210        220        230        240 
DCAHGAAYQA APMAYEAAGA EVVAVSNKPN GYNINDGVGS THIDQLQKAV VEHGADLGLA 

       250        260        270        280        290        300 
HDGDADRCLA VDAQGNVVDG DQIMAVLALS MKDGGELKRN TLVATVMSNL GLKLAMERNG 

       310        320        330        340        350        360 
ITLRQTQVGD RYVVEDLRAG DYSLGGEQSG HIVIPEHGTT GDGLLTGLFL MARMATTGKT 

       370        380        390        400        410        420 
LAELASAMQV LPQTLINVPV SNKAAIAGDA RVKQAIAKAE EELGETGRVL LRPSGTEELF 

       430        440 
RVMVEAADSA TARKIAGQLA AVVAEV 

« Hide

References

[1]"The lifestyle of Corynebacterium urealyticum derived from its complete genome sequence established by pyrosequencing."
Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A., Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S., Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B., Soriano F., Droege M., Puehler A.
J. Biotechnol. 136:11-21(2008) [PubMed: 18367281] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43042 / DSM 7109.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM942444 Genomic DNA. Translation: CAQ04338.1.
RefSeqYP_001799772.1. NC_010545.1.

3D structure databases

ProteinModelPortalB1VEZ9.
ModBaseSearch...

Protein-protein interaction databases

STRINGB1VEZ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6186043.
GenomeReviewsGene locus cu0378 in contig AM942444_GR.
KEGGcur:cur_0378.
PATRIC21520468. VBICorUre58120_0377.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG644964.
OMAGVGSTHL.
ProtClustDBPRK14318.

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_CORU7
AccessionPrimary (citable) accession number: B1VEZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: January 25, 2012
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