Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q5HE43 (GLMM_STAAC)

Last modified November 3, 2009. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10
Gene names
Name: glmM
Synonyms: femD
Ordered Locus Names: SACOL2151
OrganismStaphylococcus aureus (strain COL) [Complete proteome] [HAMAP]
Taxonomic identifier93062 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Hide | Top

Protein attributes

Sequence length451 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

Hide | Top

General annotation (Comments)

Function

Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. HAMAP MF_01554

Catalytic activity

Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. Ref.3

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Post-translational modification

Activated by phosphorylation. Can autophosphorylate in vitro using ATP. HAMAP MF_01554

Miscellaneous

Disruption of glmM results in a drastically reduced methicillin resistance. HAMAP MF_01554

Sequence similarities

Belongs to the phosphohexose mutase family.

Hide | Top

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-KW

phosphoglucosamine mutase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 451451Phosphoglucosamine mutase HAMAP MF_01554
PRO_0000147959

Sites

Active site1021Phosphoserine intermediate By similarity
Metal binding1021Magnesium; via phosphate group By similarity
Metal binding2421Magnesium By similarity
Metal binding2441Magnesium By similarity
Metal binding2461Magnesium By similarity

Amino acid modifications

Modified residue1021Phosphoserine; by autocatalysis Probable

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q5HE43-1 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: A164B280C4B9ABD8

FASTA45149,266
        10         20         30         40         50         60 
MGKYFGTDGV RGVANQELTP ELAFKLGRYG GYVLAHNKGE KHPRVLVGRD TRVSGEMLES 

        70         80         90        100        110        120 
ALIAGLISIG AEVMRLGIIS TPGVAYLTRD MGAELGVMIS ASHNPVADNG IKFFGSDGFK 

       130        140        150        160        170        180 
LSDEQENEIE ALLDQENPEL PRPVGNDIVH YSDYFEGAQK YLSYLKSTVD VNFEGLKIAL 

       190        200        210        220        230        240 
DGANGSTSSL APFLFGDLEA DTETIGCSPD GYNINEKCGS THPEKLAEKV VETESDFGLA 

       250        260        270        280        290        300 
FDGDGDRIIA VDENGQIVDG DQIMFIIGQE MHKNQELNND MIVSTVMSNL GFYKALEQEG 

       310        320        330        340        350        360 
IKSNKTKVGD RYVVEEMRRG NYNLGGEQSG HIVMMDYNTT GDGLLTGIQL ASVIKMTGKS 

       370        380        390        400        410        420 
LSELAGQMKK YPQSLINVRV TDKYRVEENV DVKEVMTKVE VEMNGEGRIL VRPSGTEPLV 

       430        440        450 
RVMVEAATDE DAERFAQQIA DVVQDKMGLD K

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"A phosphoglucomutase-like gene essential for the optimal expression of methicillin resistance in Staphylococcus aureus: molecular cloning and DNA sequencing."
Wu S., de Lencastre H., Sali A., Tomasz A.
Microb. Drug Resist. 2:277-286(1996) [PubMed: 9158773] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain."
Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. expand/collapse author list , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M.
J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase."
Jolly L., Wu S.W., Van Heijenoort J., de Lencastre H., Mengin-Lecreulx D., Tomasz A.
J. Bacteriol. 179:5321-5325(1997) [PubMed: 9286983] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[4]"Autophosphorylation of phosphoglucosamine mutase from Escherichia coli."
Jolly L., Pompeo F., van Heijenoort J., Fassy F., Mengin-Lecreulx D.
J. Bacteriol. 182:1280-1285(2000) [PubMed: 10671448] [Abstract]
Cited for: AUTOPHOSPHORYLATION AT A SERINE RESIDUE.

Hide | Top

Cross-references

Sequence databases

Y09927 Genomic DNA. Translation: CAA71060.2.
CP000046 Genomic DNA. Translation: AAW38459.1.
RefSeqYP_186964.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5HE43.

Genome annotation databases

GeneID3237428.
GenomeReviewsGene locus SACOL2151 in contig CP000046_GR.
KEGGsac:SACOL2151.
TIGRSACOL2151.

Phylogenomic databases

HOGENOMQ5HE43.
OMASTHPEAM.

Enzyme and pathway databases

BioCycSAUR93062:SACOL2151-MON.

Family and domain databases

HAMAPMF_01554.
[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. A-D-PHexomutase_N.
IPR006352. GlmM.
[Graphical view]
Gene3DG3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
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.
TIGRFAMsTIGR01455. glmM. 1 hit.
PROSITEPS00710. PGM_PMM. 1 hit.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameGLMM_STAAC
AccessionPrimary (citable) accession number: Q5HE43
Secondary accession number(s): P95685, P95710
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: February 15, 2005
Last modified: November 3, 2009
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents