ID   BADH_BETVU              Reviewed;         500 AA.
AC   P28237;
DT   01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-1992, sequence version 1.
DT   27-MAR-2024, entry version 110.
DE   RecName: Full=Betaine aldehyde dehydrogenase, chloroplastic;
DE            Short=BADH;
DE            EC=1.2.1.8;
DE   Flags: Precursor;
OS   Beta vulgaris (Sugar beet).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Chenopodiaceae; Betoideae; Beta.
OX   NCBI_TaxID=161934;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1731961; DOI=10.1007/bf00018451;
RA   McCue K.F., Hanson A.D.;
RT   "Salt-inducible betaine aldehyde dehydrogenase from sugar beet: cDNA
RT   cloning and expression.";
RL   Plant Mol. Biol. 18:1-11(1992).
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.
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; X58463; CAA41377.1; -; mRNA.
DR   EMBL; X58462; CAA41376.1; -; mRNA.
DR   PIR; S19135; S19135.
DR   AlphaFoldDB; P28237; -.
DR   SMR; P28237; -.
DR   EnsemblPlants; KMT10501; KMT10501; BVRB_5g116250.
DR   Gramene; KMT10501; KMT10501; BVRB_5g116250.
DR   OMA; NMIYGEG; -.
DR   UniPathway; UPA00529; UER00386.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0019145; F:aminobutyraldehyde dehydrogenase activity; IEA:UniProt.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0110095; P:cellular detoxification of aldehyde; IEA:UniProt.
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:SF2; BETAINE ALDEHYDE DEHYDROGENASE-RELATED; 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   Chloroplast; NAD; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT         1..7
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           8..500
FT                   /note="Betaine aldehyde dehydrogenase, chloroplastic"
FT                   /id="PRO_0000007181"
FT   ACT_SITE        260
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   ACT_SITE        294
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10007,
FT                   ECO:0000255|PROSITE-ProRule:PRU10008"
FT   BINDING         238..243
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            162
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   VARIANT         412
FT                   /note="E -> D"
SQ   SEQUENCE   500 AA;  54721 MW;  512859FBC27B67B8 CRC64;
     MSMPIPSRQL FIDGEWREPI KKNRIPIINP SNEEIIGDIP AGSSEDIEVA VAAARRALKR
     NKGREWAATS GAHRARYLRA IAAKVTERKD HFVKLETIDS GKPFDEAVLD IDDVATCFEY
     FAGQAEAMDA KQKAPVTLPM ERFKSHVLRQ PIGVVGLITP WNYPLLMATW KIAPALAAGC
     TAVLKPSELA SITCLEFGEV CNEVGLPPGV LNIVTGLGPD AGAPLAAHPD VDKVAFTGSS
     ATGSKVMASA AQLVKPVTLE LGGKSPIIVF EDVDIDQVVE WTMFGCFWTN GQICSATSRL
     LVHESIAAEF IDRLVKWTKN IKISDPFEEG CRLGPVISKG QYDKIMKFIS TAKSEGATIL
     CGGSRPEHLK KGYFIEPTII SDISTSMQIW REEVFGPVLC VKTFSSEDEA LELANDTEYG
     LASAVFSKDL ERCERVSKLL ESGAVWVNCS QPCFVHAPWG GIKRSGFGRE LGEWGIENYL
     NIKQVTSDIS NEPWGWYKSP
//