B8ZR02 (B8ZR02_MYCLB) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 27.
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 leprae (strain Br4923) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 561304 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium |
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] | "Comparative genomic and phylogeographic analysis of Mycobacterium leprae." Monot M., Honore N., Garnier T., Zidane N., Sherafi D., Paniz-Mondolfi A., Matsuoka M., Taylor G.M., Donoghue H.D., Bouwman A., Mays S., Watson C., Lockwood D., Khamispour A., Dowlati Y., Jianping S., Rea T.H., Vera-Cabrera L. Cole S.T.Nat. Genet. 41:1282-1289(2009) [PubMed: 19881526] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | FM211192 Genomic DNA. Translation: CAR71186.1. |
| RefSeq | YP_002503429.1. NC_011896.1. |
3D structure databases | |
| ProteinModelPortal | B8ZR02. |
| SMR | B8ZR02. Positions 5-329. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | B8ZR02. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBMYCT00000085380; EBMYCP00000082195; EBMYCG00000087588. |
| GeneID | 7326558. |
| GenomeReviews | Gene locus MLBr01091 in contig FM211192_GR. |
| PATRIC | 18043449. VBIMycLep121698_1954. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| GeneTree | EBGT00050000018111. |
| HOGENOM | HBG289884. |
| 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. |
| 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 | B8ZR02_MYCLB | ||||||||
| Accession | Primary (citable) accession number: B8ZR02 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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