Reviewed,
UniProtKB/Swiss-Prot P76558 (MAO2_ECOLI)
Last modified
November 4, 2008.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: NADP-dependent malic enzyme Short name=NADP-ME EC=1.1.1.40 | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli (strain K12) [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 83333 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 759 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Catalytic activity | (S)-malate + NADP(+) = pyruvate + CO(2) + NADPH. |
| Cofactor | Divalent metal cations. Prefers magnesium or manganese By similarity. |
| Subunit structure | Homooligomer. |
| 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 NADP |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Multifunctional enzyme |
Gene Ontology (GO) | |
| Cellular component | cytosol Inferred from direct assay. Source: UniProtKB |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 759 | 759 | NADP-dependent malic enzyme | PRO_0000160242 | |||||
Regions | |||||||||
| Nucleotide binding | 76 – 83 | 8 | NADP By similarity | ||||||
| Region | 1 – 428 | 428 | Malic enzyme | ||||||
| Region | 429 – 759 | 331 | Phosphate acetyltransferase | ||||||
Sites | |||||||||
| Active site | 94 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 136 | 1 | Divalent metal cation By similarity | ||||||
| Metal binding | 137 | 1 | Divalent metal cation By similarity | ||||||
| Binding site | 162 | 1 | NAD By similarity | ||||||
| Binding site | 288 | 1 | NAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 56 | 1 | N6-acetyllysine | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T.DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [2] | "The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [3] | "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911. |
| [4] | "Studies on regulatory functions of malic enzymes. VI. Purification and molecular properties of NADP-linked malic enzyme from Escherichia coli W." Iwakura M., Hattori J., Arita Y., Tokushige M., Katsuki H. J. Biochem. 85:1355-1365(1979) [PubMed: 36376] [Abstract] Cited for: CHARACTERIZATION. Strain: W / ATCC 11105 / DSM 1900. |
| [5] | "Lysine acetylation is a highly abundant and evolutionarily conserved modification in E. coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 0:0-0(2008) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-56, MASS SPECTROMETRY. |
Cross-references
Sequence databases | |
|---|---|
| U00096 Genomic DNA. Translation: AAC75516.1. AP009048 Genomic DNA. Translation: BAA16337.1. | |
| PIR | F65021. |
| RefSeq | AP_003048.1. NP_416958.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP:10141N. |
| IntAct | P76558. |
Genome annotation databases | |
| GeneID | 946947. |
| GenomeReviews | Gene locus b2463 in contig U00096_GR. Gene locus JW2447 in contig AP009048_GR. |
| KEGG | ecj:JW2447. eco:b2463. |
Organism-specific databases | |
| EchoBASE | EB3945. |
| EcoGene | EG14193. maeB. |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P76558. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:MALIC-NADP-MON. MetaCyc:MALIC-NADP-MON. |
Family and domain databases | |
| InterPro | IPR015884. Malic_enzyme_CS. IPR012301. Malic_N. IPR012302. Malic_NAD_bd. IPR012188. ME_PTA. IPR016040. NAD(P)-bd. 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] |
| BLOCKS | Search... |
| ProtoNet | Search... |
Entry information
| Entry name | MAO2_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P76558 Secondary accession number(s): P78200, P78201 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| UniProtKB secondary accession numbers Index of UniProtKB secondary accession numbers |
| SIMILARITY comments Index of protein domains and families |

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