Reviewed,
UniProtKB/Swiss-Prot Q9PI71 (GPMI_CAMJE)
Last modified
June 16, 2009.
Version 54.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 2,3-bisphosphoglycerate-independent phosphoglycerate mutase Short name=Phosphoglyceromutase Short name=BPG-independent PGAM Short name=iPGM EC=5.4.2.1 | ||||||
| Gene names |
| ||||||
| Organism | Campylobacter jejuni [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 197 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter |
Protein attributes
| Sequence length | 492 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate By similarity. |
| Catalytic activity | 2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01038 |
| Cofactor | Binds 2 manganese ions per subunit By similarity. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01038 |
| Subunit structure | Monomer By similarity. |
| 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: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 492 | 492 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP MF_01038 | PRO_0000212133 | |||||
Sites | |||||||||
| Active site | 61 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 11 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 61 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 386 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 390 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 427 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 428 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 445 | 1 | Manganese 1 By similarity | ||||||
Sequences
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References
| [1] | "The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. Barrell B.G.Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2. |
Cross-references
Sequence databases | |
|---|---|
| AL111168 Genomic DNA. Translation: CAL34584.1. | |
| PIR | H81387. |
| RefSeq | YP_002343871.1. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1O98 based on UniProtKB Q9X519. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9PI71. 35 interactions. |
Genome annotation databases | |
| GeneID | 904759. |
| GenomeReviews | Gene locus Cj0434 in contig AL111168_GR. |
| KEGG | cje:Cj0434. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | Q9PI71. DHGNAEL. |
Enzyme and pathway databases | |
| BioCyc | CJEJ192222:CJ0434-MON. |
| BRENDA | 5.4.2.1. 255835. |
Family and domain databases | |
| HAMAP | MF_01038. [Tree] |
| InterPro | IPR017849. Alkaline_Pase-like_a/b/a. IPR011258. BPG-indep_PGM_N. IPR006124. Metalloenzyme. IPR005995. Pgm_bpd_ind. [Graphical view] |
| Gene3D | G3DSA:3.40.720.10. Alk_phosphtse. 1 hit. G3DSA:3.40.1450.10. BPG-indep_PGM_N. 1 hit. |
| Pfam | PF06415. iPGM_N. 1 hit. PF01676. Metalloenzyme. 1 hit. [Graphical view] |
| PIRSF | PIRSF001492. IPGAM. 1 hit. |
| ProDom | PD004704. APGAM_DeoB. 1 hit. PD004429. Pgm_bpd_ind. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| TIGRFAMs | TIGR01307. pgm_bpd_ind. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GPMI_CAMJE | ||||||||
| Accession | Primary (citable) accession number: Q9PI71 Secondary accession number(s): Q0PB76 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


