Reviewed,
UniProtKB/Swiss-Prot Q3K7X5 (GCSP1_PSEPF)
Last modified
June 16, 2009.
Version 27.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Glycine dehydrogenase [decarboxylating] 1 EC=1.4.4.2 Alternative name(s): Glycine decarboxylase 1 Glycine cleavage system P-protein 1 | ||||
| Gene names |
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| Organism | Pseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 205922 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pseudomonadales › Pseudomonadaceae › Pseudomonas |
Protein attributes
| Sequence length | 950 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO2 is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein By similarity. |
| Catalytic activity | Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2. HAMAP MF_00711 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Subunit structure | The glycine cleavage system is composed of four proteins: P, T, L and H By similarity. |
| Sequence similarities | Belongs to the gcvP family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glycine decarboxylation via glycine cleavage system Inferred from electronic annotation. Source: HAMAP oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | glycine dehydrogenase (decarboxylating) activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred 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 – 950 | 950 | Glycine dehydrogenase [decarboxylating] 1 HAMAP MF_00711 | PRO_0000227118 | |||||
Amino acid modifications | |||||||||
| Modified residue | 704 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| [1] | "Complete sequence of Pseudomonas fluorescens PfO-1." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Saunders E.H., Schmutz J., Larimer F., Land M., Kyripides N., Anderson I., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000094 Genomic DNA. Translation: ABA76129.1. | |
| RefSeq | YP_350120.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 3712835. |
| GenomeReviews | Gene locus Pfl01_4392 in contig CP000094_GR. |
| KEGG | pfo:Pfl01_4392. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q3K7X5. |
| OMA | Q3K7X5. PETIMIE. |
Enzyme and pathway databases | |
| BioCyc | PFLU205922:PFL_4392-MON. |
Family and domain databases | |
| HAMAP | MF_00711. [Tree] |
| InterPro | IPR003437. GDC-P. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR11773. GDC-P. 1 hit. |
| Pfam | PF02347. GDC-P. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00461. gcvP. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GCSP1_PSEPF | ||||||||
| Accession | Primary (citable) accession number: Q3K7X5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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