ID   ALDH_ENCBU              Reviewed;         497 AA.
AC   Q27640;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            EC=1.2.1.3;
DE   AltName: Full=Aldehyde dehydrogenase [NAD(+)];
GN   Name=ALDH;
OS   Enchytraeus buchholzi (Grindal worm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Annelida; Clitellata;
OC   Oligochaeta; Enchytraeida; Enchytraeidae; Enchytraeus.
OX   NCBI_TaxID=34589;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=8806602; DOI=10.1006/bbrc.1996.1321;
RA   Willuhn J., Schmitt-Wrede H.-P., Otto A., Wunderlich F.;
RT   "Cadmium-detoxification in the earthworm Enchytraeus: specific expression
RT   of a putative aldehyde dehydrogenase.";
RL   Biochem. Biophys. Res. Commun. 226:128-134(1996).
CC   -!- FUNCTION: Could be indirectly involved in cadmium-detoxification, by
CC       lowering the intracellular concentrations of aldehydes.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- PATHWAY: Alcohol metabolism; ethanol degradation; acetate from ethanol:
CC       step 2/2.
CC   -!- INDUCTION: By cadmium.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X95396; CAA64680.1; -; mRNA.
DR   PIR; JC4924; JC4924.
DR   AlphaFoldDB; Q27640; -.
DR   SMR; Q27640; -.
DR   UniPathway; UPA00780; UER00768.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..497
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000056430"
FT   ACT_SITE        266
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        300
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         243..248
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            167
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  54159 MW;  A35A562876808BCC CRC64;
     MSAPKIPEPV KDLKVEFTKI FINNEFVDSV SGKTFATINP STGEKLAEVQ EGDKADIDKA
     VAAARAAFKR DAEYRKHDAS DRGRLLFKLA DLIEAHRVQL RTLETLDNGK PFAMSYLGDT
     LMAQKVLRYY AGFADKIVGQ TIPADGNVFC YTRHEPVGVV GAITPWNFPL HLAASKIAPA
     IAAGCTLVLK PAEQTPLTAL YLASLVKQAG FPAGVINIVP GLGHTAGAAL TNHPDINKIT
     FTGSTEVGQL IIQGSGKTNL KRVTLELGGK SPNIIFPDSD LDYAVEVSHQ AIMANMGQVC
     CAGSRTFVHE DIYEEFVRRS VERAKKRTVG DPFDPKNENG PQVDETQLKK ILELIESGKT
     EGAKLECGGK RLGDKGYFVE PTVFTDVTSS MRVAKEEIFG PVQLIFKFKD VDEVIERAND
     TSYGLAAAVF TKNIDTALKV ANSLEAGTVW VNTYNHFAFQ APFGGYKMSG QGREFGHYGL
     EAFLEVKTVY VRTPTKL