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UniProtKB/Swiss-Prot entry Q70E96


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

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Entry information
Entry name AL3F1_ARATH
Primary accession number Q70E96
Secondary accession number O65516
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 31)
Name and origin of the protein
Protein name Aldehyde dehydrogenase family 3 member F1
Synonym EC 1.2.1.3
Gene name
Name: ALDH3F1
OrderedLocusNames: At4g36250
ORFNames: F23E13.140
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 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND 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).
[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]
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).
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
AJ584644; CAE48163.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL022141; CAA18131.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL161589; CAB80296.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T04594; T04594.
RefSeq NP_195348.2; -.
UniGene At.27542
3D structure databases
HSSP P11883; 1AD3. [HSSP ENTRY / PDB]
ModBase Q70E96.
Protein-protein interaction databases
IntAct Q70E96; -.
Organism-specific databases
TAIR At4g36250; -.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
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; FALSE_NEG.
PS00687; ALDEHYDE_DEHYDR_GLU; FALSE_NEG.
BLOCKS Q70E96.
Genome annotation databases
GeneID 829782; -.
GenomeReviews CT486007_GR; AT4G36250.
KEGG ath:AT4G36250; -.
NMPDR fig|3702.1.peg.21723; -.
Other
ProtoNet Q70E96.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   484  484     Aldehyde dehydrogenase family 3 member F1. PRO_0000256059
NP_BIND   192   197  6     NAD (By similarity). 
ACT_SITE   214   214        Proton acceptor (By similarity). 
ACT_SITE   252   252        Nucleophile (By similarity). 
SITE   119   119  1     Transition state stabilizer (By similarity). 
CONFLICT   59    59        H -> L (in Ref. 1; CAE48163). 
CONFLICT   226   226        Missing (in Ref. 1; CAE48163). 
Sequence information
Length: 484 AA [This is the length of the unprocessed precursor] Molecular weight: 53615 Da [This is the MW of the unprocessed precursor] CRC64: A243419F0C926265 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEAMKETVEE SLREMRETFA SGRTRSLKWR KAQIGAIYEM VKDNEDKICN ALFQDLGKHS 

        70         80         90        100        110        120 
TEAFRDELGV VLRTATVAIN CLDKWAVPKH SKLPLLFYPA KGKVISEPYG TVLVLSSWNF 

       130        140        150        160        170        180 
PISLSLDPLI GAIAAGNTVL LKSSELSPNA SAFLAKTIPA YLDTKAIKVI EGGPDVATIL 

       190        200        210        220        230        240 
LQHQWDKIFF TGSPKIGRII MAAAAQHLTP VTLELGGKCP TIVDHHTISK NIKSVVKRIA 

       250        260        270        280        290        300 
GGKWGSCNGQ ACISVDYVLI EKSFAPTLID MLKPTIKSFF GENPKESGCL SRIANKHHVQ 

       310        320        330        340        350        360 
RLSRLLSDPR VQASIVYGGS IDEDKLYVEP TILLDPPLDS EIMNEEIFGP ILPIITVRDI 

       370        380        390        400        410        420 
QESIGIINTK PKPLAIYAFT NDENLKTRIL SETSSGSVTF NDVMIQYMCD ALPFGGVGES 

       430        440        450        460        470        480 
GIGRYHGKYS FDCFSHEKAI MEGSLGMDLE ARYPPWNNFK LTFIRLAFRE AYFKLILLML 


GLKR 

Q70E96 in FASTA format

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