Reviewed,
UniProtKB/Swiss-Prot Q928R9 (DCEB_LISIN)
Last modified
November 3, 2009.
Version 43.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Glutamate decarboxylase beta Short name=GAD-beta EC=4.1.1.15 | ||||
| Gene names |
| ||||
| Organism | Listeria innocua [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 1642 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Listeriaceae › Listeria |
Protein attributes
| Sequence length | 464 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Converts internalized glutamate to GABA and increases the internal pH. Involved in glutamate-dependent acid resistance in gastric fluid By similarity. |
| Catalytic activity | L-glutamate = 4-aminobutanoate + CO2. |
| Cofactor | Pyridoxal phosphate By similarity. |
| Sequence similarities | Belongs to the group II decarboxylase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Pyridoxal phosphate |
| Molecular function | Decarboxylase Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | glutamate metabolic process Inferred from electronic annotation. Source: InterPro |
| Molecular function | glutamate decarboxylase activity Inferred from electronic annotation. Source: EC pyridoxal phosphate bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Comparative genomics of Listeria species." Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E., Dominguez-Bernal G., Duchaud E. Cossart P.Science 294:849-852(2001) [PubMed: 11679669] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CLIP 11262 / Serovar 6a. |
Cross-references
Sequence databases | |
|---|---|
| AL596172 Genomic DNA. Translation: CAC97690.1. | |
| PIR | AB1740. |
| RefSeq | NP_471793.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1131252. |
| GenomeReviews | Gene locus lin2463 in contig AL592022_GR. |
| KEGG | lin:lin2463. |
| NMPDR | fig|272626.1.peg.2446. |
Organism-specific databases | |
| ListiList | LIN02463. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | Q928R9. |
| OMA | AVDEDTI. |
Enzyme and pathway databases | |
| BioCyc | LINN272626:LIN2463-MON. |
| BRENDA | 4.1.1.15. 270396. |
Family and domain databases | |
| InterPro | IPR010107. Glutamate_decarboxylase. IPR002129. PyrdxlP-dep_de-COase. IPR015421. PyrdxlP-dep_Trfase_major_sub1. [Graphical view] |
| Gene3D | G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit. |
| PANTHER | PTHR11999:SF1. Glu_decarb_GAD. 1 hit. PTHR11999. Pyridoxal_deC. 1 hit. |
| Pfam | PF00282. Pyridoxal_deC. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR01788. Glu-decarb-GAD. 1 hit. |
| PROSITE | PS00392. DDC_GAD_HDC_YDC. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DCEB_LISIN | ||||||||
| Accession | Primary (citable) accession number: Q928R9 | ||||||||
| 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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