Skip Header

Contribute Send feedback
Read comments (?) or add your own

P94135 (TFDF2_CUPPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Maleylacetate reductase 2

EC=1.3.1.32
Alternative name(s):
Chloromaleylacetate reductase
Maleylacetate reductase II
Gene names
Name:tfdFII
Ordered Locus Names:Reut_D6471
Encoded onPlasmid pJP4 Ref.1 Ref.2 Ref.4
Plasmid pReut1 Ref.3
OrganismCupriavidus pinatubonensis (strain JMP134 / LMG 1197) (Alcaligenes eutrophus) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length359 AA.
Sequence statusComplete.
Protein existenceEvidence 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

Aromatic compound metabolism; 3-chlorocatechol degradation.

Subunit structure

Homodimer Probable.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 359359Maleylacetate reductase 2
PRO_0000087852

Sequences

Sequence LengthMass (Da)Tools
P94135 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: FC951B482B2575BF

FASTA35937,504
        10         20         30         40         50         60 
MTGDLNEFVA HFWPVRVVFG AGSTERIPAE VKRLGARRAL VLCTPDQRDL AQRVLGDLGD 

        70         80         90        100        110        120 
LGAGFHDGAV MHVPEASVTR AAQAARDADA DLLVAVGGGS TIGLAKALAL HHGMRFVALP 

       130        140        150        160        170        180 
TTYAGSEMTP IWGLTADGAK RTGRDPRVLP STVLYDPHHL TSLPPEVTGP SGMNAIAHAV 

       190        200        210        220        230        240 
ESMYAPDRNP ITMLLAEESI RAMAQGLPVA VDSPGDLDAR TRTLYAAWLA GTVLGMVSMG 

       250        260        270        280        290        300 
LHHKLCHVLG GRFNLPHAPM HAVLLPHVAA FNEVAAPAEL GRVAAALGAP GPGGAGAALH 

       310        320        330        340        350 
ALLRFTCTER SLAAIGMPAQ GIYDAAEHAL ADAYANPRQA SREDIARLLR AAFTGEMPA 

« Hide

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.
RefSeqYP_025392.1. NC_005912.1.
YP_293626.1. NC_007337.1.

3D structure databases

ProteinModelPortalP94135.
ModBaseSearch...

Protein-protein interaction databases

STRING264198.Reut_D6471.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAZ65769; AAZ65769; Reut_D6471.
GeneID2847409.
3607895.
KEGGreu:Reut_D6471.
PATRIC20225322. VBIRalEut24049_0540.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1454.
HOGENOMHOG000243333.
OMAAGTISNI.
ProtClustDBCLSK881605.

Enzyme and pathway databases

BioCycCPIN264198:GIW3-6557-MONOMER.
UniPathwayUPA00083.

Family and domain databases

InterProIPR001670. ADH_Fe.
[Graphical view]
PfamPF00465. Fe-ADH. 1 hit.
[Graphical view]
PROSITEPS00913. ADH_IRON_1. False negative.
PS00060. ADH_IRON_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTFDF2_CUPPJ
AccessionPrimary (citable) accession number: P94135
Secondary accession number(s): Q46M61
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: May 1, 1997
Last modified: May 1, 2013
This is version 78 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families