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Q70E96 (AL3F1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 73. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde dehydrogenase family 3 member F1
EC=1.2.1.3
Gene names
Name:ALDH3F1
Ordered Locus Names:At4g36250
ORF Names:F23E13.140
OrganismArabidopsis thaliana (Mouse-ear cress) [Reference proteome]
Taxonomic identifier3702 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length484 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Subunit structure

Homotetramer By similarity.

Tissue specificity

Constituively expressed at low levels. Ref.1

Induction

Not induced by abscisic acid (ABA), dehydration and salt stress. Ref.1

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence caution

The sequence CAA18131.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAB80296.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 484484Aldehyde dehydrogenase family 3 member F1
PRO_0000256059

Regions

Nucleotide binding192 – 1976NAD By similarity

Sites

Active site2141Proton acceptor By similarity
Active site2521Nucleophile By similarity
Site1191Transition state stabilizer By similarity

Experimental info

Sequence conflict591H → L in CAE48163. Ref.1
Sequence conflict2261Missing in CAE48163. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q70E96 [UniParc].

Last modified October 31, 2006. Version 2.
Checksum: A243419F0C926265

FASTA48453,615
        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

« Hide

References

« Hide 'large scale' references
[1]"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: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, 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]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ584644 mRNA. Translation: CAE48163.1.
AL022141 Genomic DNA. Translation: CAA18131.1. Sequence problems.
AL161589 Genomic DNA. Translation: CAB80296.1. Sequence problems.
CP002687 Genomic DNA. Translation: AEE86639.1.
IPIIPI00516583.
PIRT04594.
RefSeqNP_195348.2. NM_119793.4.
UniGeneAt.27542.

3D structure databases

ProteinModelPortalQ70E96.
SMRQ70E96. Positions 8-455.
ModBaseSearch...

Protein-protein interaction databases

IntActQ70E96. 8 interactions.

Proteomic databases

PaxDbQ70E96.
PRIDEQ70E96.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsAT4G36250.1; AT4G36250.1; AT4G36250.
GeneID829782.
KEGGath:AT4G36250.

Organism-specific databases

TAIRAt4g36250.

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271515.
InParanoidQ70E96.
KOK00128.
OMAPLDSEIM.
PhylomeDBQ70E96.
ProtClustDBPLN02203.

Gene expression databases

ArrayExpressQ70E96.
GenevestigatorQ70E96.

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.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
IPR012394. Aldehyde_DH_NAD(P).
[Graphical view]
PANTHERPTHR11699:SF15. PTHR11699:SF15. 1 hit.
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
PIRSFPIRSF036492. ALDH. 1 hit.
SUPFAMSSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. False negative.
PS00687. ALDEHYDE_DEHYDR_GLU. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameAL3F1_ARATH
AccessionPrimary (citable) accession number: Q70E96
Secondary accession number(s): O65516
Entry history
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 29, 2013
This is version 73 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

Arabidopsis thaliana

Arabidopsis thaliana: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents