ID   ALDH_ASPNG              Reviewed;         497 AA.
AC   P41751;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            Short=ALDDH;
DE            Short=ALDH;
DE            EC=1.2.1.3;
GN   Name=aldA;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2606357; DOI=10.1016/0378-1119(89)90152-2;
RA   O'Connell M.J., Kelly J.M.;
RT   "Physical characterization of the aldehyde-dehydrogenase-encoding gene of
RT   Aspergillus niger.";
RL   Gene 84:173-180(1989).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M32351; AAA87596.1; -; Genomic_DNA.
DR   AlphaFoldDB; P41751; -.
DR   SMR; P41751; -.
DR   STRING; 5061.CADANGAP00006922; -.
DR   PRIDE; P41751; -.
DR   VEuPathDB; FungiDB:An08g07290; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1148193; -.
DR   VEuPathDB; FungiDB:ATCC64974_100780; -.
DR   VEuPathDB; FungiDB:M747DRAFT_264904; -.
DR   eggNOG; KOG2450; Eukaryota.
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..497
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000056436"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        299
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         242..247
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            166
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   497 AA;  53809 MW;  47CA353FFD8A50E8 CRC64;
     MSDLFATITT PNGVKYEQPL GLFIDGEFVK GAEGKTFETI NPSNEKPIVA VHEATEKDVD
     TAVAAARKAF EGSWRQVTPS TRGRMLTKLA DLFERDAEIL ASIEALDNGK SITMAHGDIA
     GAAGCLRYYG GWADKIHGQT IDTNSETLNY TRHEPIGVCG QIIPWNFPLL MWAWKIGPAI
     ATGNTVVIKT AEQTPLSGLY AANVIKEAGI PAGVVNVISG FGRVAGSAIS HHMDIDKVAF
     TGSTLVGRTI LQAAAKSNLK KVTLELGGKS PNIVFNDADI DNAISWANFG IFYNHGQCCC
     AGSRILVQEG IYDKFIARLK ERALQNKVGD PFAKDTFQGP QVSQLQFDRI MEYIQHGKDA
     GATVAVGGER HGTEGYFIQP TVFTDVTSDM KINQEEIFGP VVTVQKFKDV EDAIKIGNST
     SYGLAAGIHT KDVTTAIRVS NALRAGTVWV NSYNLIQYQV PFGGFKESGI GRELGSYALE
     NYTQIKAVHY RLGDALF