ID   AL7A1_BRANA             Reviewed;         494 AA.
AC   Q41247;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Aldehyde dehydrogenase family 7 member A1;
DE            EC=1.2.1.3;
DE   AltName: Full=Antiquitin-1;
DE   AltName: Full=Brassica turgor-responsive/drought-induced gene 26 protein;
DE            Short=Btg-26;
GN   Name=BTG-26;
OS   Brassica napus (Rape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=3708 {ECO:0000312|EMBL:AAB33843.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RC   STRAIN=cv. Bridger; TISSUE=Leaf;
RX   PubMed=7894018; DOI=10.1007/bf00019320;
RA   Stroeher V.L., Boothe J.G., Good A.G.;
RT   "Molecular cloning and expression of a turgor-responsive gene in Brassica
RT   napus.";
RL   Plant Mol. Biol. 27:541-551(1995).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 2-16.
RX   PubMed=11959129; DOI=10.1016/s0014-5793(02)02553-x;
RA   Tang W.-K., Cheng C.H.K., Fong W.-P.;
RT   "First purification of the antiquitin protein and demonstration of its
RT   enzymatic activity.";
RL   FEBS Lett. 516:183-186(2002).
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   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:P83402}.
CC   -!- INDUCTION: By water stress, low temperature, heat shock, high salt and
CC       abscisic acid. {ECO:0000269|PubMed:7894018}.
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; S77096; AAB33843.1; -; Genomic_DNA.
DR   PIR; S53503; S53503.
DR   AlphaFoldDB; Q41247; -.
DR   SMR; Q41247; -.
DR   PRIDE; Q41247; -.
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   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   InterPro; IPR044638; ALDH7A1-like.
DR   PANTHER; PTHR43521; PTHR43521; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; NAD; Oxidoreductase; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:11959129"
FT   CHAIN           2..494
FT                   /note="Aldehyde dehydrogenase family 7 member A1"
FT                   /id="PRO_0000056496"
FT   ACT_SITE        269
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   ACT_SITE        303
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT   BINDING         247..252
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            168
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   494 AA;  52688 MW;  13ED0096563BAE13 CRC64;
     MGSASKEYEF LSEIGLSSSH NLGNYVGGKW LGNGPLVSTL NPANNQVLPI AQVVEASLED
     YEIGLKACEE AAKTWMQVPA PKRGDIVRQI GDALRSKLDY LGRLLSLEMG KILAEGIGEV
     QEVIDMCDFA VGLSRQLNGS VIPSERPNHM MLEMWNPLGI VGVITAFNFP CAVLGWNACI
     ALVCGNCVVW KGAPTTPLIT IAMTKLVAEV LEKNHLPGAI FTAMCGGAEI GEAIAKDTRI
     PLVSFTGSSK VGLTVQQTVS ARSGKTLLEL SGNNAIIVMD DADIQLAARS VLFAAVGTAG
     QRCTTCRRLL LHESVYDKVL EQLLTSYKQV KIGDPLEKGT LLGPLHTPES KKNFEKGIEV
     IKSQGGKVLT GGKAVEGEGN FVEPTIIEIS SDAAVVKEEL FAPVLYALKF KTFEEAVAIN
     NSVPQGLSSS IFTRSPDNIF KWIGPMGSDC GIVNVNIPTN GAEIGGAFGG EKATGGGREA
     GSDSWKQYMR RSTW