ID   ALDO3_ARATH             Reviewed;        1332 AA.
AC   Q7G9P4; O64429; Q7GD73; Q9SIG7; Q9SLZ2;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-NOV-2008, entry version 47.
DE   RecName: Full=Abscisic-aldehyde oxidase;
DE            EC=1.2.3.14;
DE   AltName: Full=Aldehyde oxidase 3;
DE            Short=AO-3;
DE            Short=AtAO-3;
DE            Short=AtAO4;
GN   Name=AAO3; Synonyms=AO4; OrderedLocusNames=At2g27150;
GN   ORFNames=F20F1.2;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons;
OC   rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, TISSUE SPECIFICITY, AND
RP   INDUCTION.
RC   STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX   PubMed=15064376; DOI=10.1104/pp.103.036970;
RA   Koiwai H., Nakaminami K., Seo M., Mitsuhashi W., Toyomasu T.,
RA   Koshiba T.;
RT   "Tissue-specific localization of an abscisic acid biosynthetic enzyme,
RT   AAO3, in Arabidopsis.";
RL   Plant Physiol. 134:1697-1707(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=20083487; PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L.,
RA   Moffat K.S., Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L.,
RA   Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H.,
RA   Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D.,
RA   Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M.,
RA   Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 347-1332, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX   MEDLINE=98277700; PubMed=9615466;
RA   Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S.,
RA   Liotenberg S., Marion-Poll A., Caboche M., Kamiya Y., Koshiba T.;
RT   "Molecular cloning and characterization of aldehyde oxidases in
RT   Arabidopsis thaliana.";
RL   Plant Cell Physiol. 39:433-442(1998).
RN   [4]
RP   TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX   MEDLINE=98150273; PubMed=9489015; DOI=10.1104/pp.116.2.687;
RA   Seo M., Akaba S., Oritani T., Delarue M., Bellini C., Caboche M.,
RA   Koshiba T.;
RT   "Higher activity of an aldehyde oxidase in the auxin-overproducing
RT   superroot1 mutant of Arabidopsis thaliana.";
RL   Plant Physiol. 116:687-693(1998).
RN   [5]
RP   FUNCTION, INDUCTION, TISSUE SPECIFICITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
RX   MEDLINE=20428204; PubMed=10972874;
RX   DOI=10.1046/j.1365-313x.2000.00812.x;
RA   Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y.,
RA   Koshiba T.;
RT   "Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
RL   Plant J. 23:481-488(2000).
RN   [6]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTANT AAO3.
RX   MEDLINE=20524100; PubMed=11050171; DOI=10.1073/pnas.220426197;
RA   Seo M., Peeters A.J.M., Koiwai H., Oritani T., Marion-Poll A.,
RA   Zeevaart J.A.D., Koornneef M., Kamiya Y., Koshiba T.;
RT   "The Arabidopsis aldehyde oxidase 3 (AAO3) gene product catalyzes the
RT   final step in abscisic acid biosynthesis in leaves.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:12908-12913(2000).
RN   [7]
RP   INDUCTION.
RX   MEDLINE=21864266; PubMed=11779861; DOI=10.1074/jbc.M109275200;
RA   Xiong L., Lee H., Ishitani M., Zhu J.-K.;
RT   "Regulation of osmotic stress-responsive gene expression by the
RT   LOS6/ABA1 locus in Arabidopsis.";
RL   J. Biol. Chem. 277:8588-8596(2002).
RN   [8]
RP   INDUCTION.
RX   MEDLINE=22305397; PubMed=12417697; DOI=10.1105/tpc.006494;
RA   Cheng W.-H., Endo A., Zhou L., Penney J., Chen H.-C., Arroyo A.,
RA   Leon P., Nambara E., Asami T., Seo M., Koshiba T., Sheen J.;
RT   "A unique short-chain dehydrogenase/reductase in Arabidopsis glucose
RT   signaling and abscisic acid biosynthesis and functions.";
RL   Plant Cell 14:2723-2743(2002).
RN   [9]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=15574845; DOI=10.1093/pcp/pch198;
RA   Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T.;
RT   "Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene
RT   family revealed a major role of AAO3 in ABA biosynthesis in seeds.";
RL   Plant Cell Physiol. 45:1694-1703(2004).
RN   [10]
RP   FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF 821-LEU--LYS-826.
RX   PubMed=15122034; DOI=10.1104/pp.103.036590;
RA   Gonzalez-Guzman M., Abia D., Salinas J., Serrano R., Rodriguez P.L.;
RT   "Two new alleles of the abscisic aldehyde oxidase 3 gene reveal its
RT   role in abscisic acid biosynthesis in seeds.";
RL   Plant Physiol. 135:325-333(2004).
CC   -!- FUNCTION: In higher plants aldehyde oxidases (AO) appear to be
CC       homo- and heterodimeric assemblies of AO subunits with probably
CC       different physiological functions. AO-delta seems to be involved
CC       in the last step of abscisic acid biosynthesis, at least in leaves
CC       and seeds. In vitro, AO-delta oxidizes abscisic aldehyde to
CC       abscisic acid (ABA). In vitro, AO-delta also uses indole-3-
CC       aldehyde (IAld), benzaldehyde, 1-naphthaldehyde and cinnamaldehyde
CC       as substrate; the AAO2-AAO3 dimer also uses abscisic aldehyde as
CC       substrate.
CC   -!- CATALYTIC ACTIVITY: Abscisic aldehyde + H(2)O + O(2) = abscisate +
CC       H(2)O(2).
CC   -!- COFACTOR: Binds 2 2Fe-2S clusters (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- COFACTOR: Molybdopterin (By similarity).
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.51 uM for abscisic aldehyde;
CC         KM=34 uM for indole-3-aldehyde;
CC         KM=44 uM for benzaldehyde;
CC         KM=1.8 uM for 1-naphthaldehyde;
CC         KM=700 uM for cinnamaldehyde;
CC         Note=All these kinetic values were obtained with AO-delta dimer;
CC   -!- SUBUNIT: Aldehyde oxidases (AO) are homo- and heterodimers of AO
CC       subunits. AO-delta is a AAO3 homodimer. AAO3 also forms a dimer
CC       with AAO2.
CC   -!- TISSUE SPECIFICITY: Expressed in vascular tissues of all organs,
CC       particularly in phloem companion cells and xylem parenchymatic
CC       cells. Highly expressed in roots and rosettes, and to lower extent
CC       in seedlings, stems and flowers. Expressed at very low levels in
CC       siliques and dry seeds. Also detected in root dividing cells (tips
CC       and primordia), in mesophyll cells and inside the guard cells.
CC   -!- INDUCTION: Transcripts are induced by dehydration, in rosettes but
CC       not in roots. Induction by cold, ABA, sodium chloride (NaCl) and
CC       polyethylene glycol (PEG) is dependent of the zeaxanthin epoxidase
CC       ABA1 protein (ZEP). Induction by glucose requires the short chain
CC       alcohol dehydrogenase ABA2 protein. Repressed by mannitol.
CC   -!- MISCELLANEOUS: In vitro, can not discriminate between (+) and (-)
CC       enantiomers of abscisic acid and leads respectively to (+) and (-)
CC       cis-ABA.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; AB016622; BAA82672.1; -; mRNA.
DR   EMBL; AC007154; AAD22498.1; -; Genomic_DNA.
DR   EMBL; AB010080; BAA28630.1; -; mRNA.
DR   PIR; D84669; D84669.
DR   PIR; T52176; T52176.
DR   RefSeq; NP_001077966.1; -.
DR   RefSeq; NP_180283.1; -.
DR   UniGene; At.20239; -.
DR   HSSP; P80457; 1FO4.
DR   GeneID; 817257; -.
DR   GenomeReviews; CT485783_GR; AT2G27150.
DR   KEGG; ath:AT2G27150; -.
DR   NMPDR; fig|3702.1.peg.9746; -.
DR   GeneFarm; 4894; 470.
DR   TAIR; At2g27150; -.
DR   BioCyc; MetaCyc:AT2G27150-MON; -.
DR   ArrayExpress; Q7G9P4; -.
DR   GermOnline; AT2G27150; Arabidopsis thaliana.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0010293; F:abscisic aldehyde oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002888; 2Fe-2S_bd.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DHase_a/b.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DHase.
DR   InterPro; IPR008274; AldOxase/xan_DHase_Mopterin-bd.
DR   InterPro; IPR005107; CO_DHase_flav_C.
DR   InterPro; IPR016169; CO_DHase_flavot_FAD-bd_sub2.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR002346; Mopterin_DHase_FAD-bd.
DR   InterPro; IPR000572; OxRdtase_Mopterin-bd.
DR   Gene3D; G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
DR   Gene3D; G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
DR   Gene3D; G3DSA:3.30.390.50; CO_DH_flav_C; 1.
DR   Gene3D; G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   ProDom; PD186071; 2Fe-2S_bind; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
DR   PROSITE; PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PE   1: Evidence at protein level;
KW   2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis;
KW   Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase.
FT   CHAIN         1   1332       Abscisic-aldehyde oxidase.
FT                                /FTId=PRO_0000166111.
FT   DOMAIN        1     88       2Fe-2S ferredoxin-type.
FT   DOMAIN      219    400       FAD-binding PCMH-type.
FT   METAL        40     40       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        45     45       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        48     48       Iron-sulfur (2Fe-2S) (By similarity).
FT   MUTAGEN     821    826       LQRPVK->WDLDQ: In aao3-3; wilty phenotype
FT                                in rosette leaves, reduced ABA levels,
FT                                reduced dormancy, abnormal water loss and
FT                                abnormal response to water deficit.
SQ   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
//