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Q743Q9 (ACDH_MYCPA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 66. 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

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]
Gene names
Ordered Locus Names:MAP_0532
OrganismMycobacterium paratuberculosis (strain ATCC BAA-968 / K-10) [Complete proteome] [HAMAP]
Taxonomic identifier262316 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium avium complex (MAC)

Protein attributes

Sequence length305 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.

Ontologies

Keywords
   Biological processAromatic hydrocarbons catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
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 – 305305Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000387679

Regions

Nucleotide binding12 – 154NAD By similarity
Nucleotide binding158 – 1669NAD By similarity

Sites

Active site1271Acyl-thioester intermediate By similarity
Binding site2771NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q743Q9 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 27A423AEECD1E629

FASTA30532,339
        10         20         30         40         50         60 
MPTKAKVAIV GSGNISTDLL YKLLRSDWLE PRWMVGIDPQ SEGLARARKL GLETTHEGVD 

        70         80         90        100        110        120 
WLLAQPEKPD LVFEATSAYV HRDAAPKYEA AGIRAIDLTP AAVGPAVIPP ANLRQHLDAP 

       130        140        150        160        170        180 
NVNMITCGGQ ATIPIVFAVS RVVEVPYAEI VASVASVSAG PGTRANIDEF TKTTSRGVET 

       190        200        210        220        230        240 
IGGAKRGKAI IILNPADPPM IMRDTIFCAI PEDADRDAIA QSIHDVVKEV QTYVPGYRLL 

       250        260        270        280        290        300 
NEPQFDEPSL NSGGQAVVTT FVEVEGAGDY LPPYAGNLDI MTAAATKVGE EIAKETLATT 


AGGAQ 

« Hide

References

[1]"The complete genome sequence of Mycobacterium avium subspecies paratuberculosis."
Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., Kanjilal S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-968 / K-10.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016958 Genomic DNA. Translation: AAS02849.1.
RefSeqNP_959466.1. NC_002944.2.

3D structure databases

ProteinModelPortalQ743Q9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING262316.MAP0532.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS02849; AAS02849; MAP_0532.
GeneID2721480.
KEGGmpa:MAP0532.
PATRIC17993446. VBIMycAvi108102_0563.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
KOK04073.
OMAHLKHAPL.
OrthoDBEOG6H1PXH.
ProtClustDBPRK08300.

Enzyme and pathway databases

BioCycMAVI262316:GCQR-543-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 nameACDH_MYCPA
AccessionPrimary (citable) accession number: Q743Q9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 66 of the entry and version 1 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