[1]	NUCLEOTIDE SEQUENCE [MRNA]. DOI=10.1007/BF00018451; PubMed=1731961 [NCBI, ExPASy, EBI, Israel, Japan] McCue K.F., Hanson A.D.; "Salt-inducible betaine aldehyde dehydrogenase from sugar beet: cDNA cloning and expression."; Plant Mol. Biol. 18:1-11(1992).

Comments

CATALYTIC ACTIVITY: Betaine aldehyde + NAD⁺ + H₂O = betaine + NADH.
PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1 .
SUBUNIT: Homodimer.
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X58463; CAA41377.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X58462; CAA41376.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S19135; S19135.

3D structure databases

HSSP

P05091; 1O02. [HSSP ENTRY / PDB]

ModBase

P28237.

Ontologies

GO:0008802;	Molecular function: betaine-aldehyde dehydrogenase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chloroplast; NAD; Oxidoreductase; Plastid; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`1 7`	`7`	`Chloroplast (Potential).`
`CHAIN`	`8 500`	`493`	`Betaine aldehyde dehydrogenase, chloroplastic.`	`PRO_0000007181`
`NP_BIND`	`238 243`	`6`	`NAD (By similarity).`
`ACT_SITE`	`260 260`		`Proton acceptor (By similarity).`
`ACT_SITE`	`294 294`		`Nucleophile (By similarity).`
`SITE`	`162 162`	`1`	`Transition state stabilizer (By similarity).`
`VARIANT`	`412 412`	`1`	`E -> D.`

Sequence information

Length: 500 AA [This is the length of the unprocessed precursor]

Molecular weight: 54721 Da [This is the MW of the unprocessed precursor]

CRC64: 512859FBC27B67B8 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSMPIPSRQL FIDGEWREPI KKNRIPIINP SNEEIIGDIP AGSSEDIEVA VAAARRALKR 

        70         80         90        100        110        120 
NKGREWAATS GAHRARYLRA IAAKVTERKD HFVKLETIDS GKPFDEAVLD IDDVATCFEY 

       130        140        150        160        170        180 
FAGQAEAMDA KQKAPVTLPM ERFKSHVLRQ PIGVVGLITP WNYPLLMATW KIAPALAAGC 

       190        200        210        220        230        240 
TAVLKPSELA SITCLEFGEV CNEVGLPPGV LNIVTGLGPD AGAPLAAHPD VDKVAFTGSS 

       250        260        270        280        290        300 
ATGSKVMASA AQLVKPVTLE LGGKSPIIVF EDVDIDQVVE WTMFGCFWTN GQICSATSRL 

       310        320        330        340        350        360 
LVHESIAAEF IDRLVKWTKN IKISDPFEEG CRLGPVISKG QYDKIMKFIS TAKSEGATIL 

       370        380        390        400        410        420 
CGGSRPEHLK KGYFIEPTII SDISTSMQIW REEVFGPVLC VKTFSSEDEA LELANDTEYG 

       430        440        450        460        470        480 
LASAVFSKDL ERCERVSKLL ESGAVWVNCS QPCFVHAPWG GIKRSGFGRE LGEWGIENYL 

       490        500 
NIKQVTSDIS NEPWGWYKSP

P28237 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools