ID   ALDH_AGABI              Reviewed;         500 AA.
AC   O74187;
DT   11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            Short=ALDDH;
DE            Short=ALDH;
DE            EC=1.2.1.3;
GN   Name=aldA;
OS   Agaricus bisporus (White button mushroom).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Horst H39;
RA   Schaap P.J., Mueller Y., Visser J.;
RT   "Molecular structure and spatial expression of housekeeping genes in
RT   mushrooms.";
RL   Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
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   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; Y17825; CAA76875.1; -; Genomic_DNA.
DR   AlphaFoldDB; O74187; -.
DR   SMR; O74187; -.
DR   PRIDE; O74187; -.
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; IPR016160; Ald_DH_CS_CYS.
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; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   NAD; Oxidoreductase.
FT   CHAIN           1..500
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000056435"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         246..251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            170
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  54395 MW;  C4FCE58B50855925 CRC64;
     MPSIFTHQWD TPVYKGSTSI NTGLFINGEF VDGVKNTTID VVNPANGKLI TKISEATEAD
     IDIAVEAAHK AFETTWGLNC SGSKRGDMLY KLAQLMEKNI DDLSAIEALD NGKTFLWAKS
     VDLSLSISTI KHYAGWADKN FGQVIETDEK KLTYSRHEPI GVVGQIIPWN FPLLMLAWKI
     GPALATGNCI VLKPSEFTPL SALRMCALIQ EAGFPPGVVN VVTGYGSTTG QAISSHMKID
     KVAFTGSTLV GRKVMEAAAK SNLKNVTLEL GGKSPVVIFD DADLEQSVNW TAHGLFWNHG
     QACCAGTRIF VQEGIYDKFL QKFTDKIKEI KLGDPFGLGI DQGPQVSQIQ YDRIMSYIES
     GRAEGATVHV GGERHGNEGY FIQPTIFTDT TPDMKIVKEE IFGPVGAVIK FKDGKEVIKQ
     ANDSNYGLAA AVFSQDINKA IETAHAFKAG TAWVNCANTI DAGVPFGGYK QSGIGRELGE
     YALHNYTNVK AVHVNLNWKM