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Q70DU8

- AL3H1_ARATH

UniProt

Q70DU8 - AL3H1_ARATH

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Protein
Aldehyde dehydrogenase family 3 member H1
Gene
ALDH3H1, ALDH4, At1g44170, T7O23.15
Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed - 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 hexanal
  3. KM=29 µM for octanal
  4. KM=8 µM for nonanal
  5. KM=5 µM for dodecanal
  6. KM=180 µM for trans-2-hexenal
  7. KM=3 µM for trans-2-nonenal
  8. KM=40.3 µM for 4-hydroxynonenal
  9. KM=421 µM for NAD+ (in the presence of hexanal as co-substrate)
  10. 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 dependencei

Optimum pH is 8.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei123 – 1231Transition state stabilizer By similarity
Active sitei218 – 2181Proton acceptor By similarity
Active sitei253 – 2531Nucleophile By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi196 – 2016NAD By similarity

GO - Molecular functioni

  1. 3-chloroallyl aldehyde dehydrogenase activity Source: TAIR
  2. aldehyde dehydrogenase (NAD) activity Source: TAIR
  3. aldehyde dehydrogenase [NAD(P)+] activity Source: InterPro

GO - Biological processi

  1. cellular aldehyde metabolic process Source: InterPro
  2. response to abscisic acid Source: TAIR
  3. response to desiccation Source: TAIR
  4. 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.
ARA:GQT-1341-MONOMER.
ARA:GQT-1342-MONOMER.

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
ProteomesiUP000006548: Chromosome 1

Organism-specific databases

TAIRiAT1G44170.

Subcellular locationi

GO - Cellular componenti

  1. Golgi apparatus Source: TAIR
  2. endoplasmic reticulum Source: TAIR
  3. membrane Source: TAIR
  4. plasmodesma Source: TAIR
  5. plastid Source: TAIR
  6. vacuole Source: TAIR
Complete GO annotation...

Pathology & Biotechi

Disruption phenotypei

Increased sensitivity to salt stress.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi45 – 451C → S: Decreased solubility, loss of dimerization and strongly decreased activity. 1 Publication
Mutagenesisi149 – 1491E → 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 Publication
Mutagenesisi149 – 1491E → 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 Publication
Mutagenesisi149 – 1491E → 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 Publication
Mutagenesisi149 – 1491E → 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 Publication
Mutagenesisi178 – 1781V → R: Changed coenzyme preference from NAD(+) to NADP(+), but no effect on the catalytic efficiency; when associated with T-149 and V-200. 1 Publication
Mutagenesisi200 – 2001I → 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 Publications
Mutagenesisi200 – 2001I → 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 Publications
Mutagenesisi247 – 2471C → S: No effect on solubility, but 10% loss of activity. 1 Publication
Mutagenesisi253 – 2531C → S: No effect on solubility, but loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 484484Aldehyde dehydrogenase family 3 member H1
PRO_0000256060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi45 – 45Interchain

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ70DU8.
PRIDEiQ70DU8.

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.4 Publications

Gene expression databases

GenevestigatoriQ70DU8.

Interactioni

Subunit structurei

Homodimer and homomultimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ70DU8.
SMRiQ70DU8. Positions 13-456.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271515.
InParanoidiQ70DU8.
KOiK00128.
OMAiSKMKPIF.
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. Align

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

MAAKKVFGSA EASNLVTELR RSFDDGVTRG YEWRVTQLKK LMIICDNHEP    50
EIVAALRDDL GKPELESSVY EVSLLRNSIK LALKQLKNWM APEKAKTSLT 100
TFPASAEIVS EPLGVVLVIS AWNYPFLLSI DPVIGAISAG NAVVLKPSEL 150
APASSALLTK LLEQYLDPSA VRVVEGAVTE TSALLEQKWD KIFYTGSSKI 200
GRVIMAAAAK HLTPVVLELG GKSPVVVDSD TDLKVTVRRI IVGKWGCNNG 250
QACVSPDYIL TTKEYAPKLI DAMKLELEKF YGKNPIESKD MSRIVNSNHF 300
DRLSKLLDEK EVSDKIVYGG EKDRENLKIA PTILLDVPLD SLIMSEEIFG 350
PLLPILTLNN LEESFDVIRS RPKPLAAYLF THNKKLKERF AATVSAGGIV 400
VNDIAVHLAL HTLPFGGVGE SGMGAYHGKF SFDAFSHKKA VLYRSLFGDS 450
AVRYPPYSRG KLRLLKALVD SNIFDLFKVL LGLA 484

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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7171MAAKK…SSVYE → MFYQQRVL in isoform beta.
VSP_054869Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti200 – 2001I → V in CAE51203. 1 Publication
Sequence conflicti272 – 2721A → D in CAE51203. 1 Publication
Sequence conflicti300 – 3001F → L in CAE51203. 1 Publication
Sequence conflicti391 – 3911A → T in AAM61211. 1 Publication
Sequence conflicti435 – 4351F → S in CAE51203. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_179439.3. [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.
KEGGiath:AT1G44170.

Keywords - Coding sequence diversityi

Alternative promoter usage, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi H96505.
RefSeqi NP_001077676.1. NM_001084207.1. [Q70DU8-2 ]
NP_175081.1. NM_103541.3. [Q70DU8-1 ]
NP_849770.1. NM_179439.3. [Q70DU8-1 ]
UniGenei At.17189.
At.48278.

3D structure databases

ProteinModelPortali Q70DU8.
SMRi Q70DU8. Positions 13-456.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q70DU8.
PRIDEi Q70DU8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT1G44170.1 ; AT1G44170.1 ; AT1G44170 . [Q70DU8-1 ]
AT1G44170.2 ; AT1G44170.2 ; AT1G44170 . [Q70DU8-1 ]
AT1G44170.3 ; AT1G44170.3 ; AT1G44170 . [Q70DU8-2 ]
GeneIDi 841020.
KEGGi ath:AT1G44170.

Organism-specific databases

TAIRi AT1G44170.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271515.
InParanoidi Q70DU8.
KOi K00128.
OMAi SKMKPIF.
PhylomeDBi Q70DU8.

Enzyme and pathway databases

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

Gene expression databases

Genevestigatori Q70DU8.

Family and domain databases

Gene3Di 3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProi IPR016161. 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 ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
PIRSFi PIRSF036492. ALDH. 1 hit.
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

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: September 3, 2014
This is version 85 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

External Data

Dasty 3

Similar proteinsi