Q73F50 (GLMM_BACC1) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 56.
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 | Bacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 222523 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 448 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 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 | |
|---|---|
| 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 – 448 | 448 | Phosphoglucosamine mutase HAMAP MF_01554_B | PRO_0000147840 | |||||
Sites | |||||||||
| Active site | 100 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 100 | 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 | 100 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1." Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D. Nucleic Acids Res. 32:977-988(2004) [PubMed: 14960714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 10987. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE017194 Genomic DNA. Translation: AAS39093.1. |
| RefSeq | NP_976485.1. NC_003909.8. |
3D structure databases | |
| ProteinModelPortal | Q73F50. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | Q73F50. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000027863; EBBACP00000027213; EBBACG00000027854. |
| GeneID | 2749790. |
| GenomeReviews | Gene locus BCE_0157 in contig AE017194_GR. |
| KEGG | bca:BCE_0157. |
| NMPDR | fig|222523.1.peg.157. |
| PATRIC | 18849158. VBIBacCer118379_0151. |
| TIGR | BCE_0157. |
Phylogenomic databases | |
| eggNOG | COG1109. |
| GeneTree | EBGT00070000032132. |
| HOGENOM | HBG644964. |
| OMA | PLEDIQV. |
| ProtClustDB | PRK14316. |
Enzyme and pathway databases | |
| BioCyc | BCER405917:BCE_0157-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_BACC1 | ||||||||
| Accession | Primary (citable) accession number: Q73F50 | ||||||||
| 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 |

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