Q49W02 (GPMI_STAS1) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 61.
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: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase Short name=BPG-independent PGAM Short name=Phosphoglyceromutase Short name=iPGM EC=5.4.2.1 | ||||
| Gene names |
| ||||
| Organism | Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 342451 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcus › ![]() |
Protein attributes
| Sequence length | 505 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. HAMAP-Rule MF_01038 |
| Catalytic activity | 2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP-Rule MF_01038 |
| Cofactor | Binds 2 manganese ions per subunit By similarity. HAMAP-Rule MF_01038 |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule MF_01038 |
| Subunit structure | Monomer By similarity. HAMAP-Rule MF_01038 |
| Sequence similarities | Belongs to the BPG-independent phosphoglycerate mutase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis |
| Ligand | Manganese Metal-binding |
| Molecular function | Isomerase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | glycolysis Inferred from electronic annotation. Source: HAMAP |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: InterPro |
| Molecular_function | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity Inferred from electronic annotation. Source: HAMAP manganese ion bindingInferred 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 – 505 | 505 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038 | PRO_0000212216 | |||||
Sites | |||||||||
| Active site | 62 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 12 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 62 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 397 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 401 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 438 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 439 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 456 | 1 | Manganese 1 By similarity | ||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Whole genome sequence of Staphylococcus saprophyticus reveals the pathogenesis of uncomplicated urinary tract infection." Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T. Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 15305 / DSM 20229. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP008934 Genomic DNA. Translation: BAE19058.1. |
| RefSeq | YP_302003.1. NC_007350.1. |
3D structure databases | |
| ProteinModelPortal | Q49W02. |
| SMR | Q49W02. Positions 2-503. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 342451.SSP1913. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAE19058; BAE19058; SSP1913. |
| GeneID | 3615267. |
| KEGG | ssp:SSP1913. |
| PATRIC | 19625407. VBIStaSap90642_1907. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0696. |
| HOGENOM | HOG000223664. |
| KO | K15633. |
| OMA | NAEQMTD. |
| ProtClustDB | PRK05434. |
Enzyme and pathway databases | |
| BioCyc | SSAP342451:GKFA-1976-MONOMER. |
| UniPathway | UPA00109; UER00186. |
Family and domain databases | |
| Gene3D | 3.40.1450.10. 1 hit. 3.40.720.10. 2 hits. |
| HAMAP | MF_01038. GpmI. |
| InterPro | IPR017849. Alkaline_Pase-like_a/b/a. IPR017850. Alkaline_phosphatase_core. IPR011258. BPG-indep_PGM_N. IPR006124. Metalloenzyme. IPR005995. Pgm_bpd_ind. [Graphical view] |
| Pfam | PF06415. iPGM_N. 1 hit. PF01676. Metalloenzyme. 1 hit. [Graphical view] |
| PIRSF | PIRSF001492. IPGAM. 1 hit. |
| SUPFAM | SSF53649. Alkaline_phosphatase_core. 1 hit. SSF64158. BPG-indep_PGM_N. 1 hit. |
| TIGRFAMs | TIGR01307. pgm_bpd_ind. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GPMI_STAS1 | ||||||||
| Accession | Primary (citable) accession number: Q49W02 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
