BADH_ATRHO
ID BADH_ATRHO Reviewed; 502 AA.
AC P42757;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Betaine aldehyde dehydrogenase, chloroplastic;
DE Short=BADH;
DE EC=1.2.1.8;
DE Flags: Precursor;
OS Atriplex hortensis (Mountain spinach).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC Caryophyllales; Chenopodiaceae; Chenopodioideae; Atripliceae; Atriplex.
OX NCBI_TaxID=34272;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Leaf, and Stem;
RA Xiao G., Zhang G., Liu F., Chen S.;
RT "cDNA and partial genomic DNA sequence of Mountain spinach (Atriplex
RT hortenis) betaine aldehyde dehydrogenase (BADH).";
RL Chin. Sci. Bull. 40:741-745(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: Plastid, chloroplast.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; X69770; CAA49425.1; -; mRNA.
DR EMBL; X69772; CAA49427.1; -; Genomic_DNA.
DR PIR; S49205; S49205.
DR AlphaFoldDB; P42757; -.
DR SMR; P42757; -.
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..502
FT /note="Betaine aldehyde dehydrogenase, chloroplastic"
FT /id="PRO_0000007180"
FT ACT_SITE 262
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 240..245
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 164
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 55271 MW; 54F1A05EBBC4281E CRC64;
MAFPIPARQL FIDGEWREPL LKNRIPIINP STEEIIGDIP AATAEDVEVA VVAARKAFKR
NKGRDWAALW SHRAKYLRAI AAKITEKKDH FVKLETLDSG KPRDEAVLDI DDVATCFEYF
EYFAGQAEAL DAKQKAPVTL PMERFKSHVL RQPIGVVGLI SPWNYPLLMD TWKIAPALAA
GCTTVLKPSE LASVTCLEFG EVCNEVGLPP GVLNILTGLG PDAGAPIVSH PDIDKVAFTG
SSATGSKIMA SAAQLVKPVT LELGGKSPVI MFEDIDIETA VEWTLFGVFW TNGQICSATS
RLLVHESIAA EFVDRMVKWT KNIKISDPFE EGCRLGPVIS KGQYDKIMKF ISTAKSEGAT
ILCGGSRPEH LKKGYYIEPT IITDITTSMQ IWKEEVFGPV ICVKTFKTED EAIELANDTE
YGLAGAVFSK DLERCERVTK ALEVGAVWVN CSQPCFVHAP WGGVKRSGFG RELGEWGIEN
YLNIKQVTSD ISDEPWGWYK SP
