Q5HE43 (GLMM_STAAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 48.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Phosphoglucosamine mutase EC=5.4.2.10 | ||||||
| Gene names |
| ||||||
| Organism | Staphylococcus aureus (strain COL) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 93062 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Staphylococcus |
Protein attributes
| Sequence length | 451 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate. HAMAP MF_01554_B |
| Catalytic activity | Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. Ref.3 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. HAMAP MF_01554_B |
| Post-translational modification | Activated by phosphorylation. Can autophosphorylate in vitro using ATP. HAMAP MF_01554_B |
| Miscellaneous | Disruption of glmM results in a drastically reduced methicillin resistance. HAMAP MF_01554_B |
| Sequence similarities | Belongs to the phosphohexose mutase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding |
| Molecular function | Isomerase |
| PTM | Phosphoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucosamine mutase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 451 | 451 | Phosphoglucosamine mutase HAMAP MF_01554_B | PRO_0000147959 | |||||
Sites | |||||||||
| Active site | 102 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 102 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 242 | 1 | Magnesium By similarity | ||||||
| Metal binding | 244 | 1 | Magnesium By similarity | ||||||
| Metal binding | 246 | 1 | Magnesium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 102 | 1 | Phosphoserine; by autocatalysis Probable | ||||||
Sequences
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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. Fraser C.M.J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: COL. |
| [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. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y09927 Genomic DNA. Translation: CAA71060.2. CP000046 Genomic DNA. Translation: AAW38459.1. |
| RefSeq | YP_186964.1. NC_002951.2. |
3D structure databases | |
| ProteinModelPortal | Q5HE43. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q5HE43. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBSTAT00000008694; EBSTAP00000008429; EBSTAG00000008693. |
| GeneID | 3237428. |
| GenomeReviews | Gene locus SACOL2151 in contig CP000046_GR. |
| KEGG | sac:SACOL2151. |
| PATRIC | 19530567. VBIStaAur112458_2095. |
| TIGR | SACOL2151. |
Phylogenomic databases | |
| eggNOG | COG1109. |
| GeneTree | EBGT00050000024615. |
| HOGENOM | HBG644964. |
| OMA | PLEDIQV. |
| PhylomeDB | Q5HE43. |
| ProtClustDB | PRK14316. |
Enzyme and pathway databases | |
| BioCyc | SAUR93062:SACOL2151-MONOMER. |
Family and domain databases | |
| HAMAP | MF_01554_B. GlmM_B. [Tree] |
| InterPro | IPR005844. 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] |
| Gene3D | G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| KO | K03431. |
| Pfam | PF02878. 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] |
| PRINTS | PR00509. PGMPMM. |
| SUPFAM | SSF53738. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| TIGRFAMs | TIGR01455. GlmM. 1 hit. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLMM_STAAC | ||||||||
| Accession | Primary (citable) accession number: Q5HE43 Secondary accession number(s): P95685, P95710 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with