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Q8W033

- AL3I1_ARATH

UniProt

Q8W033 - AL3I1_ARATH

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Protein
Aldehyde dehydrogenase family 3 member I1, chloroplastic
Gene
ALDH3I1, ALDH3, At4g34240, F10M10.10
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. Can use both NAD+ and NADP+, but the coenzyme preference is substrate dependent.2 Publications

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=8053 µM for propionaldehyde1 Publication
  2. KM=111 µM for hexanal
  3. KM=24 µM for octanal
  4. KM=7 µM for nonanal
  5. KM=1.3 µM for dodecanal
  6. KM=151 µM for trans-2-hexenal
  7. KM=5.5 µM for trans-2-nonenal
  8. KM=21 µM for 4-hydroxynonenal
  9. KM=71 µM for NAD+ (in the presence of hexanal as co-substrate)
  10. KM=1868 µM for NADP+ (in the presence of hexanal as co-substrate)
  11. KM=53 µM for NAD+ (in the presence of trans-2-nonenal as co-substrate)
  12. KM=87 µM for NADP+ (in the presence of trans-2-nonenal as co-substrate)

Vmax=10.1 µmol/min/mg enzyme with propionaldehyde as substrate

Vmax=17.3 µmol/min/mg enzyme with hexanal as substrate

Vmax=16.6 µmol/min/mg enzyme with octanal as substrate

Vmax=20 µmol/min/mg enzyme with nonanal as substrate

Vmax=18.8 µmol/min/mg enzyme with dodecanal as substrate

Vmax=1.5 µmol/min/mg enzyme with trans-2-hexenal as substrate

Vmax=1.6 µmol/min/mg enzyme with trans-2-nonenal as substrate

Vmax=0.6 µmol/min/mg enzyme with 4-hydroxynonenal as substrate

pH dependencei

Optimum pH is 9.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei186 – 1861Transition state stabilizer By similarity
Active sitei281 – 2811Proton acceptor By similarity
Active sitei316 – 3161Nucleophile By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi259 – 2646NAD By similarity

GO - Molecular functioni

  1. 3-chloroallyl aldehyde dehydrogenase activity Source: TAIR
  2. aldehyde dehydrogenase (NAD) activity Source: TAIR
  3. aldehyde dehydrogenase (NADP+) activity Source: TAIR
  4. 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 water deprivation Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Stress response

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciARA:AT4G34240-MONOMER.
ARA:GQT-2498-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase family 3 member I1, chloroplastic (EC:1.2.1.3)
Short name:
AtALDH3
Short name:
Ath-ALDH3
Gene namesi
Name:ALDH3I1
Synonyms:ALDH3
Ordered Locus Names:At4g34240
ORF Names:F10M10.10
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
ProteomesiUP000006548: Chromosome 4

Organism-specific databases

TAIRiAT4G34240.

Subcellular locationi

Plastidchloroplast Reviewed prediction

GO - Cellular componenti

  1. chloroplast Source: TAIR
  2. chloroplast envelope Source: TAIR
  3. plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Plastid

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141C → S: No effect on solubility, but loss of dimerization and 80% loss of activity. 1 Publication
Mutagenesisi142 – 1421C → S: No effect on solubility, but decreased activity. 1 Publication
Mutagenesisi263 – 2631V → I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+). 1 Publication
Mutagenesisi286 – 2861C → S: No effect on solubility, but no effect on activity. 1 Publication
Mutagenesisi310 – 3101C → S: No effect on solubility, but no effect on activity. 1 Publication
Mutagenesisi316 – 3161C → S: No effect on solubility, but loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 5959Chloroplast Reviewed prediction
Add
BLAST
Chaini60 – 550491Aldehyde dehydrogenase family 3 member I1, chloroplastic
PRO_0000256061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi114 – 114Interchain

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiQ8W033.
PRIDEiQ8W033.

Expressioni

Inductioni

By abscisic acid (ABA), dehydration, salt stress in plantlets. Induced by heavy metals and H2O2.4 Publications

Gene expression databases

ArrayExpressiQ8W033.
GenevestigatoriQ8W033.

Interactioni

Subunit structurei

Homodimer and homomultimer.1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ8W033.
SMRiQ8W033. Positions 31-519.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271515.
InParanoidiQ8W033.
KOiK00128.
OMAiVARIIMA.
PhylomeDBiQ8W033.

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.
IPR016160. Ald_DH_CS_CYS.
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.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 1 isoform i produced by alternative splicing. Align

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q8W033-1) [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

MTKLLEINHI QTLCFAKGFS PARLNVATSP FRISRRGGGG YCSNACIPYR    50
LKFTCYATLS AVVKEQASDF SGKEAALLVD ELRSNFNSGR TKSYEWRISQ 100
LQNIARMIDE KEKCITEALY QDLSKPELEA FLAEISNTKS SCMLAIKELK 150
NWMAPETVKT SVTTFPSSAQ IVSEPLGVVL VISAWNFPFL LSVEPVIGAI 200
AAGNAVVLKP SEIAPAASSL LAKLFSEYLD NTTIRVIEGG VPETTALLDQ 250
KWDKIFFTGG ARVARIIMAA AARNLTPVVL ELGGKCPALV DSDVNLQVAA 300
RRIIAGKWAC NSGQACIGVD YVITTKDFAS KLIDALKTEL ETFFGQNALE 350
SKDLSRIVNS FHFKRLESML KENGVANKIV HGGRITEDKL KISPTILLDV 400
PEASSMMQEE IFGPLLPIIT VQKIEDGFQV IRSKPKPLAA YLFTNNKELE 450
KQFVQDVSAG GITINDTVLH VTVKDLPFGG VGESGIGAYH GKFSYETFSH 500
KKGVLYRSFS GDADLRYPPY TPKKKMVLKA LLSSNIFAAI LAFFGFSKDS 550
Length:550
Mass (Da):60,173
Last modified:October 31, 2006 - v2
Checksum:i42FC2BC37757A083
GO

Sequence cautioni

The sequence CAB36701.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAB80141.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321R → L in CAC84903. 1 Publication
Sequence conflicti71 – 711S → R in CAC84903. 1 Publication
Sequence conflicti435 – 4351P → S in CAC84903. 1 Publication
Sequence conflicti536 – 5361I → M in CAC84903. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ306961 mRNA. Translation: CAC84903.1.
AL035521 Genomic DNA. Translation: CAB36701.1. Sequence problems.
AL161585 Genomic DNA. Translation: CAB80141.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86347.1.
AY054633 mRNA. Translation: AAK96824.1.
AY081532 mRNA. Translation: AAM10094.1.
PIRiT04770.
RefSeqiNP_567962.1. NM_119588.5. [Q8W033-1]
UniGeneiAt.26454.

Genome annotation databases

EnsemblPlantsiAT4G34240.1; AT4G34240.1; AT4G34240. [Q8W033-1]
GeneIDi829573.
KEGGiath:AT4G34240.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ306961 mRNA. Translation: CAC84903.1 .
AL035521 Genomic DNA. Translation: CAB36701.1 . Sequence problems.
AL161585 Genomic DNA. Translation: CAB80141.1 . Sequence problems.
CP002687 Genomic DNA. Translation: AEE86347.1 .
AY054633 mRNA. Translation: AAK96824.1 .
AY081532 mRNA. Translation: AAM10094.1 .
PIRi T04770.
RefSeqi NP_567962.1. NM_119588.5. [Q8W033-1 ]
UniGenei At.26454.

3D structure databases

ProteinModelPortali Q8W033.
SMRi Q8W033. Positions 31-519.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi Q8W033.
PRIDEi Q8W033.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblPlantsi AT4G34240.1 ; AT4G34240.1 ; AT4G34240 . [Q8W033-1 ]
GeneIDi 829573.
KEGGi ath:AT4G34240.

Organism-specific databases

TAIRi AT4G34240.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000271515.
InParanoidi Q8W033.
KOi K00128.
OMAi VARIIMA.
PhylomeDBi Q8W033.

Enzyme and pathway databases

BioCyci ARA:AT4G34240-MONOMER.
ARA:GQT-2498-MONOMER.

Gene expression databases

ArrayExpressi Q8W033.
Genevestigatori Q8W033.

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.
IPR016160. Ald_DH_CS_CYS.
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 PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
  2. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
    Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
    , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
    Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  3. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  4. "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].
    Strain: cv. Columbia.
  5. "Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance."
    Sunkar R., Bartels D., Kirch H.-H.
    Plant J. 35:452-464(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION.
  6. Cited for: NOMENCLATURE.
  7. "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: INDUCTION.
  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-114; CYS-142; VAL-263; CYS-286; CYS-310 AND CYS-316, ENZYME REGULATION, 3D-STRUCTURE MODELING.
  9. "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.

Entry informationi

Entry nameiAL3I1_ARATH
AccessioniPrimary (citable) accession number: Q8W033
Secondary accession number(s): Q940H4, Q9SYY9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: June 11, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Miscellaneous

Plants overexpressing ALDH3I1 show improved tolerance when exposed to dehydration, salt stress, heavy metals and H2O2.

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

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