Reviewed,
UniProtKB/Swiss-Prot P17556 (DHA_BACSH)
Last modified
June 16, 2009.
Version 67.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin
| Protein names | Recommended name: Alanine dehydrogenase EC=1.4.1.1 | ||
| Gene names |
| ||
| Organism | Bacillus sphaericus | ||
| Taxonomic identifier | 1421 [NCBI] | ||
| Taxonomic lineage | Bacteria › Firmicutes › Bacillales › Planococcaceae › Lysinibacillus |
Protein attributes
| Sequence length | 372 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | This enzyme is a key factor in the assimilation of L-alanine as an energy source through the tricarboxylic acid cycle during sporulation. |
| Catalytic activity | L-alanine + H2O + NAD+ = pyruvate + NH3 + NADH. |
| Pathway | |
| Subunit structure | Homohexamer. |
| Subcellular location | |
| Sequence similarities | Belongs to the AlaDH/PNT family. |
| biophysicochemical properties | Temperature dependence: Loses about 50% of its initial activity when heated at 65 degrees Celsius for 5 min. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | alanine dehydrogenase activity Inferred from electronic annotation. Source: EC bindingInferred from electronic annotation. Source: InterPro electron carrier activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
| ||||||||||||||||||
References
| [1] | "Alanine dehydrogenases from two Bacillus species with distinct thermostabilities: molecular cloning, DNA and protein sequence determination, and structural comparison with other NAD(P)(+)-dependent dehydrogenases." Kuroda S., Tanizawa K., Sakamoto Y., Tanaka H., Soda K. Biochemistry 29:1009-1015(1990) [PubMed: 2340274] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 10208 / NRS 966 / NCIB 11935 / 1911. |
Cross-references
Sequence databases | |
|---|---|
| M33298 Genomic DNA. Translation: AAA22210.1. | |
| PIR | A34261. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1SAY based on UniProtKB O52942. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 1.4.1.1. 327. |
Family and domain databases | |
| InterPro | IPR007698. Ala_DH/PNT_C. IPR008142. Ala_DH/PNT_CS1. IPR008143. Ala_DH/PNT_CS2. IPR007886. Ala_DH/PNT_N. IPR008141. Ala_DH_PNT. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF01262. AlaDh_PNT_C. 1 hit. PF05222. AlaDh_PNT_N. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00518. alaDH. 1 hit. |
| PROSITE | PS00836. ALADH_PNT_1. 1 hit. PS00837. ALADH_PNT_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | DHA_BACSH | ||||||||
| Accession | Primary (citable) accession number: P17556 | ||||||||
| Entry history |
| ||||||||
| 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


