P52217 (GRDB_CLOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 53.
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: Glycine reductase complex component B subunit gamma EC=1.21.4.2 Alternative name(s): Selenoprotein PB gamma | ||
| Gene names |
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| Organism | Clostridium litorale (Bacterium W6) | ||
| Taxonomic identifier | 1557 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Clostridia › Clostridiales › Peptostreptococcaceae![]() |
Protein attributes
| Sequence length | 436 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | In the first step of glycine reductase, the substrate is bound to component PB via a Schiff base intermediate. Then the PB-activated substrate is nucleophilically attacked by the selenol anion of component PA to transform it to a carboxymethylated selenoether and the respective amine. By action of component PC, acetyl phosphate is formed, leaving component PA in its oxidized state. Finally component PA becomes reduced by the thioredoxin system to start a new catalytic cycle of reductive deamination. |
| Catalytic activity | Acetyl phosphate + NH3 + thioredoxin disulfide + H2O = glycine + phosphate + thioredoxin. |
| Subunit structure | Heterohexamer of two alpha, two beta and two gamma subunits. Component of the glycine reductase complex, together with components A and C. PB is substrate specific. |
| Sequence similarities | Belongs to the GrdB/GrdF/GrdH family. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Selenocysteine |
| Molecular function | Oxidoreductase |
| Gene Ontology (GO) | |
| Cellular_component | glycine reductase complex Inferred from electronic annotation. Source: InterPro |
| Molecular_function | glycine reductase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Glycine reductase of Clostridium litorale. Cloning, sequencing, and molecular analysis of the grdAB operon that contains two in-frame TGA codons for selenium incorporation." Kreimer S., Andreesen J.R. Eur. J. Biochem. 234:192-199(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 49638 / DSM 5388 / W6. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U24268 Genomic DNA. Translation: AAC43574.2. |
| PIR | S63988. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR010186. Gly_red_sel_B. IPR022787. GRDB. IPR010187. Various_sel_PB. [Graphical view] |
| Pfam | PF07355. GRDB. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01917. gly_red_sel_B. 1 hit. TIGR01918. various_sel_PB. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GRDB_CLOLI | ||||||||
| Accession | Primary (citable) accession number: P52217 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
