ID BADH_SPIOL Reviewed; 497 AA. AC P17202; P93555; DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1990, sequence version 1. DT 16-JUN-2009, entry version 68. DE RecName: Full=Betaine aldehyde dehydrogenase, chloroplastic; DE Short=BADH; DE EC=1.2.1.8; DE Flags: Precursor; OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; OC Caryophyllales; Amaranthaceae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC STRAIN=cv. Savoy hybrid 612; RX MEDLINE=90207274; PubMed=2320587; DOI=10.1073/pnas.87.7.2745; RA Weretilnyk E.A., Hanson A.D.; RT "Molecular cloning of a plant betaine-aldehyde dehydrogenase, an RT enzyme implicated in adaptation to salinity and drought."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2745-2749(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Shu W., Ai W., Chen S.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: Betaine aldehyde + NAD(+) + H(2)O = betaine + CC NADH. CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis CC via 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 ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; M31480; AAA34025.1; -; mRNA. DR EMBL; U69142; AAB41696.1; -; Genomic_DNA. DR PIR; A35994; A35994. DR PIR; T51173; T51173. DR HSSP; P51977; 1BXS. DR BRENDA; 1.2.1.8; 286. DR GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:EC. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR InterPro; IPR016160; Ald_DH_CS. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH. DR Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1. DR PANTHER; PTHR11699; Aldehyde_dehyd; 1. DR Pfam; PF00171; Aldedh; 1. DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1. DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 1: Evidence at protein level; KW Chloroplast; Direct protein sequencing; NAD; Oxidoreductase; Plastid; KW Transit peptide. FT TRANSIT 1 7 Chloroplast (Potential). FT CHAIN 8 497 Betaine aldehyde dehydrogenase, FT chloroplastic. FT /FTId=PRO_0000007182. FT NP_BIND 235 240 NAD (By similarity). FT ACT_SITE 257 257 Proton acceptor (By similarity). FT ACT_SITE 291 291 Nucleophile (By similarity). FT SITE 159 159 Transition state stabilizer (By FT similarity). FT MOD_RES 8 8 Blocked amino end (Arg). FT CONFLICT 424 424 S -> F (in Ref. 2; AAB41696). SQ SEQUENCE 497 AA; 54270 MW; 55088240E635B22F CRC64; MAFPIPARQL FIDGEWREPI KKNRIPVINP STEEIIGDIP AATAEDVEVA VVAARRAFRR NNWSATSGAH RATYLRAIAA KITEKKDHFV KLETIDSGKP FDEAVLDIDD VASCFEYFAG QAEALDGKQK APVTLPMERF KSHVLRQPLG VVGLISPWNY PLLMATWKIA PALAAGCTAV LKPSELASVT CLEFGEVCNE VGLPPGVLNI LTGLGPDAGA PLVSHPDVDK IAFTGSSATG SKVMASAAQL VKPVTLELGG KSPIVVFEDV DIDKVVEWTI FGCFWTNGQI CSATSRLLVH ESIAAEFVDK LVKWTKNIKI SDPFEEGCRL GPVISKGQYD KIMKFISTAK SEGATILYGG SRPEHLKKGY YIEPTIVTDI STSMQIWKEE VFGPVLCVKT FSSEDEAIAL ANDTEYGLAA AVFSNDLERC ERITKALEVG AVWVNCSQPC FVQAPWGGIK RSGFGRELGE WGIQNYLNIK QVTQDISDEP WGWYKSP //