B2HCZ2 (GLMM_MYCMM) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 26.
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 | Mycobacterium marinum (strain ATCC BAA-535 / M) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 216594 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
Protein attributes
| Sequence length | 445 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 – 445 | 445 | Phosphoglucosamine mutase HAMAP MF_01554_B | PRO_1000201120 | |||||
Sites | |||||||||
| Active site | 102 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 102 | 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 | 102 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "Insights from the complete genome sequence of Mycobacterium marinum on the evolution of Mycobacterium tuberculosis." Stinear T.P., Seemann T., Harrison P.F., Jenkin G.A., Davies J.K., Johnson P.D., Abdellah Z., Arrowsmith C., Chillingworth T., Churcher C., Clarke K., Cronin A., Davis P., Goodhead I., Holroyd N., Jagels K., Lord A., Moule S. Cole S.T.Genome Res. 18:729-741(2008) [PubMed: 18403782] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-535 / M. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000854 Genomic DNA. Translation: ACC39564.1. |
| RefSeq | YP_001849419.1. NC_010612.1. |
3D structure databases | |
| ProteinModelPortal | B2HCZ2. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B2HCZ2. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000032428; EBMYCP00000030868; EBMYCG00000032423. |
| GeneID | 6225361. |
| GenomeReviews | Gene locus MMAR_1108 in contig CP000854_GR. |
| KEGG | mmi:MMAR_1108. |
| PATRIC | 18062987. VBIMycMar75906_1182. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000015909. |
| HOGENOM | HBG644964. |
| OMA | GVGSTHL. |
| ProtClustDB | PRK14318. |
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_MYCMM | ||||||||
| Accession | Primary (citable) accession number: B2HCZ2 | ||||||||
| 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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