ID   ACDH1_RHOE4             Reviewed;         300 AA.
AC   C0ZPX0;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   10-JUN-2026, entry version 85.
DE   RecName: Full=Acetaldehyde dehydrogenase 1 {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] 1 {ECO:0000255|HAMAP-Rule:MF_01657};
GN   OrderedLocusNames=RER_07400;
OS   Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Nocardiaceae; Rhodococcus; Rhodococcus erythropolis group.
OX   NCBI_TaxID=234621;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PR4 / NBRC 100887;
RA   Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA   Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT   PR4 and Rhodococcus opacus B4.";
RL   Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + NAD(+) + CoA = acetyl-CoA + NADH + H(+);
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; AP008957; BAH31448.1; -; Genomic_DNA.
DR   RefSeq; WP_020906143.1; NC_012490.1.
DR   AlphaFoldDB; C0ZPX0; -.
DR   SMR; C0ZPX0; -.
DR   KEGG; rer:RER_07400; -.
DR   eggNOG; COG4569; Bacteria.
DR   HOGENOM; CLU_062208_0_0_11; -.
DR   Proteomes; UP000002204; Chromosome.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   CDD; cd23933; ALDH_C; 1.
DR   Gene3D; 3.30.360.10; Dihydrodipicolinate Reductase, domain 2; 1.
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   NCBIfam; NF006157; PRK08300.1; 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; Reference proteome.
FT   CHAIN           1..300
FT                   /note="Acetaldehyde dehydrogenase 1"
FT                   /id="PRO_0000387718"
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         276
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   300 AA;  31948 MW;  DB6574359F5DE4C5 CRC64;
     MTKASVAIVG SGNISTDLLY KLQRSEWLEP RWMIGIDPES EGLARARKMG LETSAEGVDW
     LLSQAEKPDL VFEATSAYVH REAAPRYEAA GIRAIDLTPA AVGPAVVPPA NLREHLDAPN
     VNMITCGGQA TIPIVYAVSR VVDVAYAEIV ASVASLSAGP GTRANIDEFT KTTSRGIETI
     GGAQRGKAII ILNPADPPMI MRDTIFCAIP EDADQAAITD SIHRVVKDIQ QYVPGYRLLN
     EPQFDKPSVV SGGYATVTTF VEVEGAGDFL PPYAGNLDIM TAAATKVGEE IAQKLLSVKA
//