ACDH_PSESP
ID ACDH_PSESP Reviewed; 316 AA.
AC Q9KWS1;
DT 01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657};
DE EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657};
GN Name=amnH;
OS Pseudomonas sp.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=306;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=AP-3;
RX PubMed=9169437; DOI=10.1074/jbc.272.23.14727;
RA Takenaka S., Murakami S., Shinke R., Hatakeyama K., Yukawa H., Aoki K.;
RT "Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas
RT species AP-3 growing on 2-aminophenol and catalytic properties of the
RT purified enzyme.";
RL J. Biol. Chem. 272:14727-14732(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AP-3;
RX PubMed=11081795; DOI=10.1007/s002030000203;
RA Takenaka S., Murakami S., Kim Y.J., Aoki K.;
RT "Complete nucleotide sequence and functional analysis of the genes for 2-
RT aminophenol metabolism from Pseudomonas sp. AP-3.";
RL Arch. Microbiol. 174:265-272(2000).
CC -!- FUNCTION: Catalyzes the conversion of acetaldehyde to acetyl-CoA, using
CC NAD(+) and coenzyme A. Is the final enzyme in the meta-cleavage pathway
CC for the degradation of 2-aminophenol. {ECO:0000269|PubMed:9169437}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01657};
CC -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01657, ECO:0000305}.
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DR EMBL; AB020521; BAB03537.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9KWS1; -.
DR SMR; Q9KWS1; -.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01657; Ac_ald_DH_ac; 1.
DR InterPro; IPR003361; Acetaldehyde_dehydrogenase.
DR InterPro; IPR015426; Acetylaldehyde_DH_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR Pfam; PF09290; AcetDehyd-dimer; 1.
DR Pfam; PF01118; Semialdhyde_dh; 1.
DR PIRSF; PIRSF015689; Actaldh_dh_actl; 1.
DR SMART; SM00859; Semialdhyde_dh; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
DR TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE 3: Inferred from homology;
KW Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT CHAIN 1..316
FT /note="Acetaldehyde dehydrogenase"
FT /id="PRO_0000383027"
FT ACT_SITE 131
FT /note="Acyl-thioester intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 13..16
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 162..170
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT BINDING 290
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ SEQUENCE 316 AA; 33170 MW; 1A709C936C057242 CRC64;
MSDDRLSVAI IGSGNIGTDL MIKIMRNSKL LKVGAMVGID PKSDGLARAQ RLGVPTTAEG
VDGLLDMPAF RDIKIAFDAT SAGAQAIHNQ KLQAHGVRVI DLTPAAIGPY VIPVVNFDQH
VDAPNINMVT CGGQATIPIV HAVSKVSPVH YAEIVASISS KSAGPGTRAN IDEFTETTSK
AILEVGGAAQ GRAIIILNPA EPPLIMRDTV YCFVSAEANI DAITDSVEQM VKSVQEYVPG
YRLKQKVQFE KIVAGNEQNI PGLGWSTGLK VSVFLEVEGA GHYLPSYAGN LDIMTSAGLT
VAERIAGSGV QVGGLK
