ID   ALDO2_ARATH             Reviewed;        1321 AA.
AC   Q7G192; O49156; O64418;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   25-NOV-2008, entry version 42.
DE   RecName: Full=Aldehyde oxidase 2;
DE            Short=AO-2;
DE            Short=AtAO-2;
DE            Short=AtAO3;
DE            EC=1.2.3.1;
GN   Name=AAO2; Synonyms=AO3; OrderedLocusNames=At3g43600;
GN   ORFNames=F22J12.40;
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], 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   MEDLINE=21016720; PubMed=11130713; DOI=10.1038/35048706;
RA   Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
RA   Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
RA   Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
RA   De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
RA   Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
RA   Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
RA   Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
RA   Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
RA   Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
RA   Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
RA   Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
RA   Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA   de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA   Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
RA   Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
RA   Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
RA   Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
RA   Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
RA   Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
RA   Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
RA   Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
RA   Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
RA   Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA   Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence and analysis of chromosome 3 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:820-822(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 758-1321, AND TISSUE SPECIFICITY.
RC   STRAIN=cv. Wassilewskija; TISSUE=Root;
RX   MEDLINE=98322131; PubMed=9655945; DOI=10.1016/S0167-4781(98)00085-2;
RA   Hoff T., Frandsen G.I., Rocher A., Mundy J.;
RT   "Biochemical and genetic characterization of three molybdenum cofactor
RT   hydroxylases in Arabidopsis thaliana.";
RL   Biochim. Biophys. Acta 1398:397-402(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   SUBUNIT, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   MEDLINE=99353970; PubMed=10423535;
RA   Akaba S., Seo M., Dohmae N., Takio K., Sekimoto H., Kamiya Y.,
RA   Furuya N., Komano T., Koshiba T.;
RT   "Production of homo- and hetero-dimeric isozymes from two aldehyde
RT   oxidase genes of Arabidopsis thaliana.";
RL   J. Biochem. 126:395-401(1999).
RN   [6]
RP   BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
RX   MEDLINE=20206746; PubMed=10739959;
RA   Koiwai H., Akaba S., Seo M., Komano T., Koshiba T.;
RT   "Functional expression of two Arabidopsis aldehyde oxidases in the
RT   yeast Pichia pastoris.";
RL   J. Biochem. 127:659-664(2000).
RN   [7]
RP   TISSUE SPECIFICITY.
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   [8]
RP   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   [9]
RP   SUBUNIT, AND SUBSTRATE SPECIFICITY.
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).
CC   -!- FUNCTION: In higher plant aldehyde oxidases (AO) appear to be
CC       homo- and heterodimeric assemblies of AO subunits with probably
CC       different physiological functions. In vitro, AO-gamma uses
CC       heptaldehyde, benzaldehyde, naphthaldehyde and cinnamaldehyde as
CC       substrates; AO-beta uses indole-3-acetaldehyde (IAAld), indole-3-
CC       aldehyde (IAld) and naphtaldehyde; the AAO2-AAO3 dimer uses
CC       abscisic aldehyde.
CC   -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylic acid
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   -!- ENZYME REGULATION: Strongly inhibited by iodoacetate, potassium
CC       cyanide (KCN), 2-mercaptoethanol, dithiothreitol (DTT), p-
CC       chloromercuribenzoate, menadione and estradiol. Weakly inhibited
CC       by 4'-(9-acridinylamino)methanesulfon-m-anisidine (mAMSA) and
CC       tritonX-100. Not affected by allopurinol.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=57 uM for heptaldehyde;
CC         KM=7.7 uM for benzaldehyde;
CC         KM=0.33 uM for naphthaldehyde;
CC         KM=410 uM for cinnamaldehyde;
CC         Vmax=24 nmol/min/mg enzyme with heptaldehyde as substrate;
CC         Vmax=8.7 nmol/min/mg enzyme with benzaldehyde as substrate;
CC         Vmax=65 nmol/min/mg enzyme with naphthaldehyde as substrate;
CC         Vmax=20 nmol/min/mg enzyme with cinnamaldehyde as substrate;
CC         Note=Kinetic values were obtained with the AO-gamma dimer;
CC       pH dependence:
CC         Optimum pH is 8;
CC       Temperature dependence:
CC         Optimum temperature is 50 degrees Celsius;
CC   -!- SUBUNIT: Aldehyde oxidases (AO) are homo- and heterodimers of AO
CC       subunits. AO-beta is a AAO1-AAO2 heterodimer; AO-gamma is a AAO2
CC       homodimer. AAO2 also forms a dimer with AAO3.
CC   -!- TISSUE SPECIFICITY: Weakly expressed in roots, leaves and
CC       seedlings. In seedlings, mostly expressed in lower part of
CC       hypocotyls. Detectable in seeds and mature siliques at low levels.
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; AB005805; BAA28625.1; -; mRNA.
DR   EMBL; AL391734; CAC05634.1; -; Genomic_DNA.
DR   EMBL; AF039896; AAC39510.1; -; mRNA.
DR   PIR; T51623; T51623.
DR   PIR; T52050; T52050.
DR   RefSeq; NP_189946.1; -.
DR   UniGene; At.462; -.
DR   HSSP; P80457; 1FO4.
DR   GeneID; 823457; -.
DR   GenomeReviews; BA000014_GR; AT3G43600.
DR   KEGG; ath:AT3G43600; -.
DR   NMPDR; fig|3702.1.peg.15566; -.
DR   GeneFarm; 4893; 470.
DR   TAIR; At3g43600; -.
DR   BioCyc; MetaCyc:AT3G43600-MON; -.
DR   GermOnline; AT3G43600; Arabidopsis thaliana.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004031; F: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: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; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur;
KW   Metal-binding; Molybdenum; NAD; Oxidoreductase.
FT   CHAIN         1   1321       Aldehyde oxidase 2.
FT                                /FTId=PRO_0000166110.
FT   DOMAIN        1     90       2Fe-2S ferredoxin-type.
FT   DOMAIN      215    404       FAD-binding PCMH-type.
FT   METAL        42     42       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        47     47       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        50     50       Iron-sulfur (2Fe-2S) (By similarity).
FT   CONFLICT    808    808       K -> N (in Ref. 3; AAC39510).
FT   CONFLICT   1083   1083       S -> T (in Ref. 3; AAC39510).
SQ   SEQUENCE   1321 AA;  144580 MW;  BFF5E02BF0406A4A CRC64;
     MSLVFAINGQ RFELELSSVD PSTTLLEFLR YQTSFKSVKL SCGEGGCGAC VVLLSKFDPV
     LQKVEDFTVS SCLTLLCSVN HCNITTSEGL GNSRDGFHPI HKRLSGFHAS QCGFCTPGMS
     VSLFSALLDA DKSQYSDLTV VEAEKAVSGN LCRCTGYRPI VDACKSFASD VDIEDLGLNS
     FCRKGDKDSS SLTRFDSEKR ICTFPEFLKD EIKSVDSGMY RWCSPASVEE LSSLLEACKA
     NSNTVSMKLV AGNTSMGYYK DEREQNYDKY IDITRIPHLK EIRENQNGVE IGSVVTISKV
     IAALKEIRVS PGVEKIFGKL ATHMEMIAAR FIRNFGSIGG NLVMAQRKQF PSDMATILLA
     AGAFVNIMSS SRGLEKLTLE EFLERSPLEA HDLVLSIEIP FWHSETNSEL FFETYRAAPR
     PHGSALAYLN AAFLAEVKDT MVVNCRLAFG AYGTKHAIRC KEIEEFLSGK VITDKVLYEA
     ITLLGNVVVP EDGTSNPAYR SSLAPGFLFK FLHTLMTHPT TDKPSNGYHL DPPKPLPMLS
     SSQNVPINNE YNPVGQPVTK VGASLQASGE AVYVDDIPSP TNCLYGAFIY SKKPFARIKG
     IHFKDDLVPT GVVAVISRKD VPKGGKNIGM KIGLGSDQLF AEDFTTSVGE CIAFVVADTQ
     RHADAAVNLA VVEYETEDLE PPILSVEDAV KKSSLFDIIP FLYPQQVGDT SKGMAEADHQ
     ILSSEIRLGS QYVFYMETQT ALAVGDEDNC IVVYSSTQTP QYVQSSVAAC LGIPENNIRV
     ITRRVGGGFG GKSVKSMPVA TACALAAKKL QRPVRTYVNR KTDMIMTGGR HPMKITYSVG
     FKSTGKITAL ELEILIDAGA SYGFSMFIPS NLIGSLKKYN WGALSFDIKL CKTNLLSRAI
     MRSPGDVQGT YIAEAIIENI ASSLSLEVDT IRKINLHTHE SLALFYKDGA GEPHEYTLSS
     MWDKVGVSSK FEERVSVVRE FNESNMWRKR GISRVPIIYE VLLFATPGRV SVLSDGTIVV
     EIGGIELGQG LWTKVKQMTS YALGMLQCDG TEELLEKIRV IQSDSLSMVQ GNFTGGSTTS
     EGSCAAVRLC CETLVERLKP LMERSDGPIT WNELISQAYA QSVNLSASDL YTPKDTPMQY
     LNYGTAVSEV EVDLVTGQTT VLQTDILYDC GKSLNPAVDL GQIEGSFVQG LGFFMLEEYI
     EDPEGLLLTD STWTYKIPTV DTIPKQFNVE ILNGGCHEKR VLSSKASGEP PLLLAASVHC
     ATRQAVKEAR KQLCMWKGEN GSSGSAFQLP VPATMPVVKE LCGLDIIESY LEWKLHDNSN
     L
//