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   16-JUN-2009, entry version 43.
DE   RecName: Full=Aldehyde dehydrogenase family 3 member I1, chloroplastic;
DE            Short=AtALDH3;
DE            EC=1.2.1.3;
DE   Flags: Precursor;
GN   Name=ALDH3I1; OrderedLocusNames=At4g34240; ORFNames=F10M10.10;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
RX   MEDLINE=21839899; PubMed=11849595;
RX   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
RT   isolated from the resurrection plant Craterostigma plantagineum and
RT   Arabidopsis thaliana.";
RL   Plant J. 28:555-567(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083488; PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G.,
RA   Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N.,
RA   Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M.,
RA   Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M.,
RA   Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T.,
RA   Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I.,
RA   Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P.,
RA   Langham S.-A., McCullagh B., Bilham L., Robben J.,
RA   van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F.,
RA   Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E.,
RA   Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W.,
RA   Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P.,
RA   Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H.,
RA   De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R.,
RA   van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S.,
RA   Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R.,
RA   Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S.,
RA   Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H.,
RA   Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A.,
RA   Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R.,
RA   Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S.,
RA   Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E.,
RA   Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A.,
RA   Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T.,
RA   Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C.,
RA   Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S.,
RA   Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K.,
RA   Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L.,
RA   Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J.,
RA   Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J.,
RA   Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D.,
RA   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.,
RA   Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C.,
RA   Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C.,
RA   Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R.,
RA   Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S.,
RA   Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A.,
RA   Chen E., Marra M.A., Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J.,
RA   Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F.,
RA   Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.,
RA   Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J.,
RA   Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y.,
RA   Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P.,
RA   Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F.,
RA   Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M.,
RA   Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J.,
RA   Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T.,
RA   Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y.,
RA   Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [4]
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   [5]
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   [6]
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).
CC   -!- FUNCTION: Involved in oxidative stress tolerance by detoxifying
CC       reactive aldehydes derived from lipid peroxidation.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + NAD(+) + H(2)O = an acid + NADH.
CC   -!- SUBUNIT: Homotetramer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Plastid, chloroplast (Potential).
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   -!- MISCELLANEOUS: Plants overexpressing ALDH3I1 show improved
CC       tolerance when exposed to dehydration, salt stress, heavy metals
CC       and H(2)O(2).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAB36701.1; Type=Erroneous gene model prediction;
CC       Sequence=CAB80141.1; Type=Erroneous gene model prediction;
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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; AY054633; AAK96824.1; -; mRNA.
DR   EMBL; AY081532; AAM10094.1; -; mRNA.
DR   IPI; IPI00516417; -.
DR   PIR; T04770; T04770.
DR   RefSeq; NP_567962.1; -.
DR   UniGene; At.26454; -.
DR   HSSP; P11883; 1AD3.
DR   PRIDE; Q8W033; -.
DR   GeneID; 829573; -.
DR   GenomeReviews; CT486007_GR; AT4G34240.
DR   KEGG; ath:AT4G34240; -.
DR   NMPDR; fig|3702.1.peg.21486; -.
DR   TAIR; At4g34240; -.
DR   OMA; Q8W033; FANCGQT.
DR   BRENDA; 1.2.1.3; 302.
DR   GO; GO:0009507; C:chloroplast; IDA:TAIR.
DR   GO; GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:EC.
DR   GO; GO:0004030; F:aldehyde dehydrogenase [NAD(P)+] activity; IEA:InterPro.
DR   GO; GO:0006081; P:cellular aldehyde metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0009737; P:response to abscisic acid stimulus; IEP:TAIR.
DR   GO; GO:0009414; P:response to water deprivation; IEP:TAIR.
DR   InterPro; IPR016160; Ald_DH_CS.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR012394; Aldehyde_DH_NAD(P).
DR   Gene3D; G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
DR   PANTHER; PTHR11699; Aldehyde_dehyd; 1.
DR   PANTHER; PTHR11699:SF15; ALDH; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   PIRSF; PIRSF036492; ALDH; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Chloroplast; Complete proteome; NAD;
KW   Oxidoreductase; Plastid; Stress response; Transit peptide.
FT   TRANSIT       1     59       Chloroplast (Potential).
FT   CHAIN        60    550       Aldehyde dehydrogenase family 3 member
FT                                I1, chloroplastic.
FT                                /FTId=PRO_0000256061.
FT   NP_BIND     259    264       NAD (By similarity).
FT   ACT_SITE    281    281       Proton acceptor (By similarity).
FT   ACT_SITE    316    316       Nucleophile (By similarity).
FT   SITE        186    186       Transition state stabilizer (By
FT                                similarity).
FT   CONFLICT     32     32       R -> L (in Ref. 1; CAC84903).
FT   CONFLICT     71     71       S -> R (in Ref. 1; CAC84903).
FT   CONFLICT    435    435       P -> S (in Ref. 1; CAC84903).
FT   CONFLICT    536    536       I -> M (in Ref. 1; CAC84903).
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
//