O34824 (GLMM_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 72.
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 subtilis | ||||||
| Taxonomic identifier | 1423 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus |
Protein attributes
| Sequence length | 448 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 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 Reference proteome |
| Gene Ontology (GO) | |
| Biological process | UDP-N-acetylglucosamine biosynthetic process Inferred from Biological aspect of Ancestor. Source: RefGenome glucose 1-phosphate metabolic processInferred from Biological aspect of Ancestor. Source: RefGenome |
| Cellular component | cytosol Inferred from Biological aspect of Ancestor. Source: RefGenome |
| Molecular function | magnesium ion binding Inferred from electronic annotation. Source: InterPro phosphoglucomutase activityInferred from Biological aspect of Ancestor. Source: RefGenome phosphoglucosamine mutase activityInferred from Biological aspect of Ancestor. Source: RefGenome |
| 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_0000147846 | |||||
Sites | |||||||||
| Active site | 100 | 1 | Phosphoserine intermediate | ||||||
| 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
| ||||||||||||||||||
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. Strain: 168. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB006424 Genomic DNA. Translation: BAA33070.1. AL009126 Genomic DNA. Translation: CAB11953.1. |
| PIR | B69745. |
| RefSeq | NP_388058.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | O34824. |
| SMR | O34824. Positions 3-445. |
| ModBase | Search... |
PTM databases | |
| PhosSite | O34824. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBBACT00000001567; EBBACP00000001567; EBBACG00000001565. |
| GeneID | 938632. |
| GenomeReviews | Gene locus BSU01770 in contig AL009126_GR. |
| KEGG | bsu:BSU01770. |
| NMPDR | fig|224308.1.peg.177. |
| PATRIC | 18971907. VBIBacSub10457_0182. |
Organism-specific databases | |
| GenoList | BSU01770. [Micado] |
Phylogenomic databases | |
| GeneTree | EBGT00070000032132. |
| HOGENOM | HBG644964. |
| OMA | PLEDIQV. |
| PhylomeDB | O34824. |
| ProtClustDB | PRK14316. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU01770-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_BACSU | ||||||||
| Accession | Primary (citable) accession number: O34824 Secondary accession number(s): O87090 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
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