Reviewed,
UniProtKB/Swiss-Prot O34824 (GLMM_BACSU)
Last modified
November 3, 2009.
Version 52.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Phosphoglucosamine mutase EC=5.4.2.10 | ||||||
| Gene names |
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| Organism | Bacillus subtilis [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 448 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity. |
| Catalytic activity | Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP 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: UniProtKB-KW 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 – 448 | 448 | Phosphoglucosamine mutase HAMAP MF_01554 | PRO_0000147846 | |||||
Sites | |||||||||
| Active site | 100 | 1 | Phosphoserine intermediate HAMAP MF_01554 | ||||||
| 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 | ||||||
Experimental info | |||||||||
| Sequence conflict | 7 | 1 | T → K in BAA33070. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Sequence analysis of the 70kb region between 17 and 23 degree of the Bacillus subtilis chromosome." Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H. Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| [3] | "The serine/threonine/tyrosine phosphoproteome of the model bacterium Bacillus subtilis." Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R., Mann M. Mol. Cell. Proteomics 6:697-707(2007) [PubMed: 17218307] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-100, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| AB006424 Genomic DNA. Translation: BAA33070.1. AL009126 Genomic DNA. Translation: CAB11953.1. | |
| PIR | B69745. |
| RefSeq | NP_388058.1. |
3D structure databases | |
| ModBase | Search... |
PTM databases | |
| PhosSite | O34824. |
Genome annotation databases | |
| GeneID | 938632. |
| GenomeReviews | Gene locus BSU01770 in contig AL009126_GR. |
| KEGG | bsu:BSU01770. |
| NMPDR | fig|224308.1.peg.177. |
Organism-specific databases | |
| SubtiList | BG12704. glmM. [Micado] |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O34824. |
| OMA | STHPEAM. |
Enzyme and pathway databases | |
| BioCyc | BSUB224308:BSU0177-MON. |
| BRENDA | 5.4.2.10. 150. |
Family and domain databases | |
| HAMAP | MF_01554. [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. A-D-PHexomutase_N. IPR006352. GlmM. [Graphical view] |
| Gene3D | G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits. |
| 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. |
| TIGRFAMs | TIGR01455. glmM. 1 hit. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLMM_BACSU | ||||||||
| Accession | Primary (citable) accession number: O34824 Secondary accession number(s): O87090 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with


