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Q70DU8 (AL3H1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase family 3 member H1

Short name=AtALDH4
Short name=Ath-ALDH4
EC=1.2.1.3
Gene names
Name:ALDH3H1
Synonyms:ALDH4
Ordered Locus Names:At1g44170
ORF Names:T7O23.15
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in oxidative stress tolerance by detoxifying reactive aldehydes derived from lipid peroxidation. Medium- to long-chain saturated aldehydes are preferred substrates, while the short-chain aldehyde propanal is a weak substrate. Is strictely NAD+ specific. Ref.8

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH. Ref.8

Enzyme regulation

Thiol-based regulation. Inactivation after dimerization under oxidizing conditions. Ref.8

Subunit structure

Homodimer and homomultimer. Ref.8

Tissue specificity

Isoform alpha is expressed in expanded leaves and flowers. Detected in seedlings. Isoform beta is mainly expressed in flowers. Detected in leaves and seedlings. Ref.9

Induction

By abscisic acid (ABA), dehydration and salt stress in roots. Isoform alpha is up-regulated in leaves but not in roots upon salt treatment. Isoforn beta is up-regulated by salt treatment in both roots and leaves. Ref.5 Ref.6 Ref.8 Ref.9

Disruption phenotype

Increased sensitivity to salt stress. Ref.9

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=510 µM for propionaldehyde Ref.8

KM=71 µM for hexanal

KM=29 µM for octanal

KM=8 µM for nonanal

KM=5 µM for dodecanal

KM=180 µM for trans-2-hexenal

KM=3 µM for trans-2-nonenal

KM=40.3 µM for 4-hydroxynonenal

KM=421 µM for NAD+ (in the presence of hexanal as co-substrate)

KM=119 µM for NAD+ (in the presence of trans-2-nonenal as co-substrate)

Vmax=7.3 µmol/min/mg enzyme with propionaldehyde as substrate

Vmax=12 µmol/min/mg enzyme with hexanal as substrate

Vmax=18 µmol/min/mg enzyme with octanal as substrate

Vmax=19.2 µmol/min/mg enzyme with nonanal as substrate

Vmax=23.9 µmol/min/mg enzyme with dodecanal as substrate

Vmax=2.4 µmol/min/mg enzyme with trans-2-hexenal as substrate

Vmax=2.9 µmol/min/mg enzyme with trans-2-nonenal as substrate

Vmax=1.4 µmol/min/mg enzyme with 4-hydroxynonenal as substrate

pH dependence:

Optimum pH is 8.0.

Alternative products

This entry describes 2 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Note: A number of isoforms are produced. According to EST sequences. An alternative promoter within intron 1 may direct expression of several alternative transcripts, including isoform beta.
Isoform alpha (identifier: Q70DU8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Note: Major isoform.
Isoform beta (identifier: Q70DU8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-71: MAAKKVFGSA...KPELESSVYE → MFYQQRVL
Note: Produced by alternative splicing. Maybe not translated into a protein or accumulates at a level below detection.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Aldehyde dehydrogenase family 3 member H1
PRO_0000256060

Regions

Nucleotide binding196 – 2016NAD By similarity

Sites

Active site2181Proton acceptor By similarity
Active site2531Nucleophile By similarity
Site1231Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond45Interchain

Natural variations

Alternative sequence1 – 7171MAAKK…SSVYE → MFYQQRVL in isoform beta.
VSP_054869

Experimental info

Mutagenesis451C → S: Decreased solubility, loss of dimerization and strongly decreased activity. Ref.8
Mutagenesis1491E → D: Small effect on NAD(+) interaction, but 40% loss of efficiency. Ability to use NADP(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Ref.10
Mutagenesis1491E → N: Ability to use NADP(+) and 33% decreased efficiency with NAD(+). 70% loss of efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Ref.10
Mutagenesis1491E → Q: Loss of specificity for NAD(+) and loss of 25% efficiency. 15% efficiency with NAD(+); when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Ref.10
Mutagenesis1491E → T: Loss of specificity and increased NADP(+) binding. Decerased catalytic efficiency. Loss of cofactor specificity and same lower efficiency with both; when associated with V-200. Impaired affinity for both cofactors and decreased catalytic efficiency; when associated with G-200. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with R-178 and V-200. Ref.10
Mutagenesis1781V → R: Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and V-200. Ref.10
Mutagenesis2001I → G: Changed coenzyme preference from NAD(+) to NADP(+), but impaired affinities for both cofactors. No effect on the interaction with the substrate. Impaired affinities for both cofactors and decreased catalytic efficiencies; when associated with D-149, Q-149, N-149 or T-149. Ref.8 Ref.10
Mutagenesis2001I → V: Also able to use NADP(+) as coenzyme, but no effect on the interaction with the substrate. 15% efficiency with NAD(+); when associated with Q-149. 70% loss of efficiency with NAD(+); when associated with D-149 or N-149. Loss of cofactor specificity and same lower efficiency with both; when associated with T-149. Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and R-178. Ref.8 Ref.10
Mutagenesis2471C → S: No effect on solubility, but 10% loss of activity. Ref.8
Mutagenesis2531C → S: No effect on solubility, but loss of activity. Ref.8
Sequence conflict2001I → V in CAE51203. Ref.5
Sequence conflict2721A → D in CAE51203. Ref.5
Sequence conflict3001F → L in CAE51203. Ref.5
Sequence conflict3911A → T in AAM61211. Ref.4
Sequence conflict4351F → S in CAE51203. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Isoform alpha [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 5D931EF77293F668

FASTA48453,159
        10         20         30         40         50         60 
MAAKKVFGSA EASNLVTELR RSFDDGVTRG YEWRVTQLKK LMIICDNHEP EIVAALRDDL 

        70         80         90        100        110        120 
GKPELESSVY EVSLLRNSIK LALKQLKNWM APEKAKTSLT TFPASAEIVS EPLGVVLVIS 

       130        140        150        160        170        180 
AWNYPFLLSI DPVIGAISAG NAVVLKPSEL APASSALLTK LLEQYLDPSA VRVVEGAVTE 

       190        200        210        220        230        240 
TSALLEQKWD KIFYTGSSKI GRVIMAAAAK HLTPVVLELG GKSPVVVDSD TDLKVTVRRI 

       250        260        270        280        290        300 
IVGKWGCNNG QACVSPDYIL TTKEYAPKLI DAMKLELEKF YGKNPIESKD MSRIVNSNHF 

       310        320        330        340        350        360 
DRLSKLLDEK EVSDKIVYGG EKDRENLKIA PTILLDVPLD SLIMSEEIFG PLLPILTLNN 

       370        380        390        400        410        420 
LEESFDVIRS RPKPLAAYLF THNKKLKERF AATVSAGGIV VNDIAVHLAL HTLPFGGVGE 

       430        440        450        460        470        480 
SGMGAYHGKF SFDAFSHKKA VLYRSLFGDS AVRYPPYSRG KLRLLKALVD SNIFDLFKVL 


LGLA 

« Hide

Isoform beta [UniParc].

Checksum: 867A5F299A010773
Show »

FASTA42146,215

References

« Hide 'large scale' references
[1]"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana."
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. expand/collapse author list , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.
Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: cv. Columbia.
[2]The Arabidopsis Information Resource (TAIR)
Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
Cited for: GENOME REANNOTATION.
Strain: cv. Columbia.
[3]"Empirical analysis of transcriptional activity in the Arabidopsis genome."
Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G. expand/collapse author list , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
Strain: cv. Columbia.
[4]"Full-length cDNA from Arabidopsis thaliana."
Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A.
Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
[5]"Detailed expression analysis of selected genes of the aldehyde dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana."
Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.
Plant Mol. Biol. 57:315-332(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 5-484 (ISOFORM ALPHA), INDUCTION.
[6]"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: IDENTIFICATION, INDUCTION.
[7]"The ALDH gene superfamily of Arabidopsis."
Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.
Trends Plant Sci. 9:371-377(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NOMENCLATURE.
[8]"Engineering the nucleotide coenzyme specificity and sulfhydryl redox sensitivity of two stress-responsive aldehyde dehydrogenase isoenzymes of Arabidopsis thaliana."
Stiti N., Adewale I.O., Petersen J., Bartels D., Kirch H.H.
Biochem. J. 434:459-471(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF CYS-45; ILE-200; CYS-247 AND CYS-253, ENZYME REGULATION, 3D-STRUCTURE MODELING.
[9]"T-DNA insertion mutants reveal complex expression patterns of the aldehyde dehydrogenase 3H1 locus in Arabidopsis thaliana."
Missihoun T.D., Kirch H.H., Bartels D.
J. Exp. Bot. 63:3887-3898(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY, INDUCTION, DISRUPTION PHENOTYPE.
Strain: cv. Columbia.
[10]"Aldehyde dehydrogenase enzyme ALDH3H1 from Arabidopsis thaliana: Identification of amino acid residues critical for cofactor specificity."
Stiti N., Podgorska K., Bartels D.
Biochim. Biophys. Acta 1844:681-693(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING, MUTAGENESIS OF GLU-149; VAL-178 AND ILE-200.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AC074228 Genomic DNA. Translation: AAG50550.1.
CP002684 Genomic DNA. Translation: AEE32025.1.
CP002684 Genomic DNA. Translation: AEE32026.1.
CP002684 Genomic DNA. Translation: AEE32027.1.
AY072122 mRNA. Translation: AAL59944.1.
AY084648 mRNA. Translation: AAM61211.1.
AJ585241 mRNA. Translation: CAE51203.1.
PIRH96505.
RefSeqNP_001077676.1. NM_001084207.1.
NP_175081.1. NM_103541.3. [Q70DU8-1]
NP_849770.1. NM_179439.3. [Q70DU8-1]
UniGeneAt.17189.
At.48278.

3D structure databases

ProteinModelPortalQ70DU8.
SMRQ70DU8. Positions 13-456.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ70DU8.
PRIDEQ70DU8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT1G44170.1; AT1G44170.1; AT1G44170. [Q70DU8-1]
AT1G44170.2; AT1G44170.2; AT1G44170. [Q70DU8-1]
AT1G44170.3; AT1G44170.3; AT1G44170. [Q70DU8-2]
GeneID841020.
KEGGath:AT1G44170.

Organism-specific databases

TAIRAT1G44170.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271515.
InParanoidQ70DU8.
KOK00128.
OMASKMKPIF.
PhylomeDBQ70DU8.

Enzyme and pathway databases

BioCycARA:AT1G44170-MONOMER.
ARA:GQT-1341-MONOMER.
ARA:GQT-1342-MONOMER.

Gene expression databases

GenevestigatorQ70DU8.

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.
IPR029510. Ald_DH_CS_GLU.
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.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL3H1_ARATH
AccessionPrimary (citable) accession number: Q70DU8
Secondary accession number(s): A8MQF0, Q8LFT7, Q9C6Y7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: July 9, 2014
This is version 84 of the entry and version 2 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

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names