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Q1B0P7 (ACDH2_MYCSS) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 61. 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 2

EC=1.2.1.10
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 2
Gene names
Ordered Locus Names:Mmcs_5437
Encoded onPlasmid pMCS1
OrganismMycobacterium sp. (strain MCS) [Complete proteome] [HAMAP]
Taxonomic identifier164756 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeMycobacteriaceaeMycobacterium

Protein attributes

Sequence length315 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
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 – 315315Acetaldehyde dehydrogenase 2 HAMAP-Rule MF_01657
PRO_0000387687

Regions

Nucleotide binding11 – 144NAD By similarity
Nucleotide binding160 – 1689NAD By similarity

Sites

Active site1291Acyl-thioester intermediate By similarity
Binding site2901NAD By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1B0P7 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: ACBAF9085CE720F2

FASTA31532,996
        10         20         30         40         50         60 
MSHSKVAVIG SGNIGTDLVV KLKKLATNVE IAVLVGIDPS SDGLARARRM GIGTVDTGVQ 

        70         80         90        100        110        120 
GLIEHAEFDE IDIIFDSTSA KAHLVNEEAL RTFGKRLIDL TPAAVGPYVV PAVNLDDHLG 

       130        140        150        160        170        180 
APNVNMVTCG GQATIPIVAA ISSVTAVHYA EIVASIASKS AGPGTRSNID EFTQTTSAAI 

       190        200        210        220        230        240 
EKVGGAAHGK AIIVLNPAEP PLIMRDTVLA LVTDPDQNRI RQSVIDMVEK VSAYVPGYRL 

       250        260        270        280        290        300 
KQEVQFTQLD DAESVATLTG GVDKGPGLWK VAVFLEVEGA AHYLPAYAGN LDIMTSAALQ 

       310 
VAERIAANTV QEATR 

« Hide

References

[1]"Complete sequence of plasmid of Mycobacterium sp. MCS."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E. expand/collapse author list , Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.
Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MCS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000385 Genomic DNA. Translation: ABG11537.1.
RefSeqYP_642593.1. NC_008147.1.

3D structure databases

ProteinModelPortalQ1B0P7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING164756.Mmcs_5437.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG11537; ABG11537; Mmcs_5437.
GeneID4114522.
KEGGmmc:Mmcs_5437.
PATRIC18121305. VBIMycSp106721_5567.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4569.
HOGENOMHOG000052149.
KOK04073.
OMAREVQKYV.
OrthoDBEOG6H1PXH.

Enzyme and pathway databases

BioCycMSP164756:GHQ8-5497-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 nameACDH2_MYCSS
AccessionPrimary (citable) accession number: Q1B0P7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: July 11, 2006
Last modified: May 14, 2014
This is version 61 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