ID   ACDH3_COMTE             Reviewed;         316 AA.
AC   Q9S153;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   13-SEP-2023, entry version 72.
DE   RecName: Full=Acetaldehyde dehydrogenase 3 {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] 3 {ECO:0000255|HAMAP-Rule:MF_01657};
GN   Name=mhpF;
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=10537203; DOI=10.1099/00221287-145-10-2813;
RA   Arai H., Yamamoto T., Ohishi T., Shimizu T., Nakata T., Kudo T.;
RT   "Genetic organization and characteristics of the 3-(3-
RT   hydroxyphenyl)propionic acid degradation pathway of Comamonas testosteroni
RT   TA441.";
RL   Microbiology 145:2813-2820(1999).
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; AB024335; BAA82883.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S153; -.
DR   SMR; Q9S153; -.
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..316
FT                   /note="Acetaldehyde dehydrogenase 3"
FT                   /id="PRO_0000387652"
FT   ACT_SITE        132
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         12..15
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         163..171
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         289
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   316 AA;  33136 MW;  A107BBAF90A009EF CRC64;
     MTRKLKAAII GSGNIGTDLM IKILRHGKNI EMGAMVGIDP HSDGLARASR MGVATTHEGV
     EGLTRMPGFA EIDFVFDATS AGAHVKNDAF LRSLKPGIRM IDLTPAAIGP YCIPVVNGDM
     HLDAPNVNMV TCGGQATIPM VAAVSRVAKV HYGEIIASIA SKSAGPGTRA NIDEFTETTS
     KAIEVVGGAT KGKAIIIMNP AEPPLIMRDT VYTLSALADE AAIAASVEQM AAAVQSYVPG
     YRLKQQVQFD RIDTPIRIPG VGNALTGLKT SIFLEVEGAA HYLPAYAGNL DIMTSAGLRT
     AEHMAERMLA TLAVAA
//