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UniProtKB/Swiss-Prot entry Q8VXQ2

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDH_CRAPL
Primary accession number Q8VXQ2
Secondary accession numbers None
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on March 1, 2002 (Sequence version 1)
Annotations were last modified on    July 22, 2008 (Entry version 25)
Name and origin of the protein
Protein name Aldehyde dehydrogenase
Synonyms EC 1.2.1.3
Cp-ALDH
Gene name
Name: ALDH
From
Craterostigma plantagineum [TaxID: 4153] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; asterids; lamiids; Lamiales; Linderniaceae; Craterostigma.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND INDUCTION.
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:   KM=2.2 µM for nonanal;
    KM=267 µM for propionaldehyde;
    KM=32.3 mM for acetaldehyde;
    Vmax=0.03 µmol/sec/mg enzyme with nonanal as substrate;
    Vmax=0.196 µmol/sec/mg enzyme with propionaldehyde as substrate;
    Vmax=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
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from electronic annotation from EC).
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.
BLOCKS Q8VXQ2.
Other
ProtoNet Q8VXQ2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Amyloplast; Chloroplast; NAD; Oxidoreductase; Plastid; Stress response.
Features
SEVIEWER logo Feature table viewer
KeyFrom   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

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