ID   BADH_HORVU              Reviewed;         505 AA.
AC   Q40024;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Betaine aldehyde dehydrogenase;
DE            Short=BADH;
DE            EC=1.2.1.8;
OS   Hordeum vulgare (Barley).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Hordeinae; Hordeum.
OX   NCBI_TaxID=4513;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7888620; DOI=10.1007/bf00020185;
RA   Ishitani M., Nakamura T., Han S.Y., Takabe T.;
RT   "Expression of the betaine aldehyde dehydrogenase gene in barley in
RT   response to osmotic stress and abscisic acid.";
RL   Plant Mol. Biol. 27:307-315(1995).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.8;
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine from betaine aldehyde: step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; D26448; BAA05466.1; -; mRNA.
DR   PIR; S71413; S71413.
DR   AlphaFoldDB; Q40024; -.
DR   SMR; Q40024; -.
DR   BioCyc; MetaCyc:MONOMER-16787; -.
DR   UniPathway; UPA00529; UER00386.
DR   ExpressionAtlas; Q40024; baseline and differential.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0071454; P:cellular response to anoxia; IEA:EnsemblPlants.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   CDD; cd07110; ALDH_F10_BADH; 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   PANTHER; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43860:SF7; BETAINE ALDEHYDE DEHYDROGENASE 1; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   2: Evidence at transcript level;
KW   NAD; Oxidoreductase; Peroxisome.
FT   CHAIN           1..505
FT                   /note="Betaine aldehyde dehydrogenase"
FT                   /id="PRO_0000056529"
FT   MOTIF           503..505
FT                   /note="Microbody targeting signal"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        261
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        296
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         239..244
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            163
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   505 AA;  54290 MW;  C30B40FF22413BB6 CRC64;
     MAAPPAIPRR GLFIGGGWRE PTLGRHIPVI NPATEDTIGD IPAATAEDVE LAVAAGGPVL
     ARRREPWARA SGATRAKYLN AIAAKITGKI AYLALLETVD SGKPKDEAVA DMDDVAACFE
     YYAALAEALD GKQHAPISLP MEEFKTYVLK EPIGVVGLIT PWNYPLLMAT WKVAPALAAG
     CTAVLKPSEL ASLTCLELGA ICEEIGLPSG VLNIITGLGP DAGAPIASHP HVDKIAFTGS
     TATGKTIMTA AAQMVKPVSL ELGGKSPLVT FDDVADIDKA VEWPMLGCFF NGGQVCSATS
     RLLLHEKIAE PFLDRLVEWA KNIKISDPLE EGCRLGSVIS KGQYEQIKKF ISTARSEGAT
     ILHGGDRPKH LGKGFFIEPT INTGVSTSMQ IWREEVFGPV ICVKVFKTES EAVELANDTH
     YGLAGGVISD DLERCERIAK VIHSGIVWKN CSQPTLVQAP WGGNKRSGFG RELGEWGLEN
     YLSVKQVTRY CKDELYGWYQ RPSKL
//