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Q8VXQ2 (ALDH_CRAPL) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase

EC=1.2.1.3
Alternative name(s):
Cp-ALDH
Gene names
Name:ALDH
OrganismCraterostigma plantagineum (Blue gem) (Torenia plantagineum)
Taxonomic identifier4153 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsLamialesLinderniaceaeCraterostigma

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidizes nonanal, propionaldehyde and acetaldehyde in vitro, in the following decreasing order of reactivity: nonanal, propionaldehyde, acetaldehyde. Ref.1

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Subcellular location

Plastidamyloplast. Plastidchloroplast Ref.1.

Induction

By abscisic acid (ABA) and dehydration. Ref.1

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

Measured at pH 9.5 for all experiments.

KM=2.2 µM for nonanal Ref.1

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

Ontologies

Keywords
   Biological processStress response
   Cellular componentAmyloplast
Chloroplast
Plastid
   LigandNAD
   Molecular functionOxidoreductase
Gene Ontology (GO)
   Biological_processcellular aldehyde metabolic process

Inferred from electronic annotation. Source: InterPro

response to stress

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentamyloplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

chloroplast

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

aldehyde dehydrogenase [NAD(P)+] activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 479479Aldehyde dehydrogenase
PRO_0000256068

Regions

Nucleotide binding190 – 1956NAD By similarity

Sites

Active site2121Proton acceptor By similarity
Active site2471Nucleophile By similarity
Site1171Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8VXQ2 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 47F266AE6CF77FCE

FASTA47952,741
        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 

« Hide

References

[1]"Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma plantagineum and Arabidopsis thaliana."
Kirch H.-H., Nair A., Bartels D.
Plant J. 28:555-567(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ306960 mRNA. Translation: CAC84900.1.

3D structure databases

ProteinModelPortalQ8VXQ2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036492. ALDH. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
ProtoNetSearch...

Entry information

Entry nameALDH_CRAPL
AccessionPrimary (citable) accession number: Q8VXQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: March 1, 2002
Last modified: June 11, 2014
This is version 51 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families