Reviewed,
UniProtKB/Swiss-Prot P0A393 (DHLE_BACCE)
Last modified
June 16, 2009.
Version 22.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names 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 › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 366 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 | branched chain family amino acid catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | binding Inferred from electronic annotation. Source: InterPro leucine dehydrogenase activityInferred from electronic annotation. Source: EC |
| 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: 9188201] [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 | |
|---|---|
| U51099 Genomic DNA. Translation: AAA96314.1. | |
3D structure databases | |
| HSSP | HSSP built from PDB template 1C1D based on UniProtKB Q59771. |
| SMR | P0A393. Positions 3-366. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.4.1.9. 604. |
Family and domain databases | |
| InterPro | IPR006095. Glu/Leu/Phe/Val_DH. IPR006096. Glu/Leu/Phe/Val_DH_C. IPR006097. Glu/Leu/Phe/Val_DH_dimer. IPR016211. Glu/Phe/Leu/Val_DH_bac/arc. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 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. |
| 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 project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


