Q6G5P7 (GLMM_BARHE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 47.
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 | Bartonella henselae (strain ATCC 49882 / Houston 1) (Rochalimaea henselae) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 283166 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bartonellaceae › Bartonella |
Protein attributes
| Sequence length | 459 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 – 459 | 459 | Phosphoglucosamine mutase HAMAP MF_01554_B | PRO_0000147848 | |||||
Sites | |||||||||
| Active site | 102 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 102 | 1 | Magnesium; via phosphate group By similarity | ||||||
| Metal binding | 243 | 1 | Magnesium By similarity | ||||||
| Metal binding | 245 | 1 | Magnesium By similarity | ||||||
| Metal binding | 247 | 1 | Magnesium By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 102 | 1 | Phosphoserine By similarity | ||||||
Sequences
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References
| [1] | "The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae." Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E. Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49882 / Houston 1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BX897699 Genomic DNA. Translation: CAF28237.1. |
| RefSeq | YP_034174.1. NC_005956.1. |
3D structure databases | |
| ProteinModelPortal | Q6G5P7. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2866034. |
| GenomeReviews | Gene locus BH14740 in contig BX897699_GR. |
| KEGG | bhe:BH14740. |
| NMPDR | fig|283166.1.peg.1302. |
| PATRIC | 20547160. VBIBarHen29080_1688. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HBG644964. |
| OMA | GVGSTHL. |
| PhylomeDB | Q6G5P7. |
| ProtClustDB | PRK10887. |
Enzyme and pathway databases | |
| BioCyc | BHEN283166:BH14740-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_BARHE | ||||||||
| Accession | Primary (citable) accession number: Q6G5P7 | ||||||||
| 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