AL3I1_ARATH
ID AL3I1_ARATH Reviewed; 550 AA.
AC Q8W033; Q940H4; Q9SYY9;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Aldehyde dehydrogenase family 3 member I1, chloroplastic;
DE Short=AtALDH3;
DE Short=Ath-ALDH3;
DE EC=1.2.1.3;
DE Flags: Precursor;
GN Name=ALDH3I1; Synonyms=ALDH3; OrderedLocusNames=At4g34240;
GN ORFNames=F10M10.10;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX PubMed=11849595; DOI=10.1046/j.1365-313x.2001.01176.x;
RA Kirch H.-H., Nair A., Bartels D.;
RT "Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated
RT from the resurrection plant Craterostigma plantagineum and Arabidopsis
RT thaliana.";
RL Plant J. 28:555-567(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP FUNCTION, AND INDUCTION.
RX PubMed=12904208; DOI=10.1046/j.1365-313x.2003.01819.x;
RA Sunkar R., Bartels D., Kirch H.-H.;
RT "Overexpression of a stress-inducible aldehyde dehydrogenase gene from
RT Arabidopsis thaliana in transgenic plants improves stress tolerance.";
RL Plant J. 35:452-464(2003).
RN [6]
RP NOMENCLATURE.
RX PubMed=15358267; DOI=10.1016/j.tplants.2004.06.004;
RA Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
RT "The ALDH gene superfamily of Arabidopsis.";
RL Trends Plant Sci. 9:371-377(2004).
RN [7]
RP INDUCTION.
RX PubMed=15830124; DOI=10.1007/s11103-004-7796-6;
RA Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
RT "Detailed expression analysis of selected genes of the aldehyde
RT dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
RL Plant Mol. Biol. 57:315-332(2005).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP MUTAGENESIS OF CYS-114; CYS-142; VAL-263; CYS-286; CYS-310 AND CYS-316,
RP ACTIVITY REGULATION, AND 3D-STRUCTURE MODELING.
RX PubMed=21166653; DOI=10.1042/bj20101337;
RA Stiti N., Adewale I.O., Petersen J., Bartels D., Kirch H.H.;
RT "Engineering the nucleotide coenzyme specificity and sulfhydryl redox
RT sensitivity of two stress-responsive aldehyde dehydrogenase isoenzymes of
RT Arabidopsis thaliana.";
RL Biochem. J. 434:459-471(2011).
RN [9]
RP 3D-STRUCTURE MODELING.
RX PubMed=24463048; DOI=10.1016/j.bbapap.2014.01.008;
RA Stiti N., Podgorska K., Bartels D.;
RT "Aldehyde dehydrogenase enzyme ALDH3H1 from Arabidopsis thaliana:
RT Identification of amino acid residues critical for cofactor specificity.";
RL Biochim. Biophys. Acta 1844:681-693(2014).
CC -!- FUNCTION: Involved in oxidative stress tolerance by detoxifying
CC reactive aldehydes derived from lipid peroxidation. Medium- to long-
CC chain saturated aldehydes are preferred substrates, while the short-
CC chain aldehyde propanal is a weak substrate. Can use both NAD(+) and
CC NADP(+), but the coenzyme preference is substrate dependent.
CC {ECO:0000269|PubMed:12904208, ECO:0000269|PubMed:21166653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH;
CC Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.3;
CC Evidence={ECO:0000269|PubMed:21166653};
CC -!- ACTIVITY REGULATION: Thiol-based regulation. Inactivation after
CC dimerization under oxidizing conditions. {ECO:0000269|PubMed:21166653}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8053 uM for propionaldehyde {ECO:0000269|PubMed:21166653};
CC KM=111 uM for hexanal {ECO:0000269|PubMed:21166653};
CC KM=24 uM for octanal {ECO:0000269|PubMed:21166653};
CC KM=7 uM for nonanal {ECO:0000269|PubMed:21166653};
CC KM=1.3 uM for dodecanal {ECO:0000269|PubMed:21166653};
CC KM=151 uM for trans-2-hexenal {ECO:0000269|PubMed:21166653};
CC KM=5.5 uM for trans-2-nonenal {ECO:0000269|PubMed:21166653};
CC KM=21 uM for 4-hydroxynonenal {ECO:0000269|PubMed:21166653};
CC KM=71 uM for NAD(+) (in the presence of hexanal as co-substrate)
CC {ECO:0000269|PubMed:21166653};
CC KM=1868 uM for NADP(+) (in the presence of hexanal as co-substrate)
CC {ECO:0000269|PubMed:21166653};
CC KM=53 uM for NAD(+) (in the presence of trans-2-nonenal as co-
CC substrate) {ECO:0000269|PubMed:21166653};
CC KM=87 uM for NADP(+) (in the presence of trans-2-nonenal as co-
CC substrate) {ECO:0000269|PubMed:21166653};
CC Vmax=10.1 umol/min/mg enzyme with propionaldehyde as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=17.3 umol/min/mg enzyme with hexanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=16.6 umol/min/mg enzyme with octanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=20 umol/min/mg enzyme with nonanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=18.8 umol/min/mg enzyme with dodecanal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=1.5 umol/min/mg enzyme with trans-2-hexenal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=1.6 umol/min/mg enzyme with trans-2-nonenal as substrate
CC {ECO:0000269|PubMed:21166653};
CC Vmax=0.6 umol/min/mg enzyme with 4-hydroxynonenal as substrate
CC {ECO:0000269|PubMed:21166653};
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:21166653};
CC -!- SUBUNIT: Homodimer and homomultimer. {ECO:0000269|PubMed:21166653}.
CC -!- SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8W033-1; Sequence=Displayed;
CC -!- INDUCTION: By abscisic acid (ABA), dehydration, salt stress in
CC plantlets. Induced by heavy metals and H(2)O(2).
CC {ECO:0000269|PubMed:11849595, ECO:0000269|PubMed:12904208,
CC ECO:0000269|PubMed:15830124}.
CC -!- MISCELLANEOUS: Plants overexpressing ALDH3I1 show improved tolerance
CC when exposed to dehydration, salt stress, heavy metals and H(2)O(2).
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB36701.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80141.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AJ306961; CAC84903.1; -; mRNA.
DR EMBL; AL035521; CAB36701.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161585; CAB80141.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86347.1; -; Genomic_DNA.
DR EMBL; AY054633; AAK96824.1; -; mRNA.
DR EMBL; AY081532; AAM10094.1; -; mRNA.
DR PIR; T04770; T04770.
DR RefSeq; NP_567962.1; NM_119588.6. [Q8W033-1]
DR AlphaFoldDB; Q8W033; -.
DR SMR; Q8W033; -.
DR STRING; 3702.AT4G34240.1; -.
DR iPTMnet; Q8W033; -.
DR PaxDb; Q8W033; -.
DR PRIDE; Q8W033; -.
DR ProteomicsDB; 245025; -. [Q8W033-1]
DR EnsemblPlants; AT4G34240.1; AT4G34240.1; AT4G34240. [Q8W033-1]
DR GeneID; 829573; -.
DR Gramene; AT4G34240.1; AT4G34240.1; AT4G34240. [Q8W033-1]
DR KEGG; ath:AT4G34240; -.
DR Araport; AT4G34240; -.
DR TAIR; locus:2116134; AT4G34240.
DR eggNOG; KOG2456; Eukaryota.
DR HOGENOM; CLU_005391_3_0_1; -.
DR InParanoid; Q8W033; -.
DR PhylomeDB; Q8W033; -.
DR BioCyc; ARA:AT4G34240-MON; -.
DR PRO; PR:Q8W033; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q8W033; baseline and differential.
DR Genevisible; Q8W033; AT.
DR GO; GO:0009507; C:chloroplast; HDA:TAIR.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR GO; GO:0009536; C:plastid; ISS:TAIR.
DR GO; GO:0004028; F:3-chloroallyl aldehyde dehydrogenase activity; ISS:TAIR.
DR GO; GO:0004029; F:aldehyde dehydrogenase (NAD+) activity; IDA:TAIR.
DR GO; GO:0033721; F:aldehyde dehydrogenase (NADP+) activity; IDA:TAIR.
DR GO; GO:0043878; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0006081; P:cellular aldehyde metabolic process; IBA:GO_Central.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR PANTHER; PTHR43570; PTHR43570; 1.
DR Pfam; PF00171; Aldedh; 1.
DR PIRSF; PIRSF036492; ALDH; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chloroplast; Disulfide bond; NAD; Oxidoreductase;
KW Plastid; Reference proteome; Stress response; Transit peptide.
FT TRANSIT 1..59
FT /note="Chloroplast"
FT /evidence="ECO:0000255"
FT CHAIN 60..550
FT /note="Aldehyde dehydrogenase family 3 member I1,
FT chloroplastic"
FT /id="PRO_0000256061"
FT ACT_SITE 281
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT ACT_SITE 316
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 259..264
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT SITE 186
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT DISULFID 114
FT /note="Interchain"
FT MUTAGEN 114
FT /note="C->S: No effect on solubility, but loss of
FT dimerization and 80% loss of activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 142
FT /note="C->S: No effect on solubility, but decreased
FT activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 263
FT /note="V->I: No effect on substrate specificity, but
FT decreased affinity for NADP(+) and increased affinity for
FT NAD(+)."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 286
FT /note="C->S: No effect on solubility, but no effect on
FT activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 310
FT /note="C->S: No effect on solubility, but no effect on
FT activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT MUTAGEN 316
FT /note="C->S: No effect on solubility, but loss of
FT activity."
FT /evidence="ECO:0000269|PubMed:21166653"
FT CONFLICT 32
FT /note="R -> L (in Ref. 1; CAC84903)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="S -> R (in Ref. 1; CAC84903)"
FT /evidence="ECO:0000305"
FT CONFLICT 435
FT /note="P -> S (in Ref. 1; CAC84903)"
FT /evidence="ECO:0000305"
FT CONFLICT 536
FT /note="I -> M (in Ref. 1; CAC84903)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 550 AA; 60173 MW; 42FC2BC37757A083 CRC64;
MTKLLEINHI QTLCFAKGFS PARLNVATSP FRISRRGGGG YCSNACIPYR LKFTCYATLS
AVVKEQASDF SGKEAALLVD ELRSNFNSGR TKSYEWRISQ LQNIARMIDE KEKCITEALY
QDLSKPELEA FLAEISNTKS SCMLAIKELK NWMAPETVKT SVTTFPSSAQ IVSEPLGVVL
VISAWNFPFL LSVEPVIGAI AAGNAVVLKP SEIAPAASSL LAKLFSEYLD NTTIRVIEGG
VPETTALLDQ KWDKIFFTGG ARVARIIMAA AARNLTPVVL ELGGKCPALV DSDVNLQVAA
RRIIAGKWAC NSGQACIGVD YVITTKDFAS KLIDALKTEL ETFFGQNALE SKDLSRIVNS
FHFKRLESML KENGVANKIV HGGRITEDKL KISPTILLDV PEASSMMQEE IFGPLLPIIT
VQKIEDGFQV IRSKPKPLAA YLFTNNKELE KQFVQDVSAG GITINDTVLH VTVKDLPFGG
VGESGIGAYH GKFSYETFSH KKGVLYRSFS GDADLRYPPY TPKKKMVLKA LLSSNIFAAI
LAFFGFSKDS
