P47668 (PT1_MYCGE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 78.
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: Phosphoenolpyruvate-protein phosphotransferase EC=2.7.3.9 Alternative name(s): Phosphotransferase system, enzyme I | ||||
| Gene names |
| ||||
| Organism | Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243273 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Tenericutes › Mollicutes › Mycoplasmataceae › Mycoplasma |
Protein attributes
| Sequence length | 572 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr) By similarity. |
| Catalytic activity | Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)-phospho-L-histidine. |
| Cofactor | Magnesium By similarity. |
| Subunit structure | Homodimer By similarity. |
| Subcellular location | |
| Domain | The N-terminal domain contains the HPr binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity. |
| Miscellaneous | The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity. |
| Sequence similarities | Belongs to the PEP-utilizing enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Phosphotransferase system Sugar transport Transport |
| Cellular component | Cytoplasm |
| Ligand | Magnesium Metal-binding |
| Molecular function | Kinase Transferase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | phosphoenolpyruvate-dependent sugar phosphotransferase system Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | kinase activity Inferred from electronic annotation. Source: UniProtKB-KW metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW phosphoenolpyruvate-protein phosphotransferase activityInferred from electronic annotation. Source: EC sugar:hydrogen symporter activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 572 | 572 | Phosphoenolpyruvate-protein phosphotransferase | PRO_0000147076 | |||||
Sites | |||||||||
| Active site | 190 | 1 | Tele-phosphohistidine intermediate By similarity | ||||||
| Active site | 498 | 1 | Proton donor By similarity | ||||||
| Metal binding | 427 | 1 | Magnesium By similarity | ||||||
| Metal binding | 451 | 1 | Magnesium By similarity | ||||||
| Binding site | 297 | 1 | Substrate By similarity | ||||||
| Binding site | 333 | 1 | Substrate By similarity | ||||||
| Binding site | 427 | 1 | Substrate By similarity | ||||||
| Binding site | 448 | 1 | Substrate; via carbonyl oxygen By similarity | ||||||
| Binding site | 449 | 1 | Substrate; via amide nitrogen By similarity | ||||||
| Binding site | 450 | 1 | Substrate By similarity | ||||||
| Binding site | 451 | 1 | Substrate; via amide nitrogen By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The minimal gene complement of Mycoplasma genitalium." Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., Nguyen D.T., Utterback T.R., Saudek D.M. Venter J.C.Science 270:397-403(1995) [PubMed: 7569993] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33530 / G-37 / NCTC 10195. |
| [2] | "Novel phosphotransferase system genes revealed by bacterial genome analysis: the complete complement of pts genes in Mycoplasma genitalium." Reizer J., Paulsen I.T., Reizer A., Titgemeyer F., Saier M.H. Jr. Microb. Comp. Genomics 1:151-164(1996) [PubMed: 9689210] [Abstract] Cited for: DISCUSSION OF SEQUENCE. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L43967 Genomic DNA. Translation: AAC72450.1. |
| PIR | D64247. |
| RefSeq | NP_073100.1. NC_000908.2. |
3D structure databases | |
| ProteinModelPortal | P47668. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 875624. |
| GenomeReviews | Gene locus MG429 in contig L43967_GR. |
| KEGG | mge:MG_429. |
| PATRIC | 20010444. VBIMycGen98045_0495. |
| TIGR | MG429. |
Phylogenomic databases | |
| HOGENOM | HBG456539. |
| OMA | KITINEC. |
| PhylomeDB | P47668. |
| ProtClustDB | CLSK335335. |
Enzyme and pathway databases | |
| BioCyc | MGEN243273:MG_429-MONOMER. |
Family and domain databases | |
| InterPro | IPR008279. PEP-util_enz_mobile_dom. IPR018274. PEP_util_AS. IPR000121. PEP_util_C. IPR023151. PEP_util_CS. IPR006318. PEP_util_enz. IPR024692. PTS_enz_I. IPR008731. PTS_PEP_utilis_N. IPR015813. Pyrv/PenolPyrv_Kinase. [Graphical view] |
| Gene3D | G3DSA:3.50.30.10. PEP_mobile. 1 hit. G3DSA:1.10.274.10. PTS_PEP_utilis_N. 1 hit. G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| KO | K08483. |
| PANTHER | PTHR22931:SF10. PTHR22931:SF10. 1 hit. |
| Pfam | PF05524. PEP-utilisers_N. 1 hit. PF00391. PEP-utilizers. 1 hit. PF02896. PEP-utilizers_C. 1 hit. [Graphical view] |
| PIRSF | PIRSF000732. PTS_enzyme_I. 1 hit. |
| PRINTS | PR01736. PHPHTRNFRASE. |
| SUPFAM | SSF47831. PEP-utilisers_N. 1 hit. SSF52009. PEP_mobile. 1 hit. SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit. |
| TIGRFAMs | TIGR01417. PTS_I_fam. 1 hit. |
| PROSITE | PS00742. PEP_ENZYMES_2. 1 hit. PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PT1_MYCGE | ||||||||
| Accession | Primary (citable) accession number: P47668 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Mycoplasma genitalium Mycoplasma genitalium (strain G-37): entries and gene names |
| SIMILARITY comments Index of protein domains and families |

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