Q7G9P4 (ALDO3_ARATH) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Abscisic-aldehyde oxidase
EC=1.2.3.14

Alternative name(s):
Aldehyde oxidase 3
Short name=AO-3
Short name=AtAO-3
Short name=AtAO4

Gene names

Name:	AAO3
Synonyms:	AO4
Ordered Locus Names:	At2g27150
ORF Names:	F20F1.2

Organism

Arabidopsis thaliana (Mouse-ear cress)

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	1332 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In higher plants aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. AO-delta seems to be involved in the last step of abscisic acid biosynthesis, at least in leaves and seeds. In vitro, AO-delta oxidizes abscisic aldehyde to abscisic acid (ABA). In vitro, AO-delta also uses indole-3-aldehyde (IAld), benzaldehyde, 1-naphthaldehyde and cinnamaldehyde as substrate; the AAO2-AAO3 dimer also uses abscisic aldehyde as substrate. Ref.6 Ref.7 Ref.10 Ref.11
Catalytic activity	Abscisic aldehyde + H2O + O2 = abscisate + H2O2.
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Molybdopterin By similarity.
Subunit structure	Aldehyde oxidases (AO) are homo- and heterodimers of AO subunits. AO-delta is a AAO3 homodimer. AAO3 also forms a dimer with AAO2. Interacts with PUB44, and this interaction probably results in targeting of this protein to the proteasome. Ref.1 Ref.6 Ref.12
Tissue specificity	Expressed in vascular tissues of all organs, particularly in phloem companion cells and xylem parenchymatic cells. Highly expressed in roots and rosettes, and to lower extent in seedlings, stems and flowers. Expressed at very low levels in siliques and dry seeds. Also detected in root dividing cells (tips and primordia), in mesophyll cells and inside the guard cells. Ref.1 Ref.4 Ref.5 Ref.6 Ref.7 Ref.10 Ref.11
Induction	Transcripts are induced by dehydration, in rosettes but not in roots. Induction by cold, ABA, sodium chloride (NaCl) and polyethylene glycol (PEG) is dependent of the zeaxanthin epoxidase ABA1 protein (ZEP). Induction by glucose requires the short chain alcohol dehydrogenase ABA2 protein. Repressed by mannitol. Ref.1 Ref.6 Ref.8 Ref.9
Miscellaneous	In vitro, can not discriminate between (+) and (-) enantiomers of abscisic acid and leads respectively to (+) and (-) cis-ABA.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.
Biophysicochemical properties	Kinetic parameters: All these kinetic values were obtained with AO-delta dimer. KM=0.51 µM for abscisic aldehyde Ref.6 KM=34 µM for indole-3-aldehyde KM=44 µM for benzaldehyde KM=1.8 µM for 1-naphthaldehyde KM=700 µM for cinnamaldehyde

Ontologies

Keywords
Biological process	Abscisic acid biosynthesis Auxin biosynthesis
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	abscisic acid biosynthetic process Inferred from mutant phenotype Ref.7. Source: TAIR auxin biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: TAIR
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW abscisic aldehyde oxidase activity Inferred from direct assay Ref.7. Source: TAIR electron carrier activity Inferred from electronic annotation. Source: InterPro flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro indole-3-acetaldehyde oxidase activity Inferred from direct assay Ref.6. Source: TAIR iron ion binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on CH-OH group of donors Inferred from electronic annotation. Source: InterPro ubiquitin protein ligase binding Inferred from physical interaction Ref.12. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1332	1332	Abscisic-aldehyde oxidase		PRO_0000166111
Regions
	Domain	1 – 88	88	2Fe-2S ferredoxin-type
	Domain	219 – 400	182	FAD-binding PCMH-type
Sites
	Metal binding	40	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	45	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	48	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Mutagenesis	821 – 826	6	LQRPVK → WDLDQ in aao3-3; wilty phenotype in rosette leaves, reduced ABA levels, reduced dormancy, abnormal water loss and abnormal response to water deficit. Ref.11

Sequences

	Sequence		Length	Mass (Da)
	Q7G9P4 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 084ED4BEE64B121B	FASTA	1,332	146,701
	10 20 30 40 50 60 MDLEFAVNGE RFKIDSVDPS TTLLEFLRLN TPFKSVKLGC GEGGCGACLV VLSKYDPELD 70 80 90 100 110 120 QVKECCINSC LTLLCSVNGC SITTSEGLGN TKKGFHPIHK RFAGFHASQC GFCTPGMCIS 130 140 150 160 170 180 LYSSLANAEN NSSKDFTVSE AEKSVSGNLC RCTGYRPIVD ACKSFASDVD IEDLGLNSFW 190 200 210 220 230 240 KKGESKEVMF KNLPPYNPKD HLVTFPEFLK KKEKVDNGSD HLKYRWTTPF SVAELHNIME 250 260 270 280 290 300 AANSGDSLKL VVGNTGTGYY KDEERFDRYI DISNIPEMSM IKKDEKGIEI GAAVTISNAI 310 320 330 340 350 360 DALEKESKSS YVFKKMATHM EKIGNRSIRN SGSIGGNLVM AQSRKFPSDV TTLLLAVDAS 370 380 390 400 410 420 VYMLNGRKTE KVTLQEFLEL SPVLDSKRVL LKVEIPSWTA PSGDDTEFLF ESYRAAPRSI 430 440 450 460 470 480 GNALPYLNAA FLALVSRQEA SRKGVTVEKC FLAFGSYGGD HSIRAIEVET FLTGKLLSYS 490 500 510 520 530 540 VLYEAVGLLK GIIVPGKDTL HSEYRKSLAV GYLFEFFYPL IESGHRICSL DSGNKHNNSH 550 560 570 580 590 600 VDTVKSLPFL SSSQQVLESN EFKPIGEAVI KVGAALQASG EAVFVDDIPT LPDCLHGAFI 610 620 630 640 650 660 YSTEPLAKIK SLSFRENVTP TGVFAVLTFK DIPQQGQNIG SKTLFGPGPL FADELTRCAG 670 680 690 700 710 720 QRIALVVADT QKHADMAAKL AVVEYDTKNL EQPILTVEDA VKRSSFFEVH PMFYPEPVGD 730 740 750 760 770 780 VIKGMEEAER KIISSELRLG SQYFFYMEPQ TALALPDEDN CVKVFSSSQA PEYVHSVIAT 790 800 810 820 830 840 CLGIQEHNVR VITRRVGGGF GGKAVKSMPV ATACALGAYK LQRPVKMFLN RKTDMIMAGG 850 860 870 880 890 900 RHPMKINYNV GFRSDGKLTA LELTMLIDAG LEPDVSPIMP RNIMGPLRKY DWGALSFDVK 910 920 930 940 950 960 VCKTNCLSRT AMRAPGEVQG SYIAESIIEN VASSLQMDVD AVRKINLHTY DSLRKFYNHI 970 980 990 1000 1010 1020 AGDPDEYTLP LLWEKLEISS KFKERSEMVK EFNLCNVWRK RGISRVPIVH QVMQRPTPGK 1030 1040 1050 1060 1070 1080 VSILSDGSVV VEVGGIEIGQ GLWTKVQQMV AYGLGMVKCE GNEKLLDRIR VVQSDTLGMI 1090 1100 1110 1120 1130 1140 QGGFTAGSTT SESSCEAVRL CCVILVERLK PIMDQMMMEK SGSVTWNILI QQAYGQYINL 1150 1160 1170 1180 1190 1200 SASTLYKPEY SSMEYLNYGV GVSEVEVDLV TGKTEILRSD IIYDCGKSLN PAVDLGQTEG 1210 1220 1230 1240 1250 1260 AFVQGIGFFM MEEYTTDEKG LVVQQGTWDY KIPTVDTIPK HFNVEIVNTG HHKNRVLSSK 1270 1280 1290 1300 1310 1320 ASGEPPLLLA ASVHCATRSA IREARKHSLS SNFIDGSDSE FELPVPATMP VVKSLCGLYS 1330 VEKYLQGKIK GQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis." Koiwai H., Nakaminami K., Seo M., Mitsuhashi W., Toyomasu T., Koshiba T. Plant Physiol. 134:1697-1707(2004) [PubMed: 15064376] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY, INDUCTION. Strain: cv. Columbia. Tissue: Seedling hypocotyl.
[2]	"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana." Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S., Cronin L.A. , Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C. Nature 402:761-768(1999) [PubMed: 10617197] [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]	"Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana." Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S., Liotenberg S., Marion-Poll A., Caboche M., Kamiya Y., Koshiba T. Plant Cell Physiol. 39:433-442(1998) [PubMed: 9615466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 347-1332, TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Seedling hypocotyl.
[5]	"Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana." Seo M., Akaba S., Oritani T., Delarue M., Bellini C., Caboche M., Koshiba T. Plant Physiol. 116:687-693(1998) [PubMed: 9489015] [Abstract] Cited for: TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.
[6]	"Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana." Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T. Plant J. 23:481-488(2000) [PubMed: 10972874] [Abstract] Cited for: FUNCTION, INDUCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
[7]	"The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves." Seo M., Peeters A.J.M., Koiwai H., Oritani T., Marion-Poll A., Zeevaart J.A.D., Koornneef M., Kamiya Y., Koshiba T. Proc. Natl. Acad. Sci. U.S.A. 97:12908-12913(2000) [PubMed: 11050171] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, MUTANT AAO3.
[8]	"Regulation of osmotic stress-responsive gene expression by the LOS6/ABA1 locus in Arabidopsis." Xiong L., Lee H., Ishitani M., Zhu J.-K. J. Biol. Chem. 277:8588-8596(2002) [PubMed: 11779861] [Abstract] Cited for: INDUCTION.
[9]	"A unique short-chain dehydrogenase/reductase in Arabidopsis glucose signaling and abscisic acid biosynthesis and functions." Cheng W.-H., Endo A., Zhou L., Penney J., Chen H.-C., Arroyo A., Leon P., Nambara E., Asami T., Seo M., Koshiba T., Sheen J. Plant Cell 14:2723-2743(2002) [PubMed: 12417697] [Abstract] Cited for: INDUCTION.
[10]	"Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds." Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T. Plant Cell Physiol. 45:1694-1703(2004) [PubMed: 15574845] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY.
[11]	"Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in abscisic acid biosynthesis in seeds." Gonzalez-Guzman M., Abia D., Salinas J., Serrano R., Rodriguez P.L. Plant Physiol. 135:325-333(2004) [PubMed: 15122034] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, MUTAGENESIS OF 821-LEU--LYS-826.
[12]	"Identification of a novel E3 ubiquitin ligase that is required for suppression of premature senescence in Arabidopsis." Raab S., Drechsel G., Zarepour M., Hartung W., Koshiba T., Bittner F., Hoth S. Plant J. 59:39-51(2009) [PubMed: 19309463] [Abstract] Cited for: INTERACTION WITH PUB44.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB016622 mRNA. Translation: BAA82672.1. AC007154 Genomic DNA. Translation: AAD22498.1. CP002685 Genomic DNA. Translation: AEC07944.1. CP002685 Genomic DNA. Translation: AEC07945.1. AB010080 mRNA. Translation: BAA28630.1.
IPI	IPI00517261.
PIR	D84669. T52176.
RefSeq	NP_001077966.1. NM_001084497.1. NP_180283.1. NM_128273.2.
UniGene	At.20239.
3D structure databases
ProteinModelPortal	Q7G9P4.
SMR	Q7G9P4. Positions 1-525, 564-1317.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7G9P4.
Proteomic databases
PRIDE	Q7G9P4.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblPlants	AT2G27150.1; AT2G27150.1; AT2G27150. AT2G27150.2; AT2G27150.2; AT2G27150.
GeneID	817257.
GenomeReviews	Gene locus AT2G27150 in contig CT485783_GR.
KEGG	ath:AT2G27150.
NMPDR	fig|3702.1.peg.9746.
Organism-specific databases
GeneFarm	4894. 470.
TAIR	At2g27150.
Phylogenomic databases
eggNOG	KOG0430.
GeneTree	EPGT00050000011134.
HOGENOM	HBG746468.
InParanoid	Q7G9P4.
OMA	ADELTRC.
PhylomeDB	Q7G9P4.
ProtClustDB	PLN00192.
Enzyme and pathway databases
BioCyc	ARA:AT2G27150-MONOMER. MetaCyc:AT2G27150-MONOMER.
BRENDA	1.2.3.14. 399.
Gene expression databases
ArrayExpress	Q7G9P4.
Genevestigator	Q7G9P4.
GermOnline	AT2G27150. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002888. 2Fe-2S-bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR016208. Ald_Oxase/xanthine_DH. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR012675. Beta-grasp_ferredoxin-type. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_FAD-bd. [Graphical view]
Gene3D	G3DSA:1.10.150.120. 2Fe-2S-bd. 1 hit. G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 4 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
KO	K09842.
Pfam	PF01315. Ald_Xan_dh_C. 1 hit. PF02738. Ald_Xan_dh_C2. 1 hit. PF03450. CO_deh_flav_C. 1 hit. PF00941. FAD_binding_5. 1 hit. PF00111. Fer2. 1 hit. PF01799. Fer2_2. 1 hit. [Graphical view]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
SMART	SM01008. Ald_Xan_dh_C. 1 hit. SM01092. CO_deh_flav_C. 1 hit. [Graphical view]
SUPFAM	SSF47741. 2Fe-2S_bind. 1 hit. SSF56003. Ald_xan_DH_mo_bd. 1 hit. SSF54665. Aldxan_dh_hamm. 1 hit. SSF55447. CO_deh_flav_C. 1 hit. SSF56176. FAD-binding_2. 1 hit. SSF54292. Ferredoxin. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. False negative. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ALDO3_ARATH

Accession

Primary (citable) accession number: Q7G9P4
Secondary accession number(s): O64429 , Q7GD73, Q9SIG7, Q9SLZ2

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	July 5, 2004
Last modified:	January 25, 2012
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Plant Protein Annotation Program