P09424 (MTLD_ECOLI) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Mannitol-1-phosphate 5-dehydrogenase EC=1.1.1.17 | ||||
| Gene names |
| ||||
| Organism | Escherichia coli (strain K12) | ||||
| Taxonomic identifier | 83333 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 382 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Catalytic activity | D-mannitol 1-phosphate + NAD+ = D-fructose 6-phosphate + NADH. HAMAP MF_00196 |
| Subunit structure | Monomer. |
| Sequence similarities | Belongs to the mannitol dehydrogenase family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| PTM | Acetylation |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Molecular function | coenzyme binding Inferred from electronic annotation. Source: InterPro mannitol-1-phosphate 5-dehydrogenase activityInferred from electronic annotation. Source: EC nucleotide bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| selA | P0A821 | 1 | EBI-554652,EBI-1118693 | |
| ydeP | P77561 | 1 | EBI-554652,EBI-545210 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 382 | 382 | Mannitol-1-phosphate 5-dehydrogenase HAMAP MF_00196 | PRO_0000170703 | |||||
Regions | |||||||||
| Nucleotide binding | 3 – 14 | 12 | NAD By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 269 | 1 | N6-acetyllysine Ref.9 | ||||||
Experimental info | |||||||||
| Sequence conflict | 5 | 1 | H → V AA sequence Ref.8 | ||||||
| Sequence conflict | 14 – 15 | 2 | GF → SL AA sequence Ref.8 | ||||||
| Sequence conflict | 86 | 1 | A → R Ref.1 | ||||||
| Sequence conflict | 86 | 1 | A → R Ref.2 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Nucleotide sequence of the mannitol (mtl) operon in Escherichia coli." Davis T., Yamada M., Elgort M., Saier M.H. Jr. Mol. Microbiol. 2:405-412(1988) [PubMed: 3135464] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12. |
| [2] | "Corrected sequence of the mannitol (mtl) operon in Escherichia coli." Jaiang W., Wu L.F., Tomich J., Saier M.H. Jr., Nichaus W.G. Mol. Microbiol. 4:2003-2006(1990) [PubMed: 1964486] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SEQUENCE REVISION. Strain: K12. |
| [3] | "Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076. |
| [4] | "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. |
| [5] | "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. |
| [6] | "The mannitol repressor (MtlR) of Escherichia coli." Figge R.M., Ramseier T.M., Saier M.H. Jr. J. Bacteriol. 176:840-847(1994) [PubMed: 8300537] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 369-382. Strain: K12. |
| [7] | "Purification and properties of D-mannitol-1-phosphate dehydrogenase and D-glucitol-6-phosphate dehydrogenase from Escherichia coli." Novotny M.J., Reizer J., Esch F., Saier M.H. Jr. J. Bacteriol. 159:986-990(1984) [PubMed: 6384188] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-25. |
| [8] | "FIS is a regulator of metabolism in Escherichia coli." Gonzalez-Gil G., Bringmann P., Kahmann R. Mol. Microbiol. 22:21-29(1996) [PubMed: 8899705] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-15. |
| [9] | "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-269, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X51359 Genomic DNA. Translation: CAA35744.1. U00039 Genomic DNA. Translation: AAB18577.1. U00096 Genomic DNA. Translation: AAC76624.1. AP009048 Genomic DNA. Translation: BAE77693.1. X06794 Genomic DNA. Translation: CAA29954.1. Sequence problems. U03845 Genomic DNA. Translation: AAA92661.1. |
| PIR | B65160. |
| RefSeq | NP_418057.1. NC_000913.2. |
3D structure databases | |
| ProteinModelPortal | P09424. |
| SMR | P09424. Positions 1-382. |
| ModBase | Search... |
Protein-protein interaction databases | |
| DIP | DIP-10268N. |
| IntAct | P09424. 11 interactions. |
| MINT | MINT-1240338. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | EBESCT00000002334; EBESCP00000002334; EBESCG00000001904. EBESCT00000017007; EBESCP00000016298; EBESCG00000016066. |
| GeneID | 948117. |
| GenomeReviews | Gene locus JW3574 in contig AP009048_GR. Gene locus b3600 in contig U00096_GR. |
| KEGG | ecj:JW3574. eco:b3600. |
| PATRIC | 32122683. VBIEscCol129921_3718. |
Organism-specific databases | |
| EchoBASE | EB0611. |
| EcoGene | EG10616. mtlD. |
Phylogenomic databases | |
| eggNOG | COG0246. |
| GeneTree | EBGT00050000009063. |
| HOGENOM | HBG568825. |
| OMA | FANTAVD. |
| PhylomeDB | P09424. |
| ProtClustDB | PRK02318. |
Enzyme and pathway databases | |
| BioCyc | EcoCyc:MANNPDEHYDROG-MONOMER. MetaCyc:MANNPDEHYDROG-MONOMER. |
Gene expression databases | |
| Genevestigator | P09424. |
Family and domain databases | |
| HAMAP | MF_00196. Mannitol_dehydrog. [Tree] |
| InterPro | IPR008927. 6-PGluconate_DH_C-like. IPR013328. DH_multihelical. IPR023028. Mannitol_1_phos_5_DH. IPR000669. Mannitol_DH. IPR013118. Mannitol_DH_C. IPR023027. Mannitol_DH_CS. IPR013131. Mannitol_DH_N. IPR016040. NAD(P)-bd_dom. [Graphical view] |
| Gene3D | G3DSA:3.40.50.720. NAD(P)-bd. 1 hit. G3DSA:1.10.1040.10. Opine_DH. 1 hit. |
| KO | K00009. |
| Pfam | PF01232. Mannitol_dh. 1 hit. PF08125. Mannitol_dh_C. 1 hit. [Graphical view] |
| PRINTS | PR00084. MTLDHDRGNASE. |
| SUPFAM | SSF48179. 6DGDH_C_like. 1 hit. |
| PROSITE | PS00974. MANNITOL_DHGENASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MTLD_ECOLI | ||||||||
| Accession | Primary (citable) accession number: P09424 Secondary accession number(s): Q2M7R3 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| Escherichia coli Escherichia coli (strain K12): entries and cross-references to EcoGene |
| SIMILARITY comments Index of protein domains and families |

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