H9ZSV8 (H9ZSV8_THETH) Unreviewed, UniProtKB/TrEMBL
Last modified
April 3, 2013.
Version 9.
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_01517 RuleBase RU004066 EC=1.1.1.37 HAMAP-Rule MF_01517 RuleBase RU004066 | ||||
| Gene names |
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| Organism | Thermus thermophilus JL-18 EMBL AFH39418.1 | ||||
| Taxonomic identifier | 798128 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Deinococcus-Thermus › Deinococci › Thermales › Thermaceae › Thermus › ![]() |
Protein attributes
| Sequence length | 327 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. SAAS SAAS001252 HAMAP-Rule MF_01517 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. SAAS SAAS010945 HAMAP-Rule MF_01517 RuleBase RU004066 |
| Subunit structure | Homodimer By similarity. SAAS SAAS010945 HAMAP-Rule MF_01517 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 2 family. HAMAP-Rule MF_01517 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle SAAS SAAS010945 RuleBase RU000422 HAMAP-Rule MF_01517 |
| Ligand | NAD SAAS SAAS010945 RuleBase RU000422 HAMAP-Rule MF_01517 |
| Molecular function | Oxidoreductase HAMAP-Rule MF_01517 RuleBase RU004066 |
| 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 | 11 – 17 | 7 | NAD By similarity HAMAP-Rule MF_01517 | ||||||
| Nucleotide binding | 129 – 131 | 3 | NAD By similarity HAMAP-Rule MF_01517 | ||||||
Sites | |||||||||
| Active site | 187 | 1 | Proton acceptor By similarity HAMAP-Rule MF_01517 | ||||||
| Binding site | 92 | 1 | Substrate By similarity HAMAP-Rule MF_01517 | ||||||
| Binding site | 98 | 1 | Substrate By similarity HAMAP-Rule MF_01517 | ||||||
| Binding site | 105 | 1 | NAD By similarity HAMAP-Rule MF_01517 | ||||||
| Binding site | 112 | 1 | NAD By similarity HAMAP-Rule MF_01517 | ||||||
| Binding site | 131 | 1 | Substrate By similarity HAMAP-Rule MF_01517 | ||||||
| Binding site | 162 | 1 | Substrate By similarity HAMAP-Rule MF_01517 | ||||||
Sequences
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References
| [1] | "Complete sequence of chromosome of Thermus thermophilus JL-18." US DOE Joint Genome Institute Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Lam J. Woyke T.Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: JL-18 EMBL AFH39418.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP003252 Genomic DNA. Translation: AFH39418.1. |
| RefSeq | YP_006059204.1. NC_017587.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AFH39418; AFH39418; TtJL18_1540. |
| GeneID | 12654214. |
| KEGG | ttl:TtJL18_1540. |
Phylogenomic databases | |
| KO | K00024. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| HAMAP | MF_01517. Malate_dehydrog_2. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. IPR001252. Malate_DH_AS. IPR010945. Malate_DH_type2. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| PANTHER | PTHR23382. PTHR23382. 1 hit. |
| Pfam | PF02866. Ldh_1_C. 1 hit. PF00056. Ldh_1_N. 1 hit. [Graphical view] |
| PIRSF | PIRSF000102. Lac_mal_DH. 1 hit. |
| SUPFAM | SSF56327. Lactate_DH/Glyco_hydro_4_C. 1 hit. |
| TIGRFAMs | TIGR01759. MalateDH-SF1. 1 hit. |
| PROSITE | PS00068. MDH. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | H9ZSV8_THETH | ||||||||
| Accession | Primary (citable) accession number: H9ZSV8 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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