BADH_BETVU
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 03-AUG-2022, entry version 105.
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 PRIDE; P28237; -.
DR EnsemblPlants; KMT10501; KMT10501; BVRB_5g116250.
DR Gramene; KMT10501; KMT10501; BVRB_5g116250.
DR UniPathway; UPA00529; UER00386.
DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; 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 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
