D6XST1 (D6XST1_BACIE) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 18.
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 selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10) [Complete proteome] [HAMAP] EMBL ADH98867.1 | ||||
| Taxonomic identifier | 439292 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › ![]() |
Protein attributes
| Sequence length | 311 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP-Rule MF_00487 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. 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 HAMAP-Rule MF_00487 |
| Ligand | NAD HAMAP-Rule MF_00487 |
| Molecular function | Oxidoreductase HAMAP-Rule MF_00487 EMBL ADH98867.1 |
| PTM | Phosphoprotein HAMAP-Rule MF_00487 |
| Technical term | Complete proteome |
| 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 sequence of Bacillus selenitireducens MLS10." US DOE Joint Genome Institute Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J. Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700615 / DSM 15326 / MLS10. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001791 Genomic DNA. Translation: ADH98867.1. |
| RefSeq | YP_003699433.1. NC_014219.1. |
3D structure databases | |
| ProteinModelPortal | D6XST1. |
| SMR | D6XST1. Positions 5-311. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ADH98867; ADH98867; Bsel_1355. |
| GeneID | 9263927. |
| KEGG | bse:Bsel_1355. |
| PATRIC | 38122005. VBIBacSel78655_1448. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | HOG000213794. |
| KO | K00024. |
Enzyme and pathway databases | |
| BioCyc | BSEL439292:GHLG-1417-MONOMER. |
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 | D6XST1_BACIE | ||||||||
| Accession | Primary (citable) accession number: D6XST1 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

Clusters with
