Q70DU8 (AL3H1_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Aldehyde dehydrogenase family 3 member H1
Short name=AtALDH4
EC=1.2.1.3

Gene names

Name:	ALDH3H1
Ordered Locus Names:	At1g44170
ORF Names:	T7O23.15

Organism

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

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Viridiplantae › Streptophyta › Streptophytina › Embryophyta › Tracheophyta › Euphyllophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › malvids › Brassicales › Brassicaceae › Camelineae › Arabidopsis

Protein attributes

Sequence length	484 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Catalytic activity	An aldehyde + NAD+ + H2O = a carboxylate + NADH.
Subunit structure	Homotetramer By similarity.
Induction	By abscisic acid (ABA), dehydration and salt stress in roots. Ref.5
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
Biological process	Stress response
Coding sequence diversity	Alternative splicing
Ligand	NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular aldehyde metabolic process Inferred from electronic annotation. Source: InterPro response to abscisic acid stimulus Inferred from expression pattern Ref.5. Source: TAIR response to desiccation Inferred from expression pattern Ref.5. Source: TAIR response to salt stress Inferred from expression pattern Ref.5. Source: TAIR
Cellular_component	Golgi apparatus Inferred from direct assay PubMed 22430844. Source: TAIR endoplasmic reticulum Inferred from direct assay PubMed 16618929PubMed 22923678. Source: TAIR membrane Inferred from direct assay PubMed 17432890. Source: TAIR plasmodesma Inferred from direct assay PubMed 21533090. Source: TAIR plastid Inferred from sequence or structural similarity PubMed 11849595. Source: TAIR vacuole Inferred from direct assay PubMed 15539469. Source: TAIR
Molecular_function	3-chloroallyl aldehyde dehydrogenase activity Inferred from sequence or structural similarity PubMed 11849595. Source: TAIR aldehyde dehydrogenase (NAD) activity Inferred from direct assay PubMed 21166653. Source: TAIR aldehyde dehydrogenase [NAD(P)+] activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 1 isoform produced by alternative splicing. [Select]

Note: A number of isoforms are produced. According to EST sequences.

Isoform 1 (identifier: Q70DU8-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 484	484	Aldehyde dehydrogenase family 3 member H1		PRO_0000256060
Regions
	Nucleotide binding	196 – 201	6	NAD By similarity
Sites
	Active site	218	1	Proton acceptor By similarity
	Active site	253	1	Nucleophile By similarity
	Site	123	1	Transition state stabilizer By similarity
Experimental info
	Sequence conflict	200	1	I → V in CAE51203. Ref.5
	Sequence conflict	272	1	A → D in CAE51203. Ref.5
	Sequence conflict	300	1	F → L in CAE51203. Ref.5
	Sequence conflict	391	1	A → T in AAM61211. Ref.4
	Sequence conflict	435	1	F → S in CAE51203. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 31, 2006. Version 2. Checksum: 5D931EF77293F668	FASTA	484	53,159
	10 20 30 40 50 60 MAAKKVFGSA EASNLVTELR RSFDDGVTRG YEWRVTQLKK LMIICDNHEP EIVAALRDDL 70 80 90 100 110 120 GKPELESSVY EVSLLRNSIK LALKQLKNWM APEKAKTSLT TFPASAEIVS EPLGVVLVIS 130 140 150 160 170 180 AWNYPFLLSI DPVIGAISAG NAVVLKPSEL APASSALLTK LLEQYLDPSA VRVVEGAVTE 190 200 210 220 230 240 TSALLEQKWD KIFYTGSSKI GRVIMAAAAK HLTPVVLELG GKSPVVVDSD TDLKVTVRRI 250 260 270 280 290 300 IVGKWGCNNG QACVSPDYIL TTKEYAPKLI DAMKLELEKF YGKNPIESKD MSRIVNSNHF 310 320 330 340 350 360 DRLSKLLDEK EVSDKIVYGG EKDRENLKIA PTILLDVPLD SLIMSEEIFG PLLPILTLNN 370 380 390 400 410 420 LEESFDVIRS RPKPLAAYLF THNKKLKERF AATVSAGGIV VNDIAVHLAL HTLPFGGVGE 430 440 450 460 470 480 SGMGAYHGKF SFDAFSHKKA VLYRSLFGDS AVRYPPYSRG KLRLLKALVD SNIFDLFKVL LGLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana." Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K. , Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W. Nature 408:816-820(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[2]	The Arabidopsis Information Resource (TAIR) Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases Cited for: GENOME REANNOTATION. Strain: cv. Columbia.
[3]	"Empirical analysis of transcriptional activity in the Arabidopsis genome." 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. Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: cv. Columbia.
[4]	"Full-length cDNA from Arabidopsis thaliana." Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B., Feldmann K.A. Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"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] OF 5-484, INDUCTION.
[6]	"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	AC074228 Genomic DNA. Translation: AAG50550.1. CP002684 Genomic DNA. Translation: AEE32025.1. CP002684 Genomic DNA. Translation: AEE32026.1. AY072122 mRNA. Translation: AAL59944.1. AY084648 mRNA. Translation: AAM61211.1. AJ585241 mRNA. Translation: CAE51203.1.
IPI	IPI00527744.
PIR	H96505.
RefSeq	NP_175081.1. NM_103541.3. NP_849770.1. NM_179439.3.
UniGene	At.17189. At.48278.
3D structure databases
HSSP	HSSP built from PDB template 1AD3 based on UniProtKB P11883.
ProteinModelPortal	Q70DU8.
SMR	Q70DU8. Positions 13-456.
ModBase	Search...
Proteomic databases
PaxDb	Q70DU8.
PRIDE	Q70DU8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT1G44170.1; AT1G44170.1; AT1G44170. AT1G44170.2; AT1G44170.2; AT1G44170.
GeneID	841020.
KEGG	ath:AT1G44170.
Organism-specific databases
TAIR	At1g44170.
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HOG000271515.
InParanoid	Q70DU8.
KO	K00128.
OMA	YPFVLTM.
PhylomeDB	Q70DU8.
ProtClustDB	PLN02174.
Gene expression databases
ArrayExpress	Q70DU8.
Genevestigator	Q70DU8.
Family and domain databases
Gene3D	3.40.309.10. 1 hit. 3.40.605.10. 1 hit.
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016163. Ald_DH_C. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR012394. Aldehyde_DH_NAD(P). [Graphical view]
PANTHER	PTHR11699:SF15. PTHR11699:SF15. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PIRSF	PIRSF036492. ALDH. 1 hit.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 1 hit.
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. False negative. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AL3H1_ARATH

Accession

Primary (citable) accession number: Q70DU8
Secondary accession number(s): Q8LFT7, Q9C6Y7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	October 31, 2006
Last modified:	May 1, 2013
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program