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Protein

Aldehyde dehydrogenase family 3 member H1

Gene

ALDH3H1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

An aldehyde + NAD+ + H2O = a carboxylate + NADH.1 Publication

Enzyme regulationi

Thiol-based regulation. Inactivation after dimerization under oxidizing conditions.1 Publication

Kineticsi

  1. KM=510 µM for propionaldehyde1 Publication
  2. KM=71 µM for hexanal1 Publication
  3. KM=29 µM for octanal1 Publication
  4. KM=8 µM for nonanal1 Publication
  5. KM=5 µM for dodecanal1 Publication
  6. KM=180 µM for trans-2-hexenal1 Publication
  7. KM=3 µM for trans-2-nonenal1 Publication
  8. KM=40.3 µM for 4-hydroxynonenal1 Publication
  9. KM=421 µM for NAD+ (in the presence of hexanal as co-substrate)1 Publication
  10. KM=119 µM for NAD+ (in the presence of trans-2-nonenal as co-substrate)1 Publication
  1. Vmax=7.3 µmol/min/mg enzyme with propionaldehyde as substrate1 Publication
  2. Vmax=12 µmol/min/mg enzyme with hexanal as substrate1 Publication
  3. Vmax=18 µmol/min/mg enzyme with octanal as substrate1 Publication
  4. Vmax=19.2 µmol/min/mg enzyme with nonanal as substrate1 Publication
  5. Vmax=23.9 µmol/min/mg enzyme with dodecanal as substrate1 Publication
  6. Vmax=2.4 µmol/min/mg enzyme with trans-2-hexenal as substrate1 Publication
  7. Vmax=2.9 µmol/min/mg enzyme with trans-2-nonenal as substrate1 Publication
  8. Vmax=1.4 µmol/min/mg enzyme with 4-hydroxynonenal as substrate1 Publication

pH dependencei

Optimum pH is 8.0.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei123Transition state stabilizerBy similarity1
Active sitei218Proton acceptorPROSITE-ProRule annotation1
Active sitei253NucleophilePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi196 – 201NADBy similarity6

GO - Molecular functioni

  • 3-chloroallyl aldehyde dehydrogenase activity Source: TAIR
  • aldehyde dehydrogenase (NAD) activity Source: TAIR
  • aldehyde dehydrogenase [NAD(P)+] activity Source: InterPro

GO - Biological processi

  • cellular aldehyde metabolic process Source: InterPro
  • response to abscisic acid Source: TAIR
  • response to desiccation Source: TAIR
  • response to salt stress Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciARA:AT1G44170-MONOMER.
ReactomeiR-ATH-1660661. Sphingolipid de novo biosynthesis.
R-ATH-211945. Phase 1 - Functionalization of compounds.
R-ATH-389599. Alpha-oxidation of phytanate.
R-ATH-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 3 member H1 (EC:1.2.1.3)
Short name:
AtALDH4
Short name:
Ath-ALDH4
Gene namesi
Name:ALDH3H1
Synonyms:ALDH4
Ordered Locus Names:At1g44170
ORF Names:T7O23.15
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 1

Organism-specific databases

TAIRiAT1G44170.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: TAIR
  • Golgi apparatus Source: TAIR
  • membrane Source: TAIR
  • plasmodesma Source: TAIR
  • plastid Source: TAIR
  • vacuole Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Increased sensitivity to salt stress.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi45C → S: Decreased solubility, loss of dimerization and strongly decreased activity. 1 Publication1
Mutagenesisi149E → 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. 1 Publication1
Mutagenesisi149E → 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. 1 Publication1
Mutagenesisi149E → 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. 1 Publication1
Mutagenesisi149E → 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. 1 Publication1
Mutagenesisi178V → R: Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and V-200. 1 Publication1
Mutagenesisi200I → 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. 2 Publications1
Mutagenesisi200I → 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. 2 Publications1
Mutagenesisi247C → S: No effect on solubility, but 10% loss of activity. 1 Publication1
Mutagenesisi253C → S: No effect on solubility, but loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002560601 – 484Aldehyde dehydrogenase family 3 member H1Add BLAST484

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi45Interchain

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ70DU8.
PRIDEiQ70DU8.

PTM databases

iPTMnetiQ70DU8.

Expressioni

Tissue specificityi

Isoform alpha is expressed in expanded leaves and flowers. Detected in seedlings. Isoform beta is mainly expressed in flowers. Detected in leaves and seedlings.1 Publication

Inductioni

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.3 Publications

Gene expression databases

ExpressionAtlasiQ70DU8. baseline and differential.
GenevisibleiQ70DU8. AT.

Interactioni

Subunit structurei

Homodimer and homomultimer.1 Publication

Protein-protein interaction databases

STRINGi3702.AT1G44170.1.

Structurei

3D structure databases

ProteinModelPortaliQ70DU8.
SMRiQ70DU8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiKOG2456. Eukaryota.
COG1012. LUCA.
HOGENOMiHOG000271515.
InParanoidiQ70DU8.
KOiK00128.
OMAiFFAPEEF.
OrthoDBiEOG093609F3.
PhylomeDBiQ70DU8.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative promoter usage and alternative splicing. AlignAdd to basket

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) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAKKVFGSA EASNLVTELR RSFDDGVTRG YEWRVTQLKK LMIICDNHEP
60 70 80 90 100
EIVAALRDDL GKPELESSVY EVSLLRNSIK LALKQLKNWM APEKAKTSLT
110 120 130 140 150
TFPASAEIVS EPLGVVLVIS AWNYPFLLSI DPVIGAISAG NAVVLKPSEL
160 170 180 190 200
APASSALLTK LLEQYLDPSA VRVVEGAVTE TSALLEQKWD KIFYTGSSKI
210 220 230 240 250
GRVIMAAAAK HLTPVVLELG GKSPVVVDSD TDLKVTVRRI IVGKWGCNNG
260 270 280 290 300
QACVSPDYIL TTKEYAPKLI DAMKLELEKF YGKNPIESKD MSRIVNSNHF
310 320 330 340 350
DRLSKLLDEK EVSDKIVYGG EKDRENLKIA PTILLDVPLD SLIMSEEIFG
360 370 380 390 400
PLLPILTLNN LEESFDVIRS RPKPLAAYLF THNKKLKERF AATVSAGGIV
410 420 430 440 450
VNDIAVHLAL HTLPFGGVGE SGMGAYHGKF SFDAFSHKKA VLYRSLFGDS
460 470 480
AVRYPPYSRG KLRLLKALVD SNIFDLFKVL LGLA
Note: Major isoform.
Length:484
Mass (Da):53,159
Last modified:October 31, 2006 - v2
Checksum:i5D931EF77293F668
GO
Isoform beta (identifier: Q70DU8-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:421
Mass (Da):46,215
Checksum:i867A5F299A010773
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti200I → V in CAE51203 (PubMed:15830124).Curated1
Sequence conflicti272A → D in CAE51203 (PubMed:15830124).Curated1
Sequence conflicti300F → L in CAE51203 (PubMed:15830124).Curated1
Sequence conflicti391A → T in AAM61211 (Ref. 4) Curated1
Sequence conflicti435F → S in CAE51203 (PubMed:15830124).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0548691 – 71MAAKK…SSVYE → MFYQQRVL in isoform beta. CuratedAdd BLAST71

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH96505.
RefSeqiNP_001077676.1. NM_001084207.1. [Q70DU8-2]
NP_175081.1. NM_103541.3. [Q70DU8-1]
NP_849770.1. NM_179439.4. [Q70DU8-1]
UniGeneiAt.17189.
At.48278.

Genome annotation databases

EnsemblPlantsiAT1G44170.1; AT1G44170.1; AT1G44170. [Q70DU8-1]
AT1G44170.2; AT1G44170.2; AT1G44170. [Q70DU8-1]
AT1G44170.3; AT1G44170.3; AT1G44170. [Q70DU8-2]
GeneIDi841020.
GrameneiAT1G44170.1; AT1G44170.1; AT1G44170.
AT1G44170.2; AT1G44170.2; AT1G44170.
AT1G44170.3; AT1G44170.3; AT1G44170.
KEGGiath:AT1G44170.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
PIRiH96505.
RefSeqiNP_001077676.1. NM_001084207.1. [Q70DU8-2]
NP_175081.1. NM_103541.3. [Q70DU8-1]
NP_849770.1. NM_179439.4. [Q70DU8-1]
UniGeneiAt.17189.
At.48278.

3D structure databases

ProteinModelPortaliQ70DU8.
SMRiQ70DU8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi3702.AT1G44170.1.

PTM databases

iPTMnetiQ70DU8.

Proteomic databases

PaxDbiQ70DU8.
PRIDEiQ70DU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT1G44170.1; AT1G44170.1; AT1G44170. [Q70DU8-1]
AT1G44170.2; AT1G44170.2; AT1G44170. [Q70DU8-1]
AT1G44170.3; AT1G44170.3; AT1G44170. [Q70DU8-2]
GeneIDi841020.
GrameneiAT1G44170.1; AT1G44170.1; AT1G44170.
AT1G44170.2; AT1G44170.2; AT1G44170.
AT1G44170.3; AT1G44170.3; AT1G44170.
KEGGiath:AT1G44170.

Organism-specific databases

TAIRiAT1G44170.

Phylogenomic databases

eggNOGiKOG2456. Eukaryota.
COG1012. LUCA.
HOGENOMiHOG000271515.
InParanoidiQ70DU8.
KOiK00128.
OMAiFFAPEEF.
OrthoDBiEOG093609F3.
PhylomeDBiQ70DU8.

Enzyme and pathway databases

BioCyciARA:AT1G44170-MONOMER.
ReactomeiR-ATH-1660661. Sphingolipid de novo biosynthesis.
R-ATH-211945. Phase 1 - Functionalization of compounds.
R-ATH-389599. Alpha-oxidation of phytanate.
R-ATH-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiQ70DU8.

Gene expression databases

ExpressionAtlasiQ70DU8. baseline and differential.
GenevisibleiQ70DU8. AT.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFiPIRSF036492. ALDH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAL3H1_ARATH
AccessioniPrimary (citable) accession number: Q70DU8
Secondary accession number(s): A8MQF0, Q8LFT7, Q9C6Y7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: November 30, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.