Q5M3V8 (GLMM_STRT2) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 57.
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 | Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 264199 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Lactobacillales › Streptococcaceae › Streptococcus › ![]() |
Protein attributes
| Sequence length | 450 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. HAMAP-Rule MF_01554 |
| Catalytic activity | Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP-Rule MF_01554 |
| Cofactor | Binds 1 magnesium ion per subunit By similarity. |
| Post-translational modification | Activated by phosphorylation By similarity. |
| 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: HAMAP phosphoglucosamine mutase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 450 | 450 | Phosphoglucosamine mutase HAMAP-Rule MF_01554 | PRO_0000147980 | |||||
Sites | |||||||||
| Active site | 101 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 101 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 240 | 1 | Magnesium By similarity | ||||||
| Metal binding | 242 | 1 | Magnesium By similarity | ||||||
| Metal binding | 244 | 1 | Magnesium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 101 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence and comparative genome analysis of the dairy bacterium Streptococcus thermophilus." Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D., Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D., Hancy F. Hols P.Nat. Biotechnol. 22:1554-1558(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-250 / LMG 18311. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000023 Genomic DNA. Translation: AAV60885.1. |
| RefSeq | YP_139700.1. NC_006448.1. |
3D structure databases | |
| ProteinModelPortal | Q5M3V8. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 264199.stu1251. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAV60885; AAV60885; stu1251. |
| GeneID | 3165474. |
| KEGG | stl:stu1251. |
| PATRIC | 19804065. VBIStrThe97850_1234. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1109. |
| HOGENOM | HOG000268678. |
| KO | K03431. |
| OMA | TLMSNMS. |
| ProtClustDB | PRK14316. |
Family and domain databases | |
| Gene3D | 3.40.120.10. 3 hits. |
| HAMAP | MF_01554_B. GlmM_B. |
| 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] |
| 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_STRT2 | ||||||||
| Accession | Primary (citable) accession number: Q5M3V8 | ||||||||
| 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
