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Q53062 (MEDH_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified September 21, 2011. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NDMA-dependent methanol dehydrogenase

EC=1.1.99.-
Gene names
Name:thcE
OrganismRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifier1833 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length423 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the oxidation of alcohols (including methanol) with the concomitant reduction of N,N'-dimethyl-4-nitroso-aniline (NDMA), aldehydes or ketones. Ref.2

Catalytic activity

Alcohol + NDMAH = aldehyde + NDMA+. Ref.2

Cofactor

NADPH. Ref.2

Subcellular location

Cytoplasm Ref.2.

Induction

Expressed during degradation of thiocarbamates and atrazine. Ref.1

Sequence similarities

Belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandNADP
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: InterPro

oxidoreductase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 423423NDMA-dependent methanol dehydrogenase
PRO_0000247755

Sequences

Sequence LengthMass (Da)Tools
Q53062 [UniParc].

Last modified July 25, 2006. Version 2.
Checksum: 5DB811D6BFDDA820

FASTA42346,356
        10         20         30         40         50         60 
AIELNQIWDF PIKEFHPFPR ALMGVGAHDI IGVEAKNLGF KRTLLMTTGL RGSGIIEELV 

        70         80         90        100        110        120 
GKIEYQGVEV VLYDKVESNP KDYNVMEAAA LYQKEKCDSI ISIGGGSSHD AAKGARVVIA 

       130        140        150        160        170        180 
HDGRNINEFE GFAKSTNKEN PPHIAVSTTA GTGSETSWAY VITDTSDMNN PHKWVGFDEA 

       190        200        210        220        230        240 
TIVTLAIDDP LLYYTCPQHF TAYCGFDVLA HGSEPFVSRL DFAPSLGNAI YSVELVAKNL 

       250        260        270        280        290        300 
REAVFEPRNL KAREGMMNAQ YIAGQAFNSG GLGIVHSISH AVSAFFDSHH GLNNAIALPR 

       310        320        330        340        350        360 
VWEYNLPSRY ERYAQLAGAL GVDTRNLTTV QAADAAVEAA IRLAKDVGIP DNFGQVRTDS 

       370        380        390        400        410        420 
YAKNQMNTKK YEGRGDVIKG DEKTVRAISE HIQDDWCTPG NPREVTVESM IPVVDHAINK 


SYF 

« Hide

References

[1]"Characterization of the Rhodococcus sp. NI86/21 gene encoding alcohol:N,N'-dimethyl-4-nitrosoaniline oxidoreductase inducible by atrazine and thiocarbamate herbicides."
Nagy I., Verheijen S., De Schrijver A., Van Damme J., Proost P., Schoofs G., Vanderleyden J., De Mot R.
Arch. Microbiol. 163:439-446(1995) [PubMed: 7575099] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-19; 88-105 AND 180-195, INDUCTION.
Strain: NI86/21.
[2]"Methanol:NDMA oxidoreductase from Rhodococcus erythropolis DSM 1069."
Schenkels P., Piersma S.R., Duine J.A.
Submitted (JUL-1999) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-30, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBCELLULAR LOCATION.
Strain: DSM 1069.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U21071 Genomic DNA. Translation: AAB80771.1.

3D structure databases

ProteinModelPortalQ53062.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

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 nameMEDH_RHOER
AccessionPrimary (citable) accession number: Q53062
Secondary accession number(s): P81938
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: July 25, 2006
Last modified: September 21, 2011
This is version 39 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families