ID   ACDH2_COMTE             Reviewed;         307 AA.
AC   Q9RHN2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-SEP-2023, entry version 77.
DE   RecName: Full=Acetaldehyde dehydrogenase 2 {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] 2 {ECO:0000255|HAMAP-Rule:MF_01657};
GN   Name=aphF;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TA441;
RX   PubMed=10878134; DOI=10.1099/00221287-146-7-1707;
RA   Arai H., Ohishi T., Chang M.Y., Kudo T.;
RT   "Arrangement and regulation of the genes for meta-pathway enzymes required
RT   for degradation of phenol in Comamonas testosteroni TA441.";
RL   Microbiology 146:1707-1715(2000).
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}.
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DR   EMBL; AB029044; BAA88503.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RHN2; -.
DR   SMR; Q9RHN2; -.
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   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
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   NCBIfam; TIGR03215; ac_ald_DH_ac; 1.
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; SSF55347; Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase.
FT   CHAIN           1..307
FT                   /note="Acetaldehyde dehydrogenase 2"
FT                   /id="PRO_0000387651"
FT   ACT_SITE        131
FT                   /note="Acyl-thioester intermediate"
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         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   307 AA;  32366 MW;  58120F1B782621E3 CRC64;
     MSQKIKCALI GPGNIGTDLL AKLQRSPVLE PVWMVGIDPD SDGLKRAREM GIKTTAEGVD
     GLLPHMHVDG VQIVFDATSA YVHAENSRKV NERGALMIDL TPAAIGPFCV PPVNLIQHLG
     SGAMNVNMVT CGGQATIPMV AAVSRVQAVA YGEIVATVSS KSVGPGTRKN IDEFTRTTAG
     AVEKVGGAKK GKAIIVINPA EPPLMMRDTV HCLTEDEPDQ AAITASIHQM LAEVQKYVPG
     YRLVNGPVFD GKRVSVFLEV EGLGDYLPKY AGNLDIMTAA AARTAEMFAE QMLAGKLTLA
     PVAPIAA
//