ID   ALDHY_YEASX             Reviewed;         511 AA.
AC   P32872;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Aldehyde dehydrogenase 2, mitochondrial;
DE            EC=1.2.1.3;
DE   Flags: Precursor;
GN   Name=ALD2; Synonyms=ALDH2;
OS   Saccharomyces cerevisiae (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=4932;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Thielen J.;
RL   Thesis (1993), Heinrich-Heine University / Duesseldorf, Germany.
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   -!- SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
CC   -!- CAUTION: Is not present in yeast genome. {ECO:0000305}.
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DR   EMBL; Z17314; CAA78962.1; -; Genomic_DNA.
DR   PIR; S31308; S31308.
DR   AlphaFoldDB; P32872; -.
DR   SMR; P32872; -.
DR   PRIDE; P32872; -.
DR   VEuPathDB; FungiDB:YER073W; -.
DR   UniPathway; UPA00780; UER00768.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
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:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
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   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 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   Mitochondrion; NAD; Oxidoreductase; Transit peptide.
FT   TRANSIT         1..21
FT                   /note="Mitochondrion"
FT   CHAIN           22..511
FT                   /note="Aldehyde dehydrogenase 2, mitochondrial"
FT                   /id="PRO_0000007164"
FT   REGION          72..92
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        297
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        331
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         274..279
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            198
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   511 AA;  56466 MW;  70EDAE951B84EE4A CRC64;
     MSKSKTKTDK RNQSSLSRIK LSALHYCMSD AEPSIAYLQD NSAFINNEWH NLVLEKIFPV
     YNPSTEEDIT QVSEKSQHDS TEEDITQVSE KSQHDDDKAV VDISERGRLL NILADLIERD
     RDILAAIEHL DNGKPFDEAY LLDLASVLKE LRYTAGWADK LHGTLRFAIT IPTFQDLRFL
     RYTRHEPVGV CGEIIPWNIP LLMYIWKIGP ALAAGNTVVL KPEELTPLTA LTVATLIKEA
     GFPPGVVNVV SGYGPTAGAA CLSHKDNDKL AFTGSTLVGK VVMKAAAKSN LKKVTLELGG
     KSPMIVFIDA DLDWAVENAH FGVFFNQGQC CIAQSRITVH ESIYDEIVER DLEKAKKQVL
     GNPFESDTRY GPQILKIEFD SIPRLINSAK AEGAKVLCGG GRDDSCVGYY IQPTVFADVT
     DEMRIAKEEI FGPVITISRF KSVDEAIKRV DNTKYGLAAY VFTKDKAIRI SAALKAGTVW
     VNCVHVASYQ IPFGGNKNSG MGRELGEYGL E