ID   ALDH_CRAPL              Reviewed;         479 AA.
AC   Q8VXQ2;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Aldehyde dehydrogenase;
DE            EC=1.2.1.3;
DE   AltName: Full=Cp-ALDH;
GN   Name=ALDH;
OS   Craterostigma plantagineum (Blue gem) (Torenia plantagineum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Lamiales; Linderniaceae; Craterostigma.
OX   NCBI_TaxID=4153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES,
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=11849595; DOI=10.1046/j.1365-313x.2001.01176.x;
RA   Kirch H.-H., Nair A., Bartels D.;
RT   "Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated
RT   from the resurrection plant Craterostigma plantagineum and Arabidopsis
RT   thaliana.";
RL   Plant J. 28:555-567(2001).
CC   -!- FUNCTION: Oxidizes nonanal, propionaldehyde and acetaldehyde in vitro,
CC       in the following decreasing order of reactivity: nonanal,
CC       propionaldehyde, acetaldehyde. {ECO:0000269|PubMed:11849595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC         Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.3;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=2.2 uM for nonanal {ECO:0000269|PubMed:11849595};
CC         KM=267 uM for propionaldehyde {ECO:0000269|PubMed:11849595};
CC         KM=32.3 mM for acetaldehyde {ECO:0000269|PubMed:11849595};
CC         Vmax=0.03 umol/sec/mg enzyme with nonanal as substrate
CC         {ECO:0000269|PubMed:11849595};
CC         Vmax=0.196 umol/sec/mg enzyme with propionaldehyde as substrate
CC         {ECO:0000269|PubMed:11849595};
CC         Vmax=0.102 umol/sec/mg enzyme with acetaldehyde as substrate
CC         {ECO:0000269|PubMed:11849595};
CC         Note=Measured at pH 9.5 for all experiments.;
CC   -!- SUBCELLULAR LOCATION: Plastid, amyloplast
CC       {ECO:0000269|PubMed:11849595}. Plastid, chloroplast
CC       {ECO:0000269|PubMed:11849595}.
CC   -!- INDUCTION: By abscisic acid (ABA) and dehydration.
CC       {ECO:0000269|PubMed:11849595}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000305}.
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DR   EMBL; AJ306960; CAC84900.1; -; mRNA.
DR   AlphaFoldDB; Q8VXQ2; -.
DR   SMR; Q8VXQ2; -.
DR   GO; GO:0009501; C:amyloplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0009507; C:chloroplast; IEA:UniProtKB-SubCell.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR   GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   PANTHER; PTHR43570; PTHR43570; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
PE   1: Evidence at protein level;
KW   Amyloplast; Chloroplast; NAD; Oxidoreductase; Plastid; Stress response.
FT   CHAIN           1..479
FT                   /note="Aldehyde dehydrogenase"
FT                   /id="PRO_0000256068"
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   BINDING         190..195
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   SITE            117
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   479 AA;  52741 MW;  47F266AE6CF77FCE CRC64;
     MSQVDAEGVV DGLRRTYISG KTKSYEWRVS QLKALLKITT HHDKEVVEAL RADLKKPEHE
     AYVHEIFMVS NACKSALKEL HQWMKPQKVK TSLATYPSSA EIVSEPLGVV LVITAWNYPF
     LLALDPMIGA IAAGNCVVLK PSEIAPATSA LLAKLLNQYV DTSAIRVVEG AVPEMQALLD
     QRWDKIFYTG SSKVGQIVLS SAAKHLTPVV LELGGKCPTV VDANIDLKVA ARRIISWKWS
     GNSGQTCISP DYIITTEENA PKLVDAIKCE LESFYGKDPL KSQDMSSIIN ERQFERMTGL
     LDDKKVSDKI VYGGQSDKSN LKIAPTILLD VSEDSSVMSE EIFGPLLPII TVGKIEECYK
     IIASKPKPLA AYLFTNDKKR TEEFVSNVSA GGITINDIAL HFLEPRLPFG GVGESGMGSY
     HGKFSFDAFS HKKSVLKRSF GGEVAARYPP YAPWKLHFME AILQGDIFGL LKAWLGWSS