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A7X524 (GLMM_STAA1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 33. 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:SAHV_2145
OrganismStaphylococcus aureus (strain Mu3 / ATCC 700698) [Complete proteome] [HAMAP]
Taxonomic identifier418127 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesStaphylococcus

Protein attributes

Sequence length451 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 – 451451Phosphoglucosamine mutase HAMAP MF_01554_B
PRO_1000068918

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 similarity

Sequences

Sequence LengthMass (Da)Tools
A7X524 [UniParc].

Last modified October 23, 2007. Version 1.
Checksum: A7330C90CA7F9CD8

FASTA45149,294
        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 VNFEGLKIVL 

       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

References

[1]"Mutated response regulator graR is responsible for phenotypic conversion of Staphylococcus aureus from heterogeneous vancomycin-intermediate resistance to vancomycin-intermediate resistance."
Neoh H.-M., Cui L., Yuzawa H., Takeuchi F., Matsuo M., Hiramatsu K.
Antimicrob. Agents Chemother. 52:45-53(2008) [PubMed: 17954695] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Mu3 / ATCC 700698.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009324 Genomic DNA. Translation: BAF79028.1.
RefSeqYP_001442735.1. NC_009782.1.

3D structure databases

ProteinModelPortalA7X524.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7X524.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000003068; EBSTAP00000002967; EBSTAG00000003068.
GeneID5560837.
GenomeReviewsGene locus SAHV_2145 in contig AP009324_GR.
KEGGsaw:SAHV_2145.
PATRIC19559456. VBIStaAur127830_2203.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00050000024615.
HOGENOMHBG644964.
OMAPLEDIQV.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycSAUR418127:SAHV_2145-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_STAA1
AccessionPrimary (citable) accession number: A7X524
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 23, 2007
Last modified: January 25, 2012
This is version 33 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