Reviewed, UniProtKB/Swiss-Prot Q8VXQ2 (ALDH_CRAPL)

Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase
    EC=1.2.1.3
Alternative name(s):
    Cp-ALDH

Gene names

Name:

ALDH

Organism

Craterostigma plantagineum

Taxonomic identifier

4153 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › lamiids › Lamiales › Linderniaceae › Craterostigma

Protein attributes

Sequence length	479 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 = an acid + NADH.
Subcellular location	Plastid › amyloplast. Plastid › chloroplast. 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 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 process	Stress response
Cellular component	Amyloplast Chloroplast Plastid
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	cellular aldehyde metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	amyloplast Inferred from electronic annotation. Source: UniProtKB-SubCell chloroplast Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 479	479	Aldehyde dehydrogenase		PRO_0000256068
Regions
	Nucleotide binding	190 – 195	6	NAD By similarity
Sites
	Active site	212	1	Proton acceptor By similarity
	Active site	247	1	Nucleophile By similarity
	Site	117	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8VXQ2-1 [UniParc]. Last modified March 1, 2002. Version 1. Checksum: 47F266AE6CF77FCE	FASTA	479	52,741
	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

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: 11849595] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, INDUCTION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ306960 mRNA. Translation: CAC84900.1.
3D structure databases
HSSP	HSSP built from PDB template 1AD3 based on UniProtKB P11883.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.2.1.3. 280962.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR012394. Aldehyde_DH_NAD(P). [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit. PTHR11699:SF15. ALDH. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF036492. ALDH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALDH_CRAPL

Accession

Primary (citable) accession number: Q8VXQ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	March 1, 2002
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)