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P46368 (DHA2_CUPNH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=1.2.1.3
Alternative name(s):
Acetaldehyde dehydrogenase II
Short name=ACDH-II
Gene names
Name:acoD
Ordered Locus Names:H16_B1960
OrganismCupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337) (Ralstonia eutropha) [Complete proteome] [HAMAP]
Taxonomic identifier381666 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeCupriavidus

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the catabolism of acetoin and ethanol.

Catalytic activity

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

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Ketone degradation; acetoin degradation.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Biological processAcetoin catabolism
   LigandNAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processacetoin catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

ethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   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

Chain1 – 506506Acetaldehyde dehydrogenase 2
PRO_0000056566

Regions

Nucleotide binding240 – 2456NAD By similarity

Sites

Active site2621 By similarity
Active site3011 By similarity

Sequences

Sequence LengthMass (Da)Tools
P46368 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: A8715BD93B126D4D

FASTA50654,882
        10         20         30         40         50         60 
MNMAEIAQLG VSNPYKQQYE NYIGGAWVPP AGGEYFESTT PITGKPFTRV PRSGQQDVDA 

        70         80         90        100        110        120 
ALDAAHAAKA AWARTSTTER ANILNRIADR IEANLKLLAV AESIDNGKPV RETTAADLPL 

       130        140        150        160        170        180 
AVDHFRYFAG CIRAQEGGIS EIDADTIAYH FHEPLGVVGQ IIPWNFPLLM ATWKLAPALA 

       190        200        210        220        230        240 
AGNCVVLKPA EQTPASILVL MEVIGDLLPP GVVNVINGFG LEAGKPLASS PRISKVAFTG 

       250        260        270        280        290        300 
ETTTGRLIMQ YASQNLIPVT LELGGKSPNI FFEDVLAADD AFFDKALEGF AMFALNQGEV 

       310        320        330        340        350        360 
CTCPSRALIQ ESIYDRFMER ALKRVAAIRQ GHPLDTGTMI GAQASAEQLE KILSYIDLGR 

       370        380        390        400        410        420 
KEGAQCLTGG ERNVLDGDLA GGYYVKPTVF AGHNKMRIFQ EEIFGPVVSV TTFKDEEEAL 

       430        440        450        460        470        480 
AIANDTLYGL GAGVWTRDGA RAFRMGRGIQ AGRVWTNCYH AYPAHAAFGG YKQSGIGREN 

       490        500 
HRMMLDHYQQ TKNLLVSYSP NALGFF 

« Hide

References

« Hide 'large scale' references
[1]"Identification and molecular characterization of the gene coding for acetaldehyde dehydrogenase II (acoD) of Alcaligenes eutrophus."
Priefert H., Krueger N., Jendrossek D., Schmidt B., Steinbuechel A.
J. Bacteriol. 174:899-907(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-20.
[2]"Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia eutropha H16."
Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I., Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.
Nat. Biotechnol. 24:1257-1262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 17699 / H16 / DSM 428 / Stanier 337.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74003 Genomic DNA. Translation: AAA21943.1.
AM260480 Genomic DNA. Translation: CAJ96742.1.
PIRA42597.
RefSeqYP_841472.1. NC_008314.1.

3D structure databases

ProteinModelPortalP46368.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING381666.H16_B1960.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ96742; CAJ96742; H16_B1960.
GeneID4456449.
KEGGreh:H16_B1960.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
KOK00128.
OMAKGEVCTC.
OrthoDBEOG6BS8QW.

Enzyme and pathway databases

BioCycCNEC381666:GJUJ-5660-MONOMER.
RETL1328306-WGS:GSTH-3798-MONOMER.
UniPathwayUPA00040.
UPA00780; UER00768.

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 nameDHA2_CUPNH
AccessionPrimary (citable) accession number: P46368
Secondary accession number(s): Q0JZT2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: July 9, 2014
This is version 92 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

PATHWAY comments

Index of metabolic and biosynthesis pathways