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Reviewed, UniProtKB/Swiss-Prot P27137 (TFDF1_RALEJ)

Last modified June 16, 2009. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Maleylacetate reductase 1
    EC=1.3.1.32
Alternative name(s):
    Maleylacetate reductase I
Gene names
Name: tfdFI
Synonyms: tfdF
Ordered Locus Names: Reut_D6463
Encoded onPlasmid pJP4 Ref.1 Ref.2
Plasmid pReut1 Ref.3
OrganismRalstonia eutropha (strain JMP134) (Alcaligenes eutrophus) [Complete proteome] [HAMAP]
Taxonomic identifier264198 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length354 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

3-oxoadipate + NAD(P)+ = 2-maleylacetate + NAD(P)H.

Pathway

Aromatic compound metabolism; 3-chlorocatechol degradation.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Plasmid
Gene Ontology (GO)
   Biological processaromatic compound catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionmaleylacetate reductase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 354354Maleylacetate reductase 1
PRO_0000087851

Sequences

Sequence LengthMass (Da)Tools
P27137-1 [UniParc].

Last modified August 1, 1992. Version 1.
Checksum: 7D88C001B5B13376

FASTA35437,900
        10         20         30         40         50         60 
MKKFTLDYLS PRVVFGAGTA SALPDEIGRL GARRPLVLSS PEQRELAKDI VRPIGDRVAG 

        70         80         90        100        110        120 
YFDGATMHVP VDVIQKAERA FNDTDADSII AIGGGSTTGL AKILSMNLDV PSLVIPTTYA 

       130        140        150        160        170        180 
GSEMTTIWGV TEGGMKRTGR DPKVLPKTVI YDPLLTVDLP LAISVTSALN AIAHAAEGLY 

       190        200        210        220        230        240 
SADLNPVLET MCKQGICALF DAIPRLVAKP TDAEARTDAL FGAWMCGTAL CHLGMGLHHK 

       250        260        270        280        290        300 
LCHTLGGTLN LPHAETHAIV LPHALAYNLP YAAPAERLLQ EVAGSSDVPS ALYDLARNAG 

       310        320        330        340        350 
APLSLAEIGM RPEDIPRVRD LALRDQYPNP RPLESDALET LLVNAFRGRR PDFK 

« Hide

References

« Hide 'large scale' references
[1]"Organization and sequence analysis of the 2,4-dichlorophenol hydroxylase and dichlorocatechol oxidative operons of plasmid pJP4."
Perkins E.J., Gordon M.P., Caceres O., Lurquin P.F.
J. Bacteriol. 172:2351-2359(1990) [PubMed: 2185214] [Abstract]
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].

Cross-references

Sequence databases

M35097 Genomic DNA. Translation: AAA98265.1.
AY365053 Genomic DNA. Translation: AAR31036.1.
CP000093 Genomic DNA. Translation: AAZ65761.1.
PIRD35255.
RefSeqYP_025384.1.
YP_293618.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2847475.
3607954.
GenomeReviewsGene locus Reut_D6463 in contig CP000093_GR.
KEGGreu:Reut_D6463.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMP27137.

Enzyme and pathway databases

BioCycREUT264198:REUT_D6463-MON.

Family and domain databases

InterProIPR001670. ADH_Fe.
IPR018211. ADH_Fe_CS.
[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 nameTFDF1_RALEJ
AccessionPrimary (citable) accession number: P27137
Secondary accession number(s): Q46M69
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents