Reviewed, UniProtKB/Swiss-Prot Q70E96 (AL3F1_ARATH)

Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase family 3 member F1
    EC=1.2.1.3

Gene names

Name:	ALDH3F1
Ordered Locus Names:	At4g36250
ORF Names:	F23E13.140

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	An aldehyde + NAD+ + H2O = an acid + 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.

Ontologies

Keywords
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	cellular aldehyde metabolic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	endoplasmic reticulum Inferred from direct assay. Source: TAIR membrane Inferred from direct assay. Source: TAIR
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
	Q2V412	1	EBI-1237774,EBI-1238781
CALM	P62157	1	EBI-1237774,EBI-397403	From a different organism.
CAM1	P25854	1	EBI-1237774,EBI-1235664
CAM6	Q03509	1	EBI-1237774,EBI-1236097
CAM7	P59220	1	EBI-1237774,EBI-1236031
CML10	P30187	1	EBI-1237774,EBI-1238722
CML8	O23320	1	EBI-1237774,EBI-1237764
CML9	Q9S744	1	EBI-1237774,EBI-1236048

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 484	484	Aldehyde dehydrogenase family 3 member F1		PRO_0000256059
Regions
	Nucleotide binding	192 – 197	6	NAD By similarity
Sites
	Active site	214	1	Proton acceptor By similarity
	Active site	252	1	Nucleophile By similarity
	Site	119	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	59	1	H → L in CAE48163. Ref.1
	Sequence conflict	226	1	Missing in CAE48163. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q70E96-1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: A243419F0C926265	FASTA	484	53,615
	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

References

	« Hide 'large scale' referencesShow '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: 15830124] [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. , 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: 10617198] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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: 15358267] [Abstract] Cited for: NOMENCLATURE.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ584644 mRNA. Translation: CAE48163.1. AL022141 Genomic DNA. Translation: CAA18131.1. Sequence problems. AL161589 Genomic DNA. Translation: CAB80296.1. Sequence problems.
IPI	IPI00516583.
PIR	T04594.
RefSeq	NP_195348.2.
UniGene	At.27542
3D structure databases
HSSP	HSSP built from PDB template 1AD3 based on UniProtKB P11883.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q70E96. 8 interactions.
Proteomic databases
PRIDE	Q70E96.
Genome annotation databases
GeneID	829782.
GenomeReviews	Gene locus AT4G36250 in contig CT486007_GR.
KEGG	ath:AT4G36250.
NMPDR	fig|3702.1.peg.21723.
Organism-specific databases
TAIR	At4g36250.
Phylogenomic databases
OMA	Q70E96. FSHEKAI.
Enzyme and pathway databases
BRENDA	1.2.1.3. 302.
Family and domain databases
InterPro	IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. IPR012394. Aldehyde_DH_NAD(P). [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit. PTHR11699:SF15. ALDH. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF036492. ALDH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AL3F1_ARATH

Accession

Primary (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:	June 16, 2009
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)