P74507 (GPMI_SYNY3) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 93.
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 | Synechocystis sp. (strain PCC 6803 / Kazusa) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 1111708 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Cyanobacteria › Oscillatoriophycideae › Chroococcales › Synechocystis › ![]() |
Protein attributes
| Sequence length | 532 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. |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP-Rule 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 Reference 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 – 532 | 532 | 2,3-bisphosphoglycerate-independent phosphoglycerate mutase HAMAP-Rule MF_01038 | PRO_0000212222 | |||||
Sites | |||||||||
| Active site | 65 | 1 | Phosphoserine intermediate By similarity | ||||||
| Metal binding | 15 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 65 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 398 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 402 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 439 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 440 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 457 | 1 | Manganese 1 By similarity | ||||||
Sequences
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References
| [1] | "Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions." Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. Tabata S.DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: PCC 6803 / Kazusa. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BA000022 Genomic DNA. Translation: BAA18611.1. |
| PIR | S76482. |
| RefSeq | NP_441933.1. NC_000911.1. YP_005651993.1. NC_017277.1. YP_007451813.1. NC_020286.1. |
3D structure databases | |
| ProteinModelPortal | P74507. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P74507. 1 interaction. |
| STRING | 1148.slr1945. |
Proteomic databases | |
| PaxDb | P74507. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAA18611; BAA18611; BAA18611. |
| GeneID | 12254653. 14617481. 955019. |
| KEGG | syn:slr1945. syy:SYNGTS_2040. |
| PATRIC | 23841414. VBISynSp132158_2256. |
Phylogenomic databases | |
| eggNOG | COG0696. |
| HOGENOM | HOG000223664. |
| KO | K15633. |
| OMA | NAEQMTD. |
| ProtClustDB | PRK05434. |
Enzyme and pathway databases | |
| 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_SYNY3 | ||||||||
| Accession | Primary (citable) accession number: P74507 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Synechocystis PCC 6803 Synechocystis (strain PCC 6803): entries and gene names |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
