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Abscisic-aldehyde oxidase (EC 1.2.3.14) (Aldehyde oxidase 3) (AO-3) (AtAO-3) (AtAO4) (Indole-3-acetaldehyde oxidase) (IAA oxidase) (EC 1.2.3.7)

 ALDO3_ARATH             Reviewed;        1332 AA.
Q7G9P4; O64429; Q7GD73; Q9SIG7; Q9SLZ2;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 122.
RecName: Full=Abscisic-aldehyde oxidase;
EC=1.2.3.14;
AltName: Full=Aldehyde oxidase 3;
Short=AO-3;
Short=AtAO-3;
Short=AtAO4;
AltName: Full=Indole-3-acetaldehyde oxidase;
Short=IAA oxidase;
EC=1.2.3.7;
Name=AAO3; Synonyms=AO4; OrderedLocusNames=At2g27150;
ORFNames=F20F1.2;
Arabidopsis thaliana (Mouse-ear cress).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
Arabidopsis.
NCBI_TaxID=3702;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY, AND
INDUCTION.
STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
PubMed=15064376; DOI=10.1104/pp.103.036970;
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;
PubMed=10617197; DOI=10.1038/45471;
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]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
The Arabidopsis Information Portal (Araport);
Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 347-1332, AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
PubMed=9615466; DOI=10.1093/oxfordjournals.pcp.a029387;
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).
[5]
TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
PubMed=9489015; DOI=10.1104/pp.116.2.687;
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).
[6]
FUNCTION, INDUCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND SUBUNIT.
PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
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).
[7]
FUNCTION, TISSUE SPECIFICITY, AND MUTANT AAO3.
PubMed=11050171; DOI=10.1073/pnas.220426197;
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).
[8]
INDUCTION.
PubMed=11779861; DOI=10.1074/jbc.M109275200;
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).
[9]
INDUCTION.
PubMed=12417697; DOI=10.1105/tpc.006494;
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).
[10]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=15574845; DOI=10.1093/pcp/pch198;
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).
[11]
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 821-LEU--LYS-826.
PubMed=15122034; DOI=10.1104/pp.103.036590;
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).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY SALT STRESS AND ABA.
STRAIN=cv. Columbia;
PubMed=16930325; DOI=10.1111/j.1365-3040.2006.01576.x;
Barrero J.M., Rodriguez P.L., Quesada V., Piqueras P., Ponce M.R.,
Micol J.L.;
"Both abscisic acid (ABA)-dependent and ABA-independent pathways
govern the induction of NCED3, AAO3 and ABA1 in response to salt
stress.";
Plant Cell Environ. 29:2000-2008(2006).
[13]
INTERACTION WITH PUB44.
PubMed=19309463; DOI=10.1111/j.1365-313X.2009.03846.x;
Raab S., Drechsel G., Zarepour M., Hartung W., Koshiba T., Bittner F.,
Hoth S.;
"Identification of a novel E3 ubiquitin ligase that is required for
suppression of premature senescence in Arabidopsis.";
Plant J. 59:39-51(2009).
-!- 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. {ECO:0000269|PubMed:10972874,
ECO:0000269|PubMed:11050171, ECO:0000269|PubMed:15122034,
ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:16930325}.
-!- CATALYTIC ACTIVITY: Abscisic aldehyde + H(2)O + O(2) = abscisate +
H(2)O(2).
-!- CATALYTIC ACTIVITY: (Indol-3-yl)acetaldehyde + H(2)O + O(2) =
(indol-3-yl)acetate + H(2)O(2).
-!- COFACTOR:
Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601;
Evidence={ECO:0000250};
Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
-!- COFACTOR:
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
-!- COFACTOR:
Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
Evidence={ECO:0000250};
Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
{ECO:0000250};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.51 uM for abscisic aldehyde {ECO:0000269|PubMed:10972874};
KM=34 uM for indole-3-aldehyde {ECO:0000269|PubMed:10972874};
KM=44 uM for benzaldehyde {ECO:0000269|PubMed:10972874};
KM=1.8 uM for 1-naphthaldehyde {ECO:0000269|PubMed:10972874};
KM=700 uM for cinnamaldehyde {ECO:0000269|PubMed:10972874};
Note=All these kinetic values were obtained with AO-delta
dimer.;
-!- SUBUNIT: Aldehyde oxidases (AO) are homodimers 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.
{ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15064376,
ECO:0000269|PubMed:19309463}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- 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.
{ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:11050171,
ECO:0000269|PubMed:15064376, ECO:0000269|PubMed:15122034,
ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:9489015,
ECO:0000269|PubMed:9615466}.
-!- 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.
{ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:11779861,
ECO:0000269|PubMed:12417697, ECO:0000269|PubMed:15064376,
ECO:0000269|PubMed:16930325}.
-!- DISRUPTION PHENOTYPE: Impaired abscisic acid (ABA) biosynthesis.
{ECO:0000269|PubMed:16930325}.
-!- MISCELLANEOUS: In vitro, cannot discriminate between (+) and (-)
enantiomers of abscisic acid and leads respectively to (+) and (-)
cis-ABA.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
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EMBL; AB016622; BAA82672.1; -; mRNA.
EMBL; AC007154; AAD22498.1; -; Genomic_DNA.
EMBL; CP002685; AEC07944.1; -; Genomic_DNA.
EMBL; CP002685; AEC07945.1; -; Genomic_DNA.
EMBL; AB010080; BAA28630.1; -; mRNA.
PIR; D84669; D84669.
PIR; T52176; T52176.
RefSeq; NP_001077966.1; NM_001084497.1.
RefSeq; NP_180283.1; NM_128273.3.
UniGene; At.20239; -.
ProteinModelPortal; Q7G9P4; -.
SMR; Q7G9P4; -.
STRING; 3702.AT2G27150.1; -.
iPTMnet; Q7G9P4; -.
PaxDb; Q7G9P4; -.
PRIDE; Q7G9P4; -.
EnsemblPlants; AT2G27150.1; AT2G27150.1; AT2G27150.
EnsemblPlants; AT2G27150.2; AT2G27150.2; AT2G27150.
GeneID; 817257; -.
Gramene; AT2G27150.1; AT2G27150.1; AT2G27150.
Gramene; AT2G27150.2; AT2G27150.2; AT2G27150.
KEGG; ath:AT2G27150; -.
Araport; AT2G27150; -.
TAIR; locus:2045149; AT2G27150.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
InParanoid; Q7G9P4; -.
KO; K09842; -.
OMA; AKATWVE; -.
OrthoDB; EOG093600DW; -.
PhylomeDB; Q7G9P4; -.
BioCyc; ARA:AT2G27150-MONOMER; -.
BioCyc; MetaCyc:AT2G27150-MONOMER; -.
BRENDA; 1.2.3.14; 399.
Reactome; R-ATH-964975; Vitamins B6 activation to pyridoxal phosphate.
SABIO-RK; Q7G9P4; -.
PRO; PR:Q7G9P4; -.
Proteomes; UP000006548; Chromosome 2.
ExpressionAtlas; Q7G9P4; baseline and differential.
Genevisible; Q7G9P4; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0010293; F:abscisic aldehyde oxidase activity; IDA:TAIR.
GO; GO:0004031; F:aldehyde oxidase activity; IDA:TAIR.
GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IDA:TAIR.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0009688; P:abscisic acid biosynthetic process; IMP:TAIR.
GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
Gene3D; 1.10.150.120; -; 1.
Gene3D; 3.10.20.30; -; 1.
Gene3D; 3.30.365.10; -; 4.
Gene3D; 3.30.43.10; -; 1.
Gene3D; 3.30.465.10; -; 1.
Gene3D; 3.90.1170.50; -; 1.
InterPro; IPR002888; 2Fe-2S-bd.
InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
InterPro; IPR006058; 2Fe2S_fd_BS.
InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
InterPro; IPR016208; Ald_Oxase/xanthine_DH.
InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016169; CO_DH_flavot_FAD-bd_sub2.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
InterPro; IPR016167; FAD-bd_2_sub1.
InterPro; IPR002346; Mopterin_DH_FAD-bd.
Pfam; PF01315; Ald_Xan_dh_C; 1.
Pfam; PF02738; Ald_Xan_dh_C2; 1.
Pfam; PF03450; CO_deh_flav_C; 1.
Pfam; PF00941; FAD_binding_5; 1.
Pfam; PF00111; Fer2; 1.
Pfam; PF01799; Fer2_2; 1.
PIRSF; PIRSF000127; Xanthine_DH; 1.
SMART; SM01008; Ald_Xan_dh_C; 1.
SMART; SM01092; CO_deh_flav_C; 1.
SUPFAM; SSF47741; SSF47741; 1.
SUPFAM; SSF54292; SSF54292; 1.
SUPFAM; SSF54665; SSF54665; 1.
SUPFAM; SSF55447; SSF55447; 1.
SUPFAM; SSF56003; SSF56003; 1.
SUPFAM; SSF56176; SSF56176; 1.
PROSITE; PS00197; 2FE2S_FER_1; 1.
PROSITE; PS51085; 2FE2S_FER_2; 1.
PROSITE; PS51387; FAD_PCMH; 1.
1: Evidence at protein level;
2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis;
Complete proteome; Cytoplasm; FAD; Flavoprotein; Iron; Iron-sulfur;
Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome.
CHAIN 1 1332 Abscisic-aldehyde oxidase.
/FTId=PRO_0000166111.
DOMAIN 1 88 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 219 400 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
METAL 40 40 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 45 45 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 48 48 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
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.
{ECO:0000269|PubMed:15122034}.
SEQUENCE 1332 AA; 146701 MW; 084ED4BEE64B121B CRC64;
MDLEFAVNGE RFKIDSVDPS TTLLEFLRLN TPFKSVKLGC GEGGCGACLV VLSKYDPELD
QVKECCINSC LTLLCSVNGC SITTSEGLGN TKKGFHPIHK RFAGFHASQC GFCTPGMCIS
LYSSLANAEN NSSKDFTVSE AEKSVSGNLC RCTGYRPIVD ACKSFASDVD IEDLGLNSFW
KKGESKEVMF KNLPPYNPKD HLVTFPEFLK KKEKVDNGSD HLKYRWTTPF SVAELHNIME
AANSGDSLKL VVGNTGTGYY KDEERFDRYI DISNIPEMSM IKKDEKGIEI GAAVTISNAI
DALEKESKSS YVFKKMATHM EKIGNRSIRN SGSIGGNLVM AQSRKFPSDV TTLLLAVDAS
VYMLNGRKTE KVTLQEFLEL SPVLDSKRVL LKVEIPSWTA PSGDDTEFLF ESYRAAPRSI
GNALPYLNAA FLALVSRQEA SRKGVTVEKC FLAFGSYGGD HSIRAIEVET FLTGKLLSYS
VLYEAVGLLK GIIVPGKDTL HSEYRKSLAV GYLFEFFYPL IESGHRICSL DSGNKHNNSH
VDTVKSLPFL SSSQQVLESN EFKPIGEAVI KVGAALQASG EAVFVDDIPT LPDCLHGAFI
YSTEPLAKIK SLSFRENVTP TGVFAVLTFK DIPQQGQNIG SKTLFGPGPL FADELTRCAG
QRIALVVADT QKHADMAAKL AVVEYDTKNL EQPILTVEDA VKRSSFFEVH PMFYPEPVGD
VIKGMEEAER KIISSELRLG SQYFFYMEPQ TALALPDEDN CVKVFSSSQA PEYVHSVIAT
CLGIQEHNVR VITRRVGGGF GGKAVKSMPV ATACALGAYK LQRPVKMFLN RKTDMIMAGG
RHPMKINYNV GFRSDGKLTA LELTMLIDAG LEPDVSPIMP RNIMGPLRKY DWGALSFDVK
VCKTNCLSRT AMRAPGEVQG SYIAESIIEN VASSLQMDVD AVRKINLHTY DSLRKFYNHI
AGDPDEYTLP LLWEKLEISS KFKERSEMVK EFNLCNVWRK RGISRVPIVH QVMQRPTPGK
VSILSDGSVV VEVGGIEIGQ GLWTKVQQMV AYGLGMVKCE GNEKLLDRIR VVQSDTLGMI
QGGFTAGSTT SESSCEAVRL CCVILVERLK PIMDQMMMEK SGSVTWNILI QQAYGQYINL
SASTLYKPEY SSMEYLNYGV GVSEVEVDLV TGKTEILRSD IIYDCGKSLN PAVDLGQTEG
AFVQGIGFFM MEEYTTDEKG LVVQQGTWDY KIPTVDTIPK HFNVEIVNTG HHKNRVLSSK
ASGEPPLLLA ASVHCATRSA IREARKHSLS SNFIDGSDSE FELPVPATMP VVKSLCGLYS
VEKYLQGKIK GQ


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GENTAUR France SARL
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Tel 01 43 25 01 50

Fax 01 43 25 01 60
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BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

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GENTAUR GmbH
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Support Karolina Elandt
Tel: 0035929830070
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San Jose, CA 95123
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Tel (408) 780-0908,
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Genprice Inc, Invoices and accounting
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GENTAUR Poland Sp. z o.o.


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