ID   ACDH_PELTS              Reviewed;         298 AA.
AC   A5D522;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
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=mhpF; OrderedLocusNames=PTH_0482;
OS   Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC   Pelotomaculum.
OX   NCBI_TaxID=370438;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13744 / JCM 10971 / SI;
RX   PubMed=18218977; DOI=10.1101/gr.7136508;
RA   Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT   "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT   evolution in anaerobic microbiota.";
RL   Genome Res. 18:442-448(2008).
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; AP009389; BAF58663.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5D522; -.
DR   SMR; A5D522; -.
DR   STRING; 370438.PTH_0482; -.
DR   EnsemblBacteria; BAF58663; BAF58663; PTH_0482.
DR   KEGG; pth:PTH_0482; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_9; -.
DR   OMA; NVNMISC; -.
DR   Proteomes; UP000006556; Chromosome.
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; Reference proteome.
FT   CHAIN           1..298
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387702"
FT   ACT_SITE        125
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         156..164
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         266
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   298 AA;  31797 MW;  26191D24090ACE6D CRC64;
     MKKVKAAIIG PGNIGTDLMY KLLRSNYIEI ALMVGIYPQS EGLARARSLG IETSHEGIGA
     VLREPDIKIV FDATAAKPHL KHAPLLREAG KIAIDLTPAA VGPYMVPVVN IDEHLEADNV
     NMVTCGGQAT VPIVAAINRV AGVRYAEIVA SLASKSAGPG TRQNIDEFTE TTARALEVVG
     GAGKGKAIII LNPAEPPIMM HNTIYTLVEN PDEELIKSAV FEMVKRIQEY VPGYRLQVEP
     LVEGNKVTTI IEVTGAGDYL PPYAGNLDIM TSAAARAGEL MAMRLLGVYK PERGDSCA