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UniProtKB/Swiss-Prot entry Q7G9P4


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

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Entry information
Entry name ALDO3_ARATH
Primary accession number Q7G9P4
Secondary accession numbers O64429 Q7GD73 Q9SIG7 Q9SLZ2
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on July 5, 2004 (Sequence version 1)
Annotations were last modified on    September 2, 2008 (Entry version 45)
Name and origin of the protein
Protein name Abscisic-aldehyde oxidase
Synonyms EC 1.2.3.14
Aldehyde oxidase 3
AO-3
AtAO-3
AtAO4
Gene name
Name: AAO3
Synonyms: AO4
OrderedLocusNames: At2g27150
ORFNames: F20F1.2
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], SUBUNIT, TISSUE SPECIFICITY, AND INDUCTION.
STRAIN=cv. Columbia;
TISSUE=Seedling hypocotyl;
DOI=10.1104/pp.103.036970; PubMed=15064376 [NCBI, ExPASy, EBI, Israel, Japan]
Koiwai H., Nakaminami K., Seo M., Mitsuhashi W., Toyomasu T., Koshiba T.;
"Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis.";
Plant Physiol. 134:1697-1707(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/45471; PubMed=10617197 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
Nature 402:761-768(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 347-1332, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
TISSUE=Seedling hypocotyl;
PubMed=9615466 [NCBI, ExPASy, EBI, Israel, Japan]
Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S., Liotenberg S., Marion-Poll A., Caboche M., Kamiya Y., Koshiba T.;
"Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana.";
Plant Cell Physiol. 39:433-442(1998).
[4]
TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
DOI=10.1104/pp.116.2.687; PubMed=9489015 [NCBI, ExPASy, EBI, Israel, Japan]
Seo M., Akaba S., Oritani T., Delarue M., Bellini C., Caboche M., Koshiba T.;
"Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana.";
Plant Physiol. 116:687-693(1998).
[5]
FUNCTION, INDUCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
DOI=10.1046/j.1365-313x.2000.00812.x; PubMed=10972874 [NCBI, ExPASy, EBI, Israel, Japan]
Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T.;
"Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
Plant J. 23:481-488(2000).
[6]
FUNCTION, TISSUE SPECIFICITY, AND MUTANT AAO3.
DOI=10.1073/pnas.220426197; PubMed=11050171 [NCBI, ExPASy, EBI, Israel, Japan]
Seo M., Peeters A.J.M., Koiwai H., Oritani T., Marion-Poll A., Zeevaart J.A.D., Koornneef M., Kamiya Y., Koshiba T.;
"The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the final step in abscisic acid biosynthesis in leaves.";
Proc. Natl. Acad. Sci. U.S.A. 97:12908-12913(2000).
[7]
INDUCTION.
DOI=10.1074/jbc.M109275200; PubMed=11779861 [NCBI, ExPASy, EBI, Israel, Japan]
Xiong L., Lee H., Ishitani M., Zhu J.-K.;
"Regulation of osmotic stress-responsive gene expression by the LOS6/ABA1 locus in Arabidopsis.";
J. Biol. Chem. 277:8588-8596(2002).
[8]
INDUCTION.
DOI=10.1105/tpc.006494; PubMed=12417697 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A unique short-chain dehydrogenase/reductase in Arabidopsis glucose signaling and abscisic acid biosynthesis and functions.";
Plant Cell 14:2723-2743(2002).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
DOI=10.1093/pcp/pch198; PubMed=15574845 [NCBI, ExPASy, EBI, Israel, Japan]
Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
"Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds.";
Plant Cell Physiol. 45:1694-1703(2004).
[10]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 821-LEU--LYS-826.
DOI=10.1104/pp.103.036590; PubMed=15122034 [NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez-Guzman M., Abia D., Salinas J., Serrano R., Rodriguez P.L.;
"Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its role in abscisic acid biosynthesis in seeds.";
Plant Physiol. 135:325-333(2004).
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.
  • CATALYTIC ACTIVITY: Abscisic aldehyde + H2O + O2 = abscisate + H2O2.
  • COFACTOR: Binds 2 2Fe-2S clusters (By similarity).
  • COFACTOR: FAD (By similarity).
  • COFACTOR: Molybdopterin (By similarity).
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   KM=0.51 µM for abscisic aldehyde;
    KM=34 µM for indole-3-aldehyde;
    KM=44 µM for benzaldehyde;
    KM=1.8 µM for 1-naphthaldehyde;
    KM=700 µM for cinnamaldehyde;
    Note=All these kinetic values were obtained with AO-delta dimer;
  • SUBUNIT: Aldehyde oxidases (AO) are homo- and heterodimers of AO subunits. AO-delta is a AAO3 homodimer. AAO3 also forms a dimer with AAO2.
  • 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.
  • 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.
  • MISCELLANEOUS: In vitro, can not discriminate between (+) and (-) enantiomers of abscisic acid and leads respectively to (+) and (-) cis-ABA.
  • SIMILARITY: Belongs to the xanthine dehydrogenase family.
  • SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
  • SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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
AB016622; BAA82672.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC007154; AAD22498.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB010080; BAA28630.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D84669; D84669.
T52176; T52176.
RefSeq NP_001077966.1; -.
NP_180283.1; -.
UniGene At.20239
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase Q7G9P4.
Enzyme and pathway databases
BioCyc MetaCyc:AT2G27150-MON; -.
Organism-specific databases
GeneFarm 4894; 470.
TAIR At2g27150; -.
Gene expression databases
ArrayExpress Q7G9P4; -.
GermOnline AT2G27150; Arabidopsis thaliana.
Family and domain databases
InterPro IPR002888; 2Fe-2S_bd.
IPR006058; 2Fe2S_fd_BS.
IPR000674; Ald_Oxase/Xan_DHase_a/b.
IPR016208; Ald_Oxase/xanthine_DHase.
IPR008274; AldOxase/xan_DHase_Mopterin-bd.
IPR005107; CO_DHase_flav_C.
IPR016169; CO_DHase_flavot_FAD-bd_sub2.
IPR001041; Ferredoxin.
IPR002346; Mopterin_DHase_FAD-bd.
IPR000572; OxRdtase_Mopterin-bd.
Graphical view of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000127; Xanthine_DH; 1.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q7G9P4.
Genome annotation databases
GeneID 817257; -.
GenomeReviews CT485783_GR; AT2G27150.
KEGG ath:AT2G27150; -.
NMPDR fig|3702.1.peg.9746; -.
Other
ProtoNet Q7G9P4.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   1332  1332     Abscisic-aldehyde oxidase. PRO_0000166111
DOMAIN   1     88  88     2Fe-2S ferredoxin-type. 
DOMAIN   219    400  182     FAD-binding PCMH-type. 
METAL   40     40        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   45     45        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   48     48        Iron-sulfur (2Fe-2S) (By similarity). 
MUTAGEN   821    826        LQRPVK->WDLDQ: In aao3-3; wilty phenotype in rosette leaves, reduced ABA levels, reduced dormancy, abnormal water loss and abnormal response to water deficit. 
Sequence information
Length: 1332 AA [This is the length of the unprocessed precursor] Molecular weight: 146701 Da [This is the MW of the unprocessed precursor] CRC64: 084ED4BEE64B121B [This is a checksum on the sequence]
        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 

Q7G9P4 in FASTA format

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