P94135 (TFDF2_CUPPJ) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 78.
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: Maleylacetate reductase 2 EC=1.3.1.32 Alternative name(s): Chloromaleylacetate reductase Maleylacetate reductase II | ||||
| Gene names |
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| Encoded on | Plasmid pJP4 Ref.1 Ref.2 Ref.4 Plasmid pReut1 Ref.3 | ||||
| Organism | Cupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 264198 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Cupriavidus › ![]() |
Protein attributes
| Sequence length | 359 AA. |
| Sequence status | Complete. |
| 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 |
| 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] [Europe PMC] [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]. Strain: JMP134 / LMG 1197. |
| [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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32, CHARACTERIZATION. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U16782 Genomic DNA. Translation: AAC44727.1. AY365053 Genomic DNA. Translation: AAR31044.1. CP000093 Genomic DNA. Translation: AAZ65769.1. |
| RefSeq | YP_025392.1. NC_005912.1. YP_293626.1. NC_007337.1. |
3D structure databases | |
| ProteinModelPortal | P94135. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 264198.Reut_D6471. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | AAZ65769; AAZ65769; Reut_D6471. |
| GeneID | 2847409. 3607895. |
| KEGG | reu:Reut_D6471. |
| PATRIC | 20225322. VBIRalEut24049_0540. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG1454. |
| HOGENOM | HOG000243333. |
| OMA | AGTISNI. |
| ProtClustDB | CLSK881605. |
Enzyme and pathway databases | |
| BioCyc | CPIN264198:GIW3-6557-MONOMER. |
| UniPathway | UPA00083. |
Family and domain databases | |
| InterPro | IPR001670. ADH_Fe. [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_CUPPJ | ||||||||
| Accession | Primary (citable) accession number: P94135 Secondary accession number(s): Q46M61 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
