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Q0RXC4 (ACDH6_RHOSR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:
Acetaldehyde dehydrogenase 6

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 6
Gene names
Name:hpdG
Ordered Locus Names:RHA1_ro09018
Encoded onPlasmid pRHL1
OrganismRhodococcus sp. (strain RHA1) [Complete proteome] [HAMAP]
Taxonomic identifier101510 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeNocardiaceaeRhodococcus

Protein attributes

Sequence length299 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds By similarity. HAMAP-Rule MF_01657

Catalytic activity

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP-Rule MF_01657

Sequence similarities

Belongs to the acetaldehyde dehydrogenase family.

Sequence caution

The sequence ABH00062.1 differs from that shown. Reason: Erroneous initiation.

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-HAMAP

   Molecular_functionNAD binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

acetaldehyde dehydrogenase (acetylating) activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 299299Acetaldehyde dehydrogenase 6 HAMAP-Rule MF_01657
PRO_0000387731

Regions

Nucleotide binding156 – 1649NAD By similarity

Sites

Active site1251Acyl-thioester intermediate By similarity
Binding site2751NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0RXC4 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: E0F9484669CC9144

FASTA29931,708
        10         20         30         40         50         60 
MEPINAAIVG PGNIGTDLLA KLERVDSIAV QYVVGVVESD GLERARAKGI SASAGGVDWL 

        70         80         90        100        110        120 
LEQDPLPEIV FEATSAKAHQ LNAPRYHELN IQAVDLTPAH IGPMVCPPVN LTHHIDAPNV 

       130        140        150        160        170        180 
SMITCGGQAT IPMVHAVSRV SAVPYAEIVA SVASRGAGPG TRANIDEFTQ TTGQAVSEVG 

       190        200        210        220        230        240 
GAARGRAIII LNPMEPPMIM RDTVYCMIDA DADRDAISES VHRMVTEVQA YVPGYRLRAD 

       250        260        270        280        290 
PQFDDPKDGW DGHGRVAIFL EVEGNGDYLP KYAGNLDIMT AAAARVGDSI ARNRMGVPA 

« Hide

References

« Hide 'large scale' references
[1]"2-Hydroxypenta-2,4-dienoate metabolic pathway genes in a strong polychlorinated biphenyl degrader, Rhodococcus sp. strain RHA1."
Sakai M., Miyauchi K., Kato N., Masai E., Fukuda M.
Appl. Environ. Microbiol. 69:427-433(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete genome of Rhodococcus sp. RHA1 provides insights into a catabolic powerhouse."
McLeod M.P., Warren R.L., Hsiao W.W.L., Araki N., Myhre M., Fernandes C., Miyazawa D., Wong W., Lillquist A.L., Wang D., Dosanjh M., Hara H., Petrescu A., Morin R.D., Yang G., Stott J.M., Schein J.E., Shin H. expand/collapse author list , Smailus D., Siddiqui A.S., Marra M.A., Jones S.J.M., Holt R., Brinkman F.S.L., Miyauchi K., Fukuda M., Davies J.E., Mohn W.W., Eltis L.D.
Proc. Natl. Acad. Sci. U.S.A. 103:15582-15587(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RHA1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB085906 Genomic DNA. Translation: BAB97164.1.
CP000432 Genomic DNA. Translation: ABH00062.1. Different initiation.
RefSeqYP_708220.1. NC_008269.1.

3D structure databases

ProteinModelPortalQ0RXC4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING101510.RHA1_ro09018.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABH00062; ABH00062; RHA1_ro09018.
GeneID4225923.
KEGGrha:RHA1_ro09018.
PATRIC23215476. VBIRhoJos26306_8301.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycRJOS101510:GJJ1-8297-MONOMER.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
HAMAPMF_01657. Ac_ald_DH_ac.
InterProIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetSearch...

Entry information

Entry nameACDH6_RHOSR
AccessionPrimary (citable) accession number: Q0RXC4
Secondary accession number(s): Q8KZT1
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: November 3, 2009
Last modified: May 14, 2014
This is version 57 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