ID   BADH_AMAHP              Reviewed;         501 AA.
AC   O04895;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Betaine aldehyde dehydrogenase, chloroplastic;
DE            Short=BADH;
DE            EC=1.2.1.8;
DE   Flags: Precursor;
GN   Name=BADH4;
OS   Amaranthus hypochondriacus (Prince-of-Wales feather) (Amaranthus hybridus
OS   var. hypochondriacus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   Caryophyllales; Amaranthaceae; Amaranthus.
OX   NCBI_TaxID=28502;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   TISSUE=Leaf;
RX   PubMed=9751804; DOI=10.1016/s0378-1119(98)00381-3;
RA   Legaria J., Rajsbaum R., Munoz-Clares R.A., Villegas-Sepulveda N.,
RA   Simpson J., Iturriaga G.;
RT   "Molecular characterization of two genes encoding betaine aldehyde
RT   dehydrogenase from amaranth. Expression in leaves under short-term exposure
RT   to osmotic stress or abscisic acid.";
RL   Gene 218:69-76(1998).
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: Plastid, chloroplast.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AF000132; AAB58165.1; -; Genomic_DNA.
DR   AlphaFoldDB; O04895; -.
DR   SMR; O04895; -.
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   3: Inferred from homology;
KW   Chloroplast; NAD; Oxidoreductase; Plastid; Transit peptide.
FT   TRANSIT         1..7
FT                   /note="Chloroplast"
FT                   /evidence="ECO:0000255"
FT   CHAIN           8..501
FT                   /note="Betaine aldehyde dehydrogenase, chloroplastic"
FT                   /id="PRO_0000007178"
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"
SQ   SEQUENCE   501 AA;  54504 MW;  D5065A91BFC0D37E CRC64;
     MAIRVPSRQL FIDGEWREPI KKNRIPIINP STEEIIGDIP AATAEDVELA VAAARRALKR
     NKGEDWASAS GAHRAKYLRA IAAKITEKKD YFAKLEAMDC GKPLDEAARD IDDVAGCFEY
     YADQAEALDA KQKAPIALPM DTFKCHVLKQ PIGVVGLISP WNYPLLMATW KVAPALAAGC
     SAVLKPSELA SVTCLELAEV CREVGLPPGV LNILTGLGPE AGGPLACHPD VDKVAFTGST
     ATGSKVMSSA AQLVKPVTLE LGGKSPIVIF EDVDLDKAAE WTAFGCFWTN GQICSATSRL
     LVHESIAAEF LDRLVKWCKN IKISDPFEEG CRLGPVVSKS QYEKVLKFIS TAKSEGATIL
     CGGSRPEHLK KGYYVEPTII SDVSTSMQIW REEVFGPVLC QKTFGSEDEA IELANDTQYG
     LGAAVLSKDL DRCERITKAL EVGAVWVNCS QPCFTQAPWG GTKRSGFGRE LGEWGIENYL
     NIKQVTRDTS TDEPWGWYKS P
//