Q9KWS1 (ACDH_PSESP) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Acetaldehyde dehydrogenase
EC=1.2.1.10

Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]

Gene names

Name:

amnH

Organism

Pseudomonas sp.

Taxonomic identifier

306 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › unclassified Proteobacteria › unclassified pseudomonads

Protein attributes

Sequence length	316 AA.
Sequence status	Complete.
Protein existence	Inferred 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 2-aminophenol. Ref.1
Catalytic activity	Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH. HAMAP-Rule MF_01657
Sequence similarities	Belongs to the acetaldehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Aromatic hydrocarbons catabolism
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological_process	aromatic compound catabolic process Inferred from electronic annotation. Source: HAMAP cellular amino acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: InterPro
Molecular_function	NAD binding Inferred from electronic annotation. Source: HAMAP acetaldehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 316	316	Acetaldehyde dehydrogenase HAMAP-Rule MF_01657		PRO_0000383027
Regions
	Nucleotide binding	13 – 16	4	NAD By similarity
	Nucleotide binding	162 – 170	9	NAD By similarity
Sites
	Active site	131	1	Acyl-thioester intermediate By similarity
	Binding site	290	1	NAD By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9KWS1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 1A709C936C057242	FASTA	316	33,170
	10 20 30 40 50 60 MSDDRLSVAI IGSGNIGTDL MIKIMRNSKL LKVGAMVGID PKSDGLARAQ RLGVPTTAEG 70 80 90 100 110 120 VDGLLDMPAF RDIKIAFDAT SAGAQAIHNQ KLQAHGVRVI DLTPAAIGPY VIPVVNFDQH 130 140 150 160 170 180 VDAPNINMVT CGGQATIPIV HAVSKVSPVH YAEIVASISS KSAGPGTRAN IDEFTETTSK 190 200 210 220 230 240 AILEVGGAAQ GRAIIILNPA EPPLIMRDTV YCFVSAEANI DAITDSVEQM VKSVQEYVPG 250 260 270 280 290 300 YRLKQKVQFE KIVAGNEQNI PGLGWSTGLK VSVFLEVEGA GHYLPSYAGN LDIMTSAGLT 310 VAERIAGSGV QVGGLK

References

[1]	"Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme." Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K. J. Biol. Chem. 272:14727-14732(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION. Strain: AP-3.
[2]	"Complete nucleotide sequence and functional analysis of the genes for 2-aminophenol metabolism from Pseudomonas sp. AP-3." Takenaka S., Murakami S., Kim Y.J., Aoki K. Arch. Microbiol. 174:265-272(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AP-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB020521 Genomic DNA. Translation: BAB03537.1.
3D structure databases
ProteinModelPortal	Q9KWS1.
SMR	Q9KWS1. Positions 3-308.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
Gene3D	3.40.50.720. 1 hit.
HAMAP	MF_01657. Ac_ald_DH_ac.
InterPro	IPR003361. Acetaldehyde_dehydrogenase. IPR015426. Acetylaldehyde_DH_C. IPR016040. NAD(P)-bd_dom. IPR000534. Semialdehyde_DH_NAD-bd. [Graphical view]
PANTHER	PTHR21123. PTHR21123. 1 hit.
Pfam	PF09290. AcetDehyd-dimer. 1 hit. PF01118. Semialdhyde_dh. 1 hit. [Graphical view]
PIRSF	PIRSF015689. Actaldh_dh_actl. 1 hit.
SMART	SM00859. Semialdhyde_dh. 1 hit. [Graphical view]
TIGRFAMs	TIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNet	Search...

Entry information

Entry name

ACDH_PSESP

Accession

Primary (citable) accession number: Q9KWS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 1, 2009
Last sequence update:	October 1, 2000
Last modified:	April 3, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program