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Q49ZA7 (GLMM_STAS1) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:SSP0724
OrganismStaphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP]
Taxonomic identifier342451 [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_0000147968

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
Q49ZA7 [UniParc].

Last modified September 13, 2005. Version 1.
Checksum: 3FBCE030614CB100

FASTA45149,182
        10         20         30         40         50         60 
MAKYFGTDGV RGVANKELTP ELAFKLGRYG GYVLAHNEGE KHPKVLVGRD TRVSGEMLES 

        70         80         90        100        110        120 
ALIAGLISIG AEVMRLGVIS TPGVAYLTRE MEADLGVMIS ASHNPVPDNG IKFFGSDGFK 

       130        140        150        160        170        180 
LSDDQEQEIE HLLDQDNPDL PRPVGEDIVH YSDYFEGAQK YISYLKSTVD VDLAGMKIAL 

       190        200        210        220        230        240 
DGAHGSTSSL APFLFGDLEA DTVTIGCNPN GYNINQEVGS THPESLAKVV VESECDFGLA 

       250        260        270        280        290        300 
FDGDGDRLIA IDEKGNIVDG DQIMFIIGQA MSKNQELNNN MIVSTVMSNL GFYKALENEG 

       310        320        330        340        350        360 
IQSNKTKVGD RYVVEEMRRG NYNLGGEQSG HIVLMDYNTT GDGLLTGVQL ASIIKMTGKS 

       370        380        390        400        410        420 
LSQLTSQMKK YPQSLVNVRV TDKYRVEENI DVQEIMTKVE VEMNGEGRIL VRPSGTEPLV 

       430        440        450 
RVMVEAATDE DAQRYANTIA EVVQDKMGLD N 

« Hide

References

[1]"Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection."
Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.
Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed: 16135568] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15305 / DSM 20229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP008934 Genomic DNA. Translation: BAE17869.1.
RefSeqYP_300814.1. NC_007350.1.

3D structure databases

ProteinModelPortalQ49ZA7.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ49ZA7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000047604; EBSTAP00000045973; EBSTAG00000047601.
GeneID3615925.
GenomeReviewsGene locus SSP0724 in contig AP008934_GR.
KEGGssp:SSP0724.
NMPDRfig|342451.4.peg.1137.
PATRIC19622950. VBIStaSap90642_0726.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1109.
GeneTreeEBGT00050000024615.
HOGENOMHBG644964.
OMAGVGSTHL.
PhylomeDBQ49ZA7.
ProtClustDBPRK14316.

Enzyme and pathway databases

BioCycSSAP342451:SSP0724-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_STAS1
AccessionPrimary (citable) accession number: Q49ZA7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: September 13, 2005
Last modified: January 25, 2012
This is version 44 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