C2E3K8 (C2E3K8_LACJH) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 20.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2 HAMAP MF_01039 Short name=BPG-dependent PGAM 2 HAMAP MF_01039 Short name=PGAM 2 HAMAP MF_01039 Short name=Phosphoglyceromutase 2 HAMAP MF_01039 Short name=dPGM 2 HAMAP MF_01039 EC=5.4.2.1 HAMAP MF_01039 | ||||||
| Gene names |
| ||||||
| Organism | Lactobacillus johnsonii ATCC 33200 EMBL EEJ60310.1 | ||||||
| Taxonomic identifier | 525330 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Lactobacillales › Lactobacillaceae › Lactobacillus |
Protein attributes
| Sequence length | 230 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 MF_01039 RuleBase RU004512 |
| Catalytic activity | 2-phospho-D-glycerate = 3-phospho-D-glycerate. HAMAP MF_01039 RuleBase RU004512 SAAS SAAS005952 |
| Pathway | Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5. HAMAP MF_01039 RuleBase RU004512 |
| Sequence similarities | Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily. HAMAP MF_01039 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Glycolysis HAMAP MF_01039 SAAS SAAS005952 |
| Molecular function | Isomerase HAMAP MF_01039 SAAS SAAS005952 EMBL EEJ60310.1 |
| Gene Ontology (GO) | |
| Biological process | glycolysis Inferred from electronic annotation. Source: HAMAP |
| Molecular function | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity Inferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Sites | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Active site | 9 | 1 | Tele-phosphohistidine intermediate By similarity HAMAP MF_01039 | ||||||
| Active site | 182 | 1 | By similarity HAMAP MF_01039 | ||||||
| Site | 60 | 1 | Interaction with carboxyl group of phosphoglycerates By similarity HAMAP MF_01039 | ||||||
Sequences
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References
| [1] | Qin X., Bachman B., Battles P., Bell A., Bess C., Bickham C., Chaboub L., Chen D., Coyle M., Deiros D.R., Dinh H., Forbes L., Fowler G., Francisco L., Fu Q., Gubbala S., Hale W., Han Y. Gibbs R.Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: ATCC 33200 EMBL EEJ60310.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ACGR01000024 Genomic DNA. Translation: EEJ60310.1. |
3D structure databases | |
| ProteinModelPortal | C2E3K8. |
| SMR | C2E3K8. Positions 1-229. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| PATRIC | 27455784. VBILacJoh81045_1367. |
Phylogenomic databases | |
| OMA | EWNALNL. |
Family and domain databases | |
| HAMAP | MF_01039. PGAM_GpmA. [Tree] |
| InterPro | IPR013078. His_Pase_superF_clade-1. IPR001345. PG/BPGM_mutase_AS. IPR005952. Phosphogly_mut1. [Graphical view] |
| PANTHER | PTHR11931. Phosphogly_mut1. 1 hit. |
| Pfam | PF00300. His_Phos_1. 1 hit. [Graphical view] |
| SMART | SM00855. PGAM. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01258. Pgm_1. 1 hit. |
| PROSITE | PS00175. PG_MUTASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | C2E3K8_LACJH | ||||||||
| Accession | Primary (citable) accession number: C2E3K8 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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