Q6LYB4 (GLMM_METMP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 58.
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 |
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| Organism | Methanococcus maripaludis (strain S2 / LL) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 267377 [NCBI] | ||||
| Taxonomic lineage | Archaea › Euryarchaeota › Methanococci › Methanococcales › Methanococcaceae › Methanococcus › ![]() |
Protein attributes
| Sequence length | 447 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. Also catalyzes the isomerization of glucose-1-phosphate to glucose-6-phosphate, but at a 5-fold lower rate. Ref.2 |
| Catalytic activity | Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. Ref.2 |
| Cofactor | Binds 1 magnesium ion per subunit. Ref.2 |
| Subunit structure | Monomer. Also forms large aggregates. Ref.2 |
| Post-translational modification | Activated by phosphorylation. Glucose-1,6-bisphosphate or fructose-1,6-bisphosphate can activate the enzyme in vitro. However, since glucose-1,6-bisphosphate is not believed to form in methanogens, the physiologically relevant activator might be a serine kinase protein. HAMAP-Rule MF_01554_A |
| 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 – 447 | 447 | Phosphoglucosamine mutase HAMAP-Rule MF_01554_A | PRO_0000337813 | |||||
Sites | |||||||||
| Active site | 88 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 88 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 231 | 1 | Magnesium By similarity | ||||||
| Metal binding | 233 | 1 | Magnesium By similarity | ||||||
| Metal binding | 235 | 1 | Magnesium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 88 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete genome sequence of the genetically tractable hydrogenotrophic methanogen Methanococcus maripaludis." Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J., Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M., Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A., Moore B.C. Leigh J.A.J. Bacteriol. 186:6956-6969(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: S2 / LL. |
| [2] | "Acetamido sugar biosynthesis in the Euryarchaea." Namboori S.C., Graham D.E. J. Bacteriol. 190:2987-2996(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PTM, PH DEPENDENCE, SUBUNIT. Strain: 900. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX950229 Genomic DNA. Translation: CAF30633.1. |
| RefSeq | NP_988197.1. NC_005791.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1WQA based on UniProtKB O58651. |
| ProteinModelPortal | Q6LYB4. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 267377.MMP1077. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAF30633; CAF30633; MMP1077. |
| GeneID | 2762645. |
| KEGG | mmp:MMP1077. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1109. |
| HOGENOM | HOG000268680. |
| KO | K03431. |
| OMA | TWIHRDI. |
| ProtClustDB | CLSK2517686. |
Enzyme and pathway databases | |
| BioCyc | MMAR267377:GJ77-1108-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.120.10. 3 hits. |
| HAMAP | MF_01554_A. GlmM_A. |
| 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. IPR023666. GlmM_arc. IPR024086. GlmM_arc-related. [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 | TIGR03990. Arch_GlmM. 1 hit. |
| PROSITE | PS00710. PGM_PMM. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GLMM_METMP | ||||||||
| Accession | Primary (citable) accession number: Q6LYB4 | ||||||||
| 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
