ID   ACDH_GEOSE              Reviewed;         294 AA.
AC   B0VXM6;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   13-SEP-2023, entry version 49.
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=pheF;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OG   Plasmid pGGO1.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 67824 / DSM 6285 / BR219;
RA   Jaentges U.K., Omokoko B., Wilkening U., Reiss M., Zimmermann M.,
RA   Hartmeier W.;
RT   "Characterization of the phe-operon responsible for phenol degradation in
RT   Geobacillus stearothermophilus.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; DQ146476; ACA01538.1; -; Genomic_DNA.
DR   PDB; 7Z3S; X-ray; 1.99 A; A=1-294.
DR   PDBsum; 7Z3S; -.
DR   AlphaFoldDB; B0VXM6; -.
DR   SMR; B0VXM6; -.
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   1: Evidence at protein level;
KW   3D-structure; Aromatic hydrocarbons catabolism; NAD; Oxidoreductase;
KW   Plasmid.
FT   CHAIN           1..294
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387626"
FT   ACT_SITE        126
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         11..14
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         157..165
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         269
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   STRAND          4..9
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           13..22
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          26..34
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           41..48
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          52..54
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           57..63
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           65..67
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          69..73
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           77..89
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          93..96
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          103..105
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   TURN            108..110
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           112..114
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          119..122
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           126..139
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          144..154
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           165..179
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          184..193
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          201..209
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           216..231
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          237..241
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          244..246
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          249..256
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   STRAND          261..263
FT                   /evidence="ECO:0007829|PDB:7Z3S"
FT   HELIX           268..291
FT                   /evidence="ECO:0007829|PDB:7Z3S"
SQ   SEQUENCE   294 AA;  31478 MW;  5F35DB4CBF043B23 CRC64;
     MSKVKVAILG SGNIGTDLMM KLERSNILQL TAMIGIDPES DGLRRAKEKG YTVISTGIKG
     FLEQPELADI VFDATSAKAH IRHAKLLKEA GKTVLDLTPA AVGALVVPPV NLHKHLDEWN
     VNLITCGGQA TIPIVHAINR VHPVGYAEIV ATIASKSAGP GTRANIDEFT QTTARGIEKI
     GGAKKGKAII ILNPAEPPIM MRNTVYALVE EGKIDENAIV QSILEMVKTV QSYVPGYRIR
     TEPIMDGNKI TVFLEVEGAG DYLPKYSGNL DIMTAAAVKV AEELAKHKLA AQTA
//