Reviewed,
UniProtKB/Swiss-Prot O30807 (MAO1_RHIME)
Last modified
June 16, 2009.
Version 67.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: NAD-dependent malic enzyme Short name=NAD-ME EC=1.1.1.39 | ||||||
| Gene names |
| ||||||
| Organism | Rhizobium meliloti (Sinorhizobium meliloti) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 382 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Rhizobiaceae › Sinorhizobium/Ensifer group › Sinorhizobium |
Protein attributes
| Sequence length | 770 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Required for symbiotic nitrogen fixation. Plays a key role in the conversion of malate to acetyl-CoA for efficient tricarboxylic acid cycle function in nitrogen-fixating bacteria. |
| Catalytic activity | (S)-malate + NAD+ = pyruvate + CO2 + NADH. |
| Cofactor | Divalent metal cations. Prefers magnesium or manganese By similarity. |
| Enzyme regulation | Subject to substrate inhibition and shows allosteric regulation by acetyl-CoA. |
| Subunit structure | Homooctamer. |
| Sequence similarities | In the N-terminal section; belongs to the malic enzymes family. In the C-terminal section; belongs to the phosphate acetyltransferase and butyryltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Metal-binding NAD |
| Molecular function | Oxidoreductase |
| Technical term | Allosteric enzyme Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | NAD or NADH binding Inferred from electronic annotation. Source: InterPro acyltransferase activityInferred from electronic annotation. Source: InterPro malate dehydrogenase (decarboxylating) activityInferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 770 | 770 | NAD-dependent malic enzyme | PRO_0000160245 | |||||
Regions | |||||||||
| Region | 1 – 440 | 440 | Malic enzyme | ||||||
| Region | 441 – 770 | 330 | Phosphate acetyltransferase | ||||||
Sites | |||||||||
| Active site | 107 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 149 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 150 | 1 | Divalent metal cation By similarity | ||||||
| Binding site | 175 | 1 | NAD By similarity | ||||||
| Binding site | 300 | 1 | NAD By similarity | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Chimeric structure of the NAD(P)+- and NADP+-dependent malic enzymes of Rhizobium (Sinorhizobium) meliloti." Mitsch M.J., Voegele R.T., Cowie A., Oesteras M., Finan T.M. J. Biol. Chem. 273:9330-9336(1998) [PubMed: 9535928] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION. Strain: RCR2011 / SU47. |
| [2] | "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium meliloti strain 1021." Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J., Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S., Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D.  Galibert F.Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(2001) [PubMed: 11481430] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 1021. |
| [3] | "Characterization of two members of a novel malic enzyme class." Voegele R.T., Mitsch M.J., Finan T.M. Biochim. Biophys. Acta 1432:275-285(1999) [PubMed: 10407149] [Abstract] Cited for: CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| AF017443 Genomic DNA. Translation: AAB82459.1. AL591688 Genomic DNA. Translation: CAC46416.1. | |
| RefSeq | NP_385943.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1233502. |
| GenomeReviews | Gene locus R01837 in contig AL591688_GR. |
| KEGG | sme:SMc00169. |
| NMPDR | fig|266834.1.peg.3131. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | O30807. |
| OMA | O30807. PEGDPRY. |
Enzyme and pathway databases | |
| BioCyc | SMEL266834:SMC00169-MON. |
| BRENDA | 1.1.1.39. 142. |
Family and domain databases | |
| InterPro | IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD_bd. IPR012188. ME_PTA. IPR016040. NAD(P)-bd_dom. IPR002505. PTA_PTB. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. |
| Pfam | PF00390. malic. 1 hit. PF03949. Malic_M. 1 hit. PF01515. PTA_PTB. 1 hit. [Graphical view] |
| PIRSF | PIRSF036684. ME_PTA. 1 hit. |
| PROSITE | PS00331. MALIC_ENZYMES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MAO1_RHIME | ||||||||
| Accession | Primary (citable) accession number: O30807 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
