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P46369 (THCA_RHOER) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
EPTC-inducible aldehyde dehydrogenase

EC=1.2.1.3
Gene names
Name:thcA
OrganismRhodococcus erythropolis (Arthrobacter picolinophilus)
Taxonomic identifier1833 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Degrades all aldehydes potentially generated by N dealkylation of thiocarbamates and may also participate in ethanolamine metabolism and further assimilation of degradation products by thiocarbamate-induced cytochrome P-450.

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Induction

By EPTC (S-ethyl dipropylcarbamothioate).

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   LigandNAD
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed
Chain2 – 506505EPTC-inducible aldehyde dehydrogenase
PRO_0000056453

Regions

Nucleotide binding219 – 2257NAD By similarity

Sites

Active site2631 By similarity
Active site3021 By similarity

Sequences

Sequence LengthMass (Da)Tools
P46369 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DDA25B7138B34B37

FASTA50654,994
        10         20         30         40         50         60 
MTKYARPGTA DAIMSFQSRY DNWIGNEWVA PVKGQYFENP TPVTGQNFCD VARSTAEDIE 

        70         80         90        100        110        120 
LALDAAHAAA PAWGKTSVAE RAIILNKIAD RMEENLESIA LAESWDNGKP IRETLNADIP 

       130        140        150        160        170        180 
LAIDHFRYFA GAIRAQEGSL SEINSDTVAY HFHEPLGVVG QIIPWNFPIL MAVWKLAPAL 

       190        200        210        220        230        240 
AAGNAIVLKP AEQTPVSILH LIGIIGDLLP AGVLNIVNGF GVEAGKPLAS SPRIKKIAFT 

       250        260        270        280        290        300 
GETTTGRLIM QYASQNLIPV TLELGGKSPN VFFSDVLASN DDYQDKALEG FTMFALNQGE 

       310        320        330        340        350        360 
VCTAPSRALI QEDIFDEFLA MAAIRTKAVR QGDPLDTDTM IGAQASNDQL EKILSYIEIG 

       370        380        390        400        410        420 
KAEGAKVITG GERAELGGDL SGGYYVQPTV FTGNNKMRIF QEIFGPVVSV TSFKDYDEAI 

       430        440        450        460        470        480 
EIANDTLYGL GAGVWSRDGG VAYRAGRDIQ AGRVWTNTYH QYPAHAAFGG YKQSGIGREN 

       490        500 
HLMMLSHYQQ TKNLLVSYAQ KAQGFF 

« Hide

References

[1]"Degradation of the thiocarbamate herbicide EPTC (S-ethyl dipropylcarbamothioate) and biosafening by Rhodococcus sp. strain NI86/21 involve an inducible cytochrome P-450 system and aldehyde dehydrogenase."
Nagy I., Schoofs G., Compernolle F., Proost P., Vanderleyden J., de Mot R.
J. Bacteriol. 177:676-687(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: NI86/21.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U17129 Genomic DNA. Translation: AAC77472.1.

3D structure databases

ProteinModelPortalP46369.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP46369.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS_CYS.
IPR029510. Ald_DH_CS_GLU.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHCA_RHOER
AccessionPrimary (citable) accession number: P46369
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 67 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