Reviewed,
UniProtKB/Swiss-Prot P0A392 (DHLE_BACCR)
Last modified
January 19, 2010.
Version 36.
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 (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 226900 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group |
Protein attributes
| Sequence length | 366 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
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 | Complete proteome |
| 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] | "Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. Kyrpides N.C.Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AE016877 Genomic DNA. Translation: AAP11078.1. |
| RefSeq | NP_833877.1. |
3D structure databases | |
| SMR | P0A392. Positions 3-366. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P0A392. |
Genome annotation databases | |
| GeneID | 1206507. |
| GenomeReviews | Gene locus BC_4162 in contig AE016877_GR. |
| KEGG | bce:BC4162. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0334. |
| HOGENOM | HBG590661. |
| OMA | LCRHLHE. |
Enzyme and pathway databases | |
| BioCyc | BCER226900:BC_4162-MONOMER. |
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_dom. 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. |
| SMART | SM00839. ELFV_dehydrog. 1 hit. [Graphical view] |
| PROSITE | PS00074. GLFV_DEHYDROGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHLE_BACCR | ||||||||
| Accession | Primary (citable) accession number: P0A392 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


