P0A393 (DHLE_BACCE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 40.
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: Leucine dehydrogenase Short name=LeuDH EC=1.4.1.9 | ||
| Gene names |
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| Organism | Bacillus cereus | ||
| Taxonomic identifier | 1396 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group![]() |
Protein attributes
| Sequence length | 366 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Functions catabolically in the bacterial metabolism of branched-chain L-amino acids, and plays an important role in spore germination in cooperation with alanine dehydrogenase By similarity. |
| Catalytic activity | L-leucine + H2O + NAD+ = 4-methyl-2-oxopentanoate + NH3 + NADH. |
| Pathway | |
| Subunit structure | Homohexamer By similarity. |
| Sequence similarities | Belongs to the Glu/Leu/Phe/Val dehydrogenases family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Branched-chain amino acid catabolism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | leucine catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | leucine dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning, sequencing and overexpression of the leucine dehydrogenase gene from Bacillus cereus." Stoyan T., Recktenwald A., Kula M.R. J. Biotechnol. 54:77-80(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-18; 47-56; 160-192; 214-254 AND 279-298. Strain: DSM 626. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U51099 Genomic DNA. Translation: AAA96314.1. |
3D structure databases | |
| ProteinModelPortal | P0A393. |
| SMR | P0A393. Positions 3-366. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00363; UER00858. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. |
| InterPro | IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR006097. Glu/Leu/Phe/Val_DH_dimer_dom. IPR016211. Glu/Phe/Leu/Val_DH_bac/arc. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR11606:SF3. PTHR11606:SF3. 1 hit. |
| Pfam | PF00208. ELFV_dehydrog. 1 hit. PF02812. ELFV_dehydrog_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000188. Phe_leu_dh. 1 hit. |
| PRINTS | PR00082. GLFDHDRGNASE. |
| SMART | SM00839. ELFV_dehydrog. 1 hit. [Graphical view] |
| PROSITE | PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHLE_BACCE | ||||||||
| Accession | Primary (citable) accession number: P0A393 Secondary accession number(s): Q59194 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
