NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
DOI=10.1046/j.1365-313X.2001.01176.x; PubMed=11849595 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Nair A., Bartels D.;
"Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma plantagineum and Arabidopsis thaliana.";
Plant J. 28:555-567(2001).

Comments

FUNCTION: Oxidizes nonanal, propionaldehyde and acetaldehyde in vitro, in the following decreasing order of reactivity: nonanal, propionaldehyde, acetaldehyde.
CATALYTIC ACTIVITY: An aldehyde + NAD⁺ + H₂O = an acid + NADH.

BIOPHYSICOCHEMICAL PROPERTIES:

Kinetic parameters:	K_M=2.2 µM for nonanal;
	K_M=267 µM for propionaldehyde;
	K_M=32.3 mM for acetaldehyde;
	V_max=0.03 µmol/sec/mg enzyme with nonanal as substrate;
	V_max=0.196 µmol/sec/mg enzyme with propionaldehyde as substrate;
	V_max=0.102 µmol/sec/mg enzyme with acetaldehyde as substrate;
	Note=Measured at pH 9.5 for all experiments;

SUBCELLULAR LOCATION: Plastid, amyloplast. Plastid, chloroplast.
INDUCTION: By abscisic acid (ABA) and dehydration.
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

AJ306960; CAC84900.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P11883; 1AD3. [HSSP ENTRY / PDB]

ModBase

Q8VXQ2.

Ontologies

GO:0009501;	Cellular component: amyloplast (inferred from electronic annotation from UniProtKB-KW).
GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0004029;	Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from electronic annotation from EC).
GO:0004030;	Molecular function: aldehyde dehydrogenase [NAD(P)+] activity (inferred from electronic annotation from InterPro).
GO:0006081;	Biological process: cellular aldehyde metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
GO:0006950;	Biological process: response to stress (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR012394; Ald_DHase_NAD(P).
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF15; ALDH; 1.

Pfam

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

PIRSF

PIRSF036492; ALDH; 1.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; FALSE_NEG.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.

ProtoNet

Q8VXQ2.

Other

UniRef

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

Keywords

Amyloplast; Chloroplast; NAD; Oxidoreductase; Plastid; Stress response.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 479`	`479`	`Aldehyde dehydrogenase.`	`PRO_0000256068`
`NP_BIND`	`190 195`	`6`	`NAD (By similarity).`
`ACT_SITE`	`212 212`		`Proton acceptor (By similarity).`
`ACT_SITE`	`247 247`		`Nucleophile (By similarity).`
`SITE`	`117 117`	`1`	`Transition state stabilizer (By similarity).`

Sequence information

Length: 479 AA [This is the length of the unprocessed precursor]

Molecular weight: 52741 Da [This is the MW of the unprocessed precursor]

CRC64: 47F266AE6CF77FCE [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSQVDAEGVV DGLRRTYISG KTKSYEWRVS QLKALLKITT HHDKEVVEAL RADLKKPEHE 

        70         80         90        100        110        120 
AYVHEIFMVS NACKSALKEL HQWMKPQKVK TSLATYPSSA EIVSEPLGVV LVITAWNYPF 

       130        140        150        160        170        180 
LLALDPMIGA IAAGNCVVLK PSEIAPATSA LLAKLLNQYV DTSAIRVVEG AVPEMQALLD 

       190        200        210        220        230        240 
QRWDKIFYTG SSKVGQIVLS SAAKHLTPVV LELGGKCPTV VDANIDLKVA ARRIISWKWS 

       250        260        270        280        290        300 
GNSGQTCISP DYIITTEENA PKLVDAIKCE LESFYGKDPL KSQDMSSIIN ERQFERMTGL 

       310        320        330        340        350        360 
LDDKKVSDKI VYGGQSDKSN LKIAPTILLD VSEDSSVMSE EIFGPLLPII TVGKIEECYK 

       370        380        390        400        410        420 
IIASKPKPLA AYLFTNDKKR TEEFVSNVSA GGITINDIAL HFLEPRLPFG GVGESGMGSY 

       430        440        450        460        470 
HGKFSFDAFS HKKSVLKRSF GGEVAARYPP YAPWKLHFME AILQGDIFGL LKAWLGWSS

Q8VXQ2 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