P11386 (MDH_SULAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 93.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Malate dehydrogenase EC=1.1.1.37 | ||||
| Gene names |
| ||||
| Organism | Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 330779 [NCBI] | ||||
| Taxonomic lineage | Archaea › Crenarchaeota › Thermoprotei › Sulfolobales › Sulfolobaceae › Sulfolobus › ![]() |
Protein attributes
| Sequence length | 306 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Tricarboxylic acid cycle |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | cellular carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro tricarboxylic acid cycleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | L-malate dehydrogenase activity Inferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.2 | ||||||
| Chain | 2 – 306 | 305 | Malate dehydrogenase HAMAP-Rule MF_00487 | PRO_0000113492 | |||||
Regions | |||||||||
| Nucleotide binding | 8 – 13 | 6 | NAD By similarity | ||||||
| Nucleotide binding | 118 – 120 | 3 | NAD By similarity | ||||||
Sites | |||||||||
| Active site | 172 | 1 | Proton acceptor By similarity | ||||||
| Binding site | 33 | 1 | NAD By similarity | ||||||
| Binding site | 82 | 1 | Substrate By similarity | ||||||
| Binding site | 88 | 1 | Substrate By similarity | ||||||
| Binding site | 95 | 1 | NAD By similarity | ||||||
| Binding site | 120 | 1 | Substrate By similarity | ||||||
| Binding site | 148 | 1 | Substrate By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 11 | 1 | R → RG AA sequence Ref.2 | ||||||
| Sequence conflict | 40 – 42 | 3 | EKF → TKK AA sequence Ref.2 | ||||||
Sequences
| ||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "The genome of Sulfolobus acidocaldarius, a model organism of the Crenarchaeota." Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E., Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A. J. Bacteriol. 187:4992-4999(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770. |
| [2] | "Archaebacterial malate dehydrogenase: the amino-terminal sequence of the enzyme from Sulfolobus acidocaldarius is homologous to the eubacterial and eukaryotic malate dehydrogenases." Gorisch H., Jany K.-D. FEBS Lett. 247:259-262(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-42. Strain: ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000077 Genomic DNA. Translation: AAY79663.1. |
| PIR | S03958. |
| RefSeq | YP_254956.1. NC_007181.1. |
3D structure databases | |
| ProteinModelPortal | P11386. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 330779.Saci_0246. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAY79663; AAY79663; Saci_0246. |
| GeneID | 3474728. |
| KEGG | sai:Saci_0246. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0039. |
| HOGENOM | HOG000213793. |
| KO | K00024. |
| OMA | CLIDVCA. |
| ProtClustDB | CLSK883804. |
Enzyme and pathway databases | |
| BioCyc | SACI330779:GH9J-322-MONOMER. |
Family and domain databases | |
| Gene3D | 3.40.50.720. 1 hit. 3.90.110.10. 1 hit. |
| HAMAP | MF_00487. Malate_dehydrog_3. Divergent sequence. |
| InterPro | IPR001557. L-lactate/malate_DH. IPR022383. Lactate/malate_DH_C. IPR001236. Lactate/malate_DH_N. IPR015955. Lactate_DH/Glyco_Ohase_4_C. 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. |
| ProtoNet | Search... |
Entry information
| Entry name | MDH_SULAC | ||||||||
| Accession | Primary (citable) accession number: P11386 Secondary accession number(s): Q4JC16 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
