Reviewed,
UniProtKB/Swiss-Prot P94135 (TFDF2_RALEJ)
Last modified
June 16, 2009.
Version 56.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Maleylacetate reductase 2 EC=1.3.1.32 Alternative name(s): Maleylacetate reductase II Chloromaleylacetate reductase | ||||
| Gene names |
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| Encoded on | Plasmid pJP4 Ref.1 Ref.2 Ref.4 Plasmid pReut1 Ref.3 | ||||
| Organism | Ralstonia eutropha (strain JMP134) (Alcaligenes eutrophus) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 264198 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Plays a major role in the degradation of chloroaromatic compounds by channeling maleylacetate and some of its substituted derivatives into the 3-oxoadipate pathway. This enzyme converts maleylacetate and 2-chloromaleylacetate with similar efficiencies. NADH is preferred to NADPH as the cosubstrate. |
| Catalytic activity | 3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H. |
| Enzyme regulation | Inhibited by p-chloromercuribenzoate and by 3-oxoadipate, and, in a temperature-dependent manner, by manganese. |
| Pathway | |
| Subunit structure | Homodimer Probable. |
| Sequence similarities | Belongs to the iron-containing alcohol dehydrogenase family. |
| biophysicochemical properties | pH dependence: Optimum pH is 7.5. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Aromatic hydrocarbons catabolism |
| Ligand | NAD |
| Molecular function | Oxidoreductase |
| Technical term | Complete proteome Direct protein sequencing Plasmid |
| Gene Ontology (GO) | |
| Biological process | aromatic compound catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reductionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | maleylacetate reductase activity Inferred from electronic annotation. Source: EC metal ion bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||
Molecule processing | |||||||
|---|---|---|---|---|---|---|---|
| Chain | 1 – 359 | 359 | Maleylacetate reductase 2 | PRO_0000087852 | |||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | van der Meer J.R. Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Genetic organization of the catabolic plasmid pJP4 from Ralstonia eutropha JMP134 (pJP4) reveals mechanisms of adaptation to chloroaromatic pollutants and evolution of specialized chloroaromatic degradation pathways." Trefault N., De la Iglesia R., Molina A.M., Manzano M., Ledger T., Perez-Pantoja D., Sanchez M.A., Stuardo M., Gonzalez B. Environ. Microbiol. 6:655-668(2004) [PubMed: 15186344] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [3] | "Complete sequence of plasmid 1 of Ralstonia eutropha JMP134." Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Goltsman E., Martinez M., Schmutz J., Larimer F., Land M., Lykidis A., Richardson P. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "Purification and characterization of maleylacetate reductase from Alcaligenes eutrophus JMP134(pJP4)." Seibert V., Stadler-Fritzsche K., Schlomann M. J. Bacteriol. 175:6745-6754(1993) [PubMed: 8226615] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| U16782 Genomic DNA. Translation: AAC44727.1. AY365053 Genomic DNA. Translation: AAR31044.1. CP000093 Genomic DNA. Translation: AAZ65769.1. | |
| RefSeq | YP_025392.1. YP_293626.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 2847409. 3607895. |
| GenomeReviews | Gene locus Reut_D6471 in contig CP000093_GR. |
| KEGG | reu:Reut_D6471. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P94135. |
| OMA | P94135. GSTERIP. |
Enzyme and pathway databases | |
| BioCyc | REUT264198:REUT_D6471-MON. |
Family and domain databases | |
| InterPro | IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. [Graphical view] |
| Pfam | PF00465. Fe-ADH. 1 hit. [Graphical view] |
| PROSITE | PS00913. ADH_IRON_1. False negative. PS00060. ADH_IRON_2. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | TFDF2_RALEJ | ||||||||
| Accession | Primary (citable) accession number: P94135 Secondary accession number(s): Q46M61 | ||||||||
| 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
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with


