P54377 (GCSPB_BACSU) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 92.
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: Probable glycine dehydrogenase [decarboxylating] subunit 2 EC=1.4.4.2 Alternative name(s): Glycine cleavage system P-protein subunit 2 Glycine decarboxylase subunit 2 | ||||||
| Gene names |
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| Organism | Bacillus subtilis (strain 168) [Reference proteome] [HAMAP] | ||||||
| Taxonomic identifier | 224308 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 488 AA. |
| Sequence status | Complete. |
| 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. HAMAP-Rule MF_00713 |
| Catalytic activity | Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO2. HAMAP-Rule MF_00713 |
| Cofactor | Pyridoxal phosphate By similarity. |
| Subunit structure | The glycine cleavage system is composed of four proteins: P, T, L and H. In this organism, the P 'protein' is a heterodimer of two subunits. |
| Sequence similarities | Belongs to the GcvP family. C-terminal subunit subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | glycine decarboxylation via glycine cleavage system Inferred from electronic annotation. Source: HAMAP |
| 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 – 488 | 488 | Probable glycine dehydrogenase [decarboxylating] subunit 2 HAMAP-Rule MF_00713 | PRO_0000167001 | |||||
Amino acid modifications | |||||||||
| Modified residue | 273 | 1 | N6-(pyridoxal phosphate)lysine By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes." Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y. Microbiology 142:3103-3111(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168 / JH642. |
| [2] | "The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. Danchin A.Nature 390:249-256(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D84432 Genomic DNA. Translation: BAA12548.1. AL009126 Genomic DNA. Translation: CAB14386.1. |
| PIR | B69959. |
| RefSeq | NP_390335.1. NC_000964.3. |
3D structure databases | |
| ProteinModelPortal | P54377. |
| SMR | P54377. Positions 6-486. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 224308.BSU24550. |
Proteomic databases | |
| PaxDb | P54377. |
| PRIDE | P54377. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | CAB14386; CAB14386; BSU24550. |
| GeneID | 938549. |
| KEGG | bsu:BSU24550. |
| PATRIC | 18976744. VBIBacSub10457_2562. |
Organism-specific databases | |
| GenoList | BSU24550. [Micado] |
Phylogenomic databases | |
| eggNOG | COG1003. |
| HOGENOM | HOG000239368. |
| KO | K00283. |
| OMA | RHYTRLS. |
| ProtClustDB | PRK04366. |
Enzyme and pathway databases | |
| BioCyc | BSUB:BSU24550-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.640.10. 1 hit. |
| HAMAP | MF_00713. GcvPB. |
| InterPro | IPR020580. GDC-P_N. IPR020581. GDC_P. IPR023012. GDC_P_su2. IPR015424. PyrdxlP-dep_Trfase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| PANTHER | PTHR11773. PTHR11773. 1 hit. |
| Pfam | PF02347. GDC-P. 1 hit. [Graphical view] |
| SUPFAM | SSF53383. PyrdxlP-dep_Trfase_major. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GCSPB_BACSU | ||||||||
| Accession | Primary (citable) accession number: P54377 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Bacillus subtilis Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList |
| SIMILARITY comments Index of protein domains and families |

Clusters with
