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Q8W033 (AL3I1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 86. 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 I1, chloroplastic

Short name=AtALDH3
Short name=Ath-ALDH3
EC=1.2.1.3
Gene names
Name:ALDH3I1
Synonyms:ALDH3
Ordered Locus Names:At4g34240
ORF Names:F10M10.10
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis

Protein attributes

Sequence length550 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. Can use both NAD+ and NADP+, but the coenzyme preference is substrate dependent. Ref.5 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

Subcellular location

Plastidchloroplast Potential.

Induction

By abscisic acid (ABA), dehydration, salt stress in plantlets. Induced by heavy metals and H2O2. Ref.1 Ref.5 Ref.7 Ref.8

Miscellaneous

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

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=8053 µM for propionaldehyde Ref.8

KM=111 µM for hexanal

KM=24 µM for octanal

KM=7 µM for nonanal

KM=1.3 µM for dodecanal

KM=151 µM for trans-2-hexenal

KM=5.5 µM for trans-2-nonenal

KM=21 µM for 4-hydroxynonenal

KM=71 µM for NAD+ (in the presence of hexanal as co-substrate)

KM=1868 µM for NADP+ (in the presence of hexanal as co-substrate)

KM=53 µM for NAD+ (in the presence of trans-2-nonenal as co-substrate)

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 dependence:

Optimum pH is 9.0.

Sequence caution

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.

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.
Isoform 1 (identifier: Q8W033-1)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Chloroplast Potential
Chain60 – 550491Aldehyde dehydrogenase family 3 member I1, chloroplastic
PRO_0000256061

Regions

Nucleotide binding259 – 2646NAD By similarity

Sites

Active site2811Proton acceptor By similarity
Active site3161Nucleophile By similarity
Site1861Transition state stabilizer By similarity

Amino acid modifications

Disulfide bond114Interchain

Experimental info

Mutagenesis1141C → S: No effect on solubility, but loss of dimerization and 80% loss of activity. Ref.8
Mutagenesis1421C → S: No effect on solubility, but decreased activity. Ref.8
Mutagenesis2631V → I: No effect on substrate specificity, but decreased affinity for NADP(+) and increased affinity for NAD(+). Ref.8
Mutagenesis2861C → S: No effect on solubility, but no effect on activity. Ref.8
Mutagenesis3101C → S: No effect on solubility, but no effect on activity. Ref.8
Mutagenesis3161C → S: No effect on solubility, but loss of activity. Ref.8
Sequence conflict321R → L in CAC84903. Ref.1
Sequence conflict711S → R in CAC84903. Ref.1
Sequence conflict4351P → S in CAC84903. Ref.1
Sequence conflict5361I → M in CAC84903. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: 42FC2BC37757A083

FASTA55060,173
        10         20         30         40         50         60 
MTKLLEINHI QTLCFAKGFS PARLNVATSP FRISRRGGGG YCSNACIPYR LKFTCYATLS 

        70         80         90        100        110        120 
AVVKEQASDF SGKEAALLVD ELRSNFNSGR TKSYEWRISQ LQNIARMIDE KEKCITEALY 

       130        140        150        160        170        180 
QDLSKPELEA FLAEISNTKS SCMLAIKELK NWMAPETVKT SVTTFPSSAQ IVSEPLGVVL 

       190        200        210        220        230        240 
VISAWNFPFL LSVEPVIGAI AAGNAVVLKP SEIAPAASSL LAKLFSEYLD NTTIRVIEGG 

       250        260        270        280        290        300 
VPETTALLDQ KWDKIFFTGG ARVARIIMAA AARNLTPVVL ELGGKCPALV DSDVNLQVAA 

       310        320        330        340        350        360 
RRIIAGKWAC NSGQACIGVD YVITTKDFAS KLIDALKTEL ETFFGQNALE SKDLSRIVNS 

       370        380        390        400        410        420 
FHFKRLESML KENGVANKIV HGGRITEDKL KISPTILLDV PEASSMMQEE IFGPLLPIIT 

       430        440        450        460        470        480 
VQKIEDGFQV IRSKPKPLAA YLFTNNKELE KQFVQDVSAG GITINDTVLH VTVKDLPFGG 

       490        500        510        520        530        540 
VGESGIGAYH GKFSYETFSH KKGVLYRSFS GDADLRYPPY TPKKKMVLKA LLSSNIFAAI 

       550 
LAFFGFSKDS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. 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].
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]"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.
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT04770.
RefSeqNP_567962.1. NM_119588.5. [Q8W033-1]
UniGeneAt.26454.

3D structure databases

ProteinModelPortalQ8W033.
SMRQ8W033. Positions 31-519.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PaxDbQ8W033.
PRIDEQ8W033.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G34240.1; AT4G34240.1; AT4G34240. [Q8W033-1]
GeneID829573.
KEGGath:AT4G34240.

Organism-specific databases

TAIRAT4G34240.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271515.
InParanoidQ8W033.
KOK00128.
OMAVARIIMA.
PhylomeDBQ8W033.

Enzyme and pathway databases

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

Gene expression databases

ArrayExpressQ8W033.
GenevestigatorQ8W033.

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.
IPR016160. Ald_DH_CS_CYS.
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.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL3I1_ARATH
AccessionPrimary (citable) accession number: Q8W033
Secondary accession number(s): Q940H4, Q9SYY9
Entry history
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 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