ID   ACDH1_COMTE             Reviewed;         307 AA.
AC   Q83VZ4;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 75.
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   Name=tesF;
OS   Comamonas testosteroni (Pseudomonas testosteroni).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=285;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=TA441;
RX   PubMed=12676694; DOI=10.1128/aem.69.4.2139-2152.2003;
RA   Horinouchi M., Hayashi T., Koshino H., Yamamoto T., Kudo T.;
RT   "Gene encoding the hydrolase for the product of the meta-cleavage reaction
RT   in testosterone degradation by Comamonas testosteroni.";
RL   Appl. Environ. Microbiol. 69:2139-2152(2003).
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; AB063482; BAC67695.1; -; Genomic_DNA.
DR   RefSeq; WP_004341179.1; NZ_BKBW01000005.1.
DR   AlphaFoldDB; Q83VZ4; -.
DR   SMR; Q83VZ4; -.
DR   GeneID; 60804722; -.
DR   OMA; NVNMISC; -.
DR   BioCyc; MetaCyc:MON-16930; -.
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.
FT   CHAIN           1..307
FT                   /note="Acetaldehyde dehydrogenase 1"
FT                   /id="PRO_0000387650"
FT   ACT_SITE        132
FT                   /note="Acyl-thioester intermediate"
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         274
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   307 AA;  32667 MW;  F19FDF0742DB27B1 CRC64;
     MTQKKIKCAL IGPGNIGTDL LMKLQRSPIL EPVWMVGIDP ESDGLKRARE MGIKTTADGV
     DGLLPFVKED GIQIAFDATS AYVHAENSRK LNELGVLMID LTPAAIGPYC VPSVNLAEKV
     AEKAMNVNMV TCGGQATIPM VAAVSRVQAV SYGEIVATVS SRSVGPGTRK NIDEFTRTTS
     GAVEKIGGAQ KGKAIIVINP AEPPLIMRDT IHCLTVDTPK PAEIEASVHA MIKEVQKYVP
     GYKLVNGPVI DGNRVSIYME VEGLGDYLPK YAGNLDIMTA AAARTAEMFA EEILAGRFEL
     AEAAVAV