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UniProtKB/Swiss-Prot entry Q8W033


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AL3I1_ARATH
Primary accession number Q8W033
Secondary accession numbers Q940H4 Q9SYY9
Integrated into Swiss-Prot on October 31, 2006
Sequence was last modified on October 31, 2006 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 35)
Name and origin of the protein
Protein name Aldehyde dehydrogenase family 3 member I1, chloroplastic [Precursor]
Synonyms AtALDH3
EC 1.2.1.3
Gene name
Name: ALDH3I1
OrderedLocusNames: At4g34240
ORFNames: F10M10.10
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INDUCTION.
PubMed=11849595 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Nair A., Bartels D.;
"Novel ABA- and dehydration-inducible aldehyde dehydrogenase genes isolated from the resurrection plant Craterostigma plantagineum and Arabidopsis thaliana.";
Plant J. 28:555-567(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/47134; PubMed=10617198 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
Nature 402:769-777(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=cv. Columbia;
DOI=10.1126/science.1088305; PubMed=14593172 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Empirical analysis of transcriptional activity in the Arabidopsis genome.";
Science 302:842-846(2003).
[4]
FUNCTION, AND INDUCTION.
DOI=10.1046/j.1365-313X.2003.01819.x; PubMed=12904208 [NCBI, ExPASy, EBI, Israel, Japan]
Sunkar R., Bartels D., Kirch H.-H.;
"Overexpression of a stress-inducible aldehyde dehydrogenase gene from Arabidopsis thaliana in transgenic plants improves stress tolerance.";
Plant J. 35:452-464(2003).
[5]
NOMENCLATURE.
DOI=10.1016/j.tplants.2004.06.004; PubMed=15358267 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Bartels D., Wei Y., Schnable P.S., Wood A.J.;
"The ALDH gene superfamily of Arabidopsis.";
Trends Plant Sci. 9:371-377(2004).
[6]
INDUCTION.
DOI=10.1007/s11103-004-7796-6; PubMed=15830124 [NCBI, ExPASy, EBI, Israel, Japan]
Kirch H.-H., Schlingensiepen S., Kotchoni S., Sunkar R., Bartels D.;
"Detailed expression analysis of selected genes of the aldehyde dehydrogenase(ALDH) gene superfamily in Arabidopsis thaliana.";
Plant Mol. Biol. 57:315-322(2005).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AJ306961; CAC84903.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL035521; CAB36701.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161585; CAB80141.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY054633; AAK96824.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY081532; AAM10094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04770; T04770.
RefSeq NP_567962.1; -.
UniGene At.26454
3D structure databases
HSSP P11883; 1AD3. [HSSP ENTRY / PDB]
ModBase Q8W033.
Organism-specific databases
TAIR At4g34240; -.
Ontologies
GO
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from electronic annotation from EC).
QuickGo view.
Family and domain databases
InterPro IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR012394; Ald_DHase_NAD(P).
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.
Gene3D G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.
PANTHER PTHR11699; Aldehyde_dehyd; 1.
PTHR11699:SF15; ALDH; 1.
Pfam PF00171; Aldedh; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF036492; ALDH; 1.
PROSITE PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
BLOCKS Q8W033.
Genome annotation databases
GeneID 829573; -.
GenomeReviews CT486007_GR; AT4G34240.
KEGG ath:AT4G34240; -.
NMPDR fig|3702.1.peg.21486; -.
Other
ProtoNet Q8W033.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Chloroplast; Complete proteome; NAD; Oxidoreductase; Plastid; Stress response; Transit peptide.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
TRANSIT   1    59  59     Chloroplast (Potential). 
CHAIN   60   550  491     Aldehyde dehydrogenase family 3 member I1, chloroplastic. PRO_0000256061
NP_BIND   259   264  6     NAD (By similarity). 
ACT_SITE   281   281        Proton acceptor (By similarity). 
ACT_SITE   316   316        Nucleophile (By similarity). 
SITE   186   186  1     Transition state stabilizer (By similarity). 
CONFLICT   32    32        R -> L (in Ref. 1; CAC84903). 
CONFLICT   71    71        S -> R (in Ref. 1; CAC84903). 
CONFLICT   435   435        P -> S (in Ref. 1; CAC84903). 
CONFLICT   536   536        I -> M (in Ref. 1; CAC84903). 
Sequence information
Length: 550 AA [This is the length of the unprocessed precursor] Molecular weight: 60173 Da [This is the MW of the unprocessed precursor] CRC64: 42FC2BC37757A083 [This is a checksum on the sequence]
        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 

Q8W033 in FASTA format

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