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P9WQH2 (ACDH_MYCTO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 4. 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
Name:mhpF
Ordered Locus Names:MT3639
OrganismMycobacterium tuberculosis (strain CDC 1551 / Oshkosh) [Complete proteome] [HAMAP]
Taxonomic identifier83331 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

Protein attributes

Sequence length303 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 – 303303Acetaldehyde dehydrogenase HAMAP-Rule MF_01657
PRO_0000426776

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
P9WQH2 [UniParc].

Last modified April 16, 2014. Version 1.
Checksum: D52F1BEA88A56827

FASTA30332,009
        10         20         30         40         50         60 
MPSKAKVAIV GSGNISTDLL YKLLRSEWLE PRWMVGIDPE SDGLARAAKL GLETTHEGVD 

        70         80         90        100        110        120 
WLLAQPDKPD LVFEATSAYV HRDAAPKYAE AGIRAIDLTP AAVGPAVIPP ANLREHLDAP 

       130        140        150        160        170        180 
NVNMITCGGQ ATIPIVYAVS RIVEVPYAEI VASVASVSAG PGTRANIDEF TKTTARGVQT 

       190        200        210        220        230        240 
IGGAARGKAI IILNPADPPM IMRDTIFCAI PTDADREAIA ASIHDVVKEV QTYVPGYRLL 

       250        260        270        280        290        300 
NEPQFDEPSI NSGGQALVTT FVEVEGAGDY LPPYAGNLDI MTAAATKVGE EIAKETLVVG 


GAR 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000516 Genomic DNA. Translation: AAK47998.1.
PIRH70675.
RefSeqNP_338184.1. NC_002755.2.

3D structure databases

ProteinModelPortalP9WQH2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID926564.

Organism-specific databases

CMRSearch...

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_MYCTO
AccessionPrimary (citable) accession number: P9WQH2
Secondary accession number(s): L0TEF0, P71866, Q7D5C3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 16, 2014
Last sequence update: April 16, 2014
Last modified: July 9, 2014
This is version 4 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