A5WLR9 (A5WLR9_MYCTF) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 26.
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 MF_01517 RuleBase RU000422 EC=1.1.1.37 HAMAP MF_01517 RuleBase RU000422 | ||||
| Gene names |
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| Organism | Mycobacterium tuberculosis (strain F11) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 336982 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 329 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the reversible oxidation of malate to oxaloacetate By similarity. HAMAP MF_01517 SAAS SAAS001252 |
| Catalytic activity | (S)-malate + NAD+ = oxaloacetate + NADH. HAMAP MF_01517 RuleBase RU000422 SAAS SAAS010945 |
| Subunit structure | Homodimer By similarity. HAMAP MF_01517 SAAS SAAS010945 |
| Sequence similarities | Belongs to the LDH/MDH superfamily. MDH type 2 family. HAMAP MF_01517 RuleBase RU000421 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle HAMAP MF_01517 RuleBase RU000422 SAAS SAAS010945 |
| Ligand | NAD HAMAP MF_01517 RuleBase RU000422 SAAS SAAS010945 |
| Molecular function | Oxidoreductase HAMAP MF_01517 RuleBase RU000421 |
| 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 – 18 | 7 | NAD By similarity HAMAP MF_01517 | ||||||
| Nucleotide binding | 130 – 132 | 3 | NAD By similarity HAMAP MF_01517 | ||||||
Sites | |||||||||
| Active site | 188 | 1 | Proton acceptor By similarity HAMAP MF_01517 | ||||||
| Binding site | 93 | 1 | Substrate By similarity HAMAP MF_01517 | ||||||
| Binding site | 99 | 1 | Substrate By similarity HAMAP MF_01517 | ||||||
| Binding site | 106 | 1 | NAD By similarity HAMAP MF_01517 | ||||||
| Binding site | 113 | 1 | NAD By similarity HAMAP MF_01517 | ||||||
| Binding site | 132 | 1 | Substrate By similarity HAMAP MF_01517 | ||||||
| Binding site | 163 | 1 | Substrate By similarity HAMAP MF_01517 | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium tuberculosis F11." Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S. Murray M.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000717 Genomic DNA. Translation: ABR05608.1. |
| RefSeq | YP_001287210.1. NC_009565.1. |
3D structure databases | |
| ProteinModelPortal | A5WLR9. |
| SMR | A5WLR9. Positions 4-329. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5WLR9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5221942. |
| GenomeReviews | Gene locus TBFG_11265 in contig CP000717_GR. |
| KEGG | mtf:TBFG_11265. |
| PATRIC | 18133462. VBIMycTub9078_1390. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | NKIQISL. |
| ProtClustDB | PRK05442. |
Family and domain databases | |
| HAMAP | MF_01517. Malate_dehydrog_2. [Tree] |
| 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] |
| Gene3D | G3DSA:3.90.110.10. lact_mal_DH. 1 hit. G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| KO | K00024. |
| PANTHER | PTHR23382. MDH_SF1. 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 | A5WLR9_MYCTF | ||||||||
| Accession | Primary (citable) accession number: A5WLR9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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