H0NW58 (H0NW58_BACCE) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 11.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Malate dehydrogenase HAMAP-Rule MF_00487 EC=1.1.1.37 HAMAP-Rule MF_00487 | ||||
| Gene names |
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| Organism | Bacillus cereus NC7401 EMBL BAL20286.1 | ||||
| Taxonomic identifier | 334406 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group › ![]() |
Protein attributes
| Sequence length | 312 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. SAAS SAAS011275 HAMAP-Rule MF_00487 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. SAAS SAAS011275 HAMAP-Rule MF_00487 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 3 family. HAMAP-Rule MF_00487 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle SAAS SAAS011275 HAMAP-Rule MF_00487 |
| Ligand | NAD SAAS SAAS011275 HAMAP-Rule MF_00487 |
| Molecular function | Oxidoreductase SAAS SAAS011275 HAMAP-Rule MF_00487 |
| PTM | Phosphoprotein HAMAP-Rule MF_00487 |
| Gene Ontology (GO) | |
| Biological_process | cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro malate metabolic processInferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: HAMAP |
| Molecular_function | L-malate dehydrogenase activity Inferred from electronic annotation. Source: HAMAP nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Nucleotide binding | 12 – 17 | 6 | NAD By similarity HAMAP-Rule MF_00487 | ||||||
| Nucleotide binding | 123 – 125 | 3 | NAD By similarity HAMAP-Rule MF_00487 | ||||||
Sites | |||||||||
| Active site | 180 | 1 | Proton acceptor By similarity HAMAP-Rule MF_00487 | ||||||
| Binding site | 36 | 1 | NAD By similarity HAMAP-Rule MF_00487 | ||||||
| Binding site | 87 | 1 | Substrate By similarity HAMAP-Rule MF_00487 | ||||||
| Binding site | 93 | 1 | Substrate By similarity HAMAP-Rule MF_00487 | ||||||
| Binding site | 100 | 1 | NAD By similarity HAMAP-Rule MF_00487 | ||||||
| Binding site | 125 | 1 | Substrate By similarity HAMAP-Rule MF_00487 | ||||||
| Binding site | 156 | 1 | Substrate By similarity HAMAP-Rule MF_00487 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 149 | 1 | Phosphoserine By similarity HAMAP-Rule MF_00487 | ||||||
Sequences
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References
| [1] | "Complete Genome Sequence of Bacillus cereus NC7401, Which Produces High Levels of the Emetic Toxin Cereulide." Takeno A., Okamoto A., Tori K., Oshima K., Hirakawa H., Toh H., Agata N., Yamada K., Ogasawara N., Hayashi T., Shimizu T., Kuhara S., Hattori M., Ohta M. J. Bacteriol. 194:4767-4768(2012) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: NC7401 EMBL BAL20286.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AP007209 Genomic DNA. Translation: BAL20286.1. |
| RefSeq | YP_005107026.1. NC_016771.1. |
3D structure databases | |
| ProteinModelPortal | H0NW58. |
| SMR | H0NW58. Positions 5-309. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | BAL20286; BAL20286; BCN_4493. |
| GeneID | 11688767. |
| KEGG | bnc:BCN_4493. |
Phylogenomic databases | |
| KO | K00024. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| HAMAP | MF_00487. Malate_dehydrog_3. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR011275. Malate_DH_type3. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR11540. PTHR11540. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| PRINTS | PR00086. LLDHDRGNASE. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| TIGRFAMs | TIGR01763. MalateDH_bact. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | H0NW58_BACCE | ||||||||
| Accession | Primary (citable) accession number: H0NW58 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
