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Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase 2) (AO-2) (AtAO-2) (AtAO3)

 ALDO2_ARATH             Reviewed;        1321 AA.
Q7G192; O49156; O64418;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
23-MAY-2018, entry version 121.
RecName: Full=Indole-3-acetaldehyde oxidase;
Short=IAA oxidase;
EC=1.2.3.7;
AltName: Full=Aldehyde oxidase 2;
Short=AO-2;
Short=AtAO-2;
Short=AtAO3;
Name=AAO2; Synonyms=AO3; OrderedLocusNames=At3g43600;
ORFNames=F22J12.40;
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], 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130713; DOI=10.1038/35048706;
Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M.,
Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B.,
Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P.,
De Simone V., Choisne N., Artiguenave F., Robert C., Brottier P.,
Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F.,
Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V.,
Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S.,
Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G.,
Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B.,
Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G.,
Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J.,
Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D.,
Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
Monfort A., Argiriou A., Flores M., Liguori R., Vitale D.,
Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W.,
Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J.,
Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P.,
Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S.,
Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V.,
Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C.,
Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E.,
Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y.,
Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A.,
Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Tabata S.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis
thaliana.";
Nature 408:820-822(2000).
[3]
GENOME REANNOTATION.
STRAIN=cv. Columbia;
PubMed=27862469; DOI=10.1111/tpj.13415;
Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
Town C.D.;
"Araport11: a complete reannotation of the Arabidopsis thaliana
reference genome.";
Plant J. 89:789-804(2017).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 758-1321, AND TISSUE SPECIFICITY.
STRAIN=cv. Wassilewskija; TISSUE=Root;
PubMed=9655945; DOI=10.1016/S0167-4781(98)00085-2;
Hoff T., Frandsen G.I., Rocher A., Mundy J.;
"Biochemical and genetic characterization of three molybdenum cofactor
hydroxylases in Arabidopsis thaliana.";
Biochim. Biophys. Acta 1398:397-402(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]
SUBUNIT, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10423535; DOI=10.1093/oxfordjournals.jbchem.a022463;
Akaba S., Seo M., Dohmae N., Takio K., Sekimoto H., Kamiya Y.,
Furuya N., Komano T., Koshiba T.;
"Production of homo- and hetero-dimeric isozymes from two aldehyde
oxidase genes of Arabidopsis thaliana.";
J. Biochem. 126:395-401(1999).
[7]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=10739959; DOI=10.1093/oxfordjournals.jbchem.a022654;
Koiwai H., Akaba S., Seo M., Komano T., Koshiba T.;
"Functional expression of two Arabidopsis aldehyde oxidases in the
yeast Pichia pastoris.";
J. Biochem. 127:659-664(2000).
[8]
TISSUE SPECIFICITY.
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).
[9]
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).
[10]
SUBUNIT, AND SUBSTRATE SPECIFICITY.
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).
-!- FUNCTION: In higher plant aldehyde oxidases (AO) appear to be
homo- and heterodimeric assemblies of AO subunits with probably
different physiological functions. In vitro, AO-gamma uses
heptaldehyde, benzaldehyde, naphthaldehyde and cinnamaldehyde as
substrates; AO-beta uses indole-3-acetaldehyde (IAAld), indole-3-
aldehyde (IAld) and naphtaldehyde; the AAO2-AAO3 dimer uses
abscisic aldehyde.
-!- CATALYTIC ACTIVITY: (Indol-3-yl)acetaldehyde + H(2)O + O(2) =
(indol-3-yl)acetate + H(2)O(2). {ECO:0000269|PubMed:10423535}.
-!- 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};
-!- ENZYME REGULATION: Strongly inhibited by iodoacetate, potassium
cyanide (KCN), 2-mercaptoethanol, dithiothreitol (DTT), p-
chloromercuribenzoate, menadione and estradiol. Weakly inhibited
by 4'-(9-acridinylamino)methanesulfon-m-anisidine (mAMSA) and
tritonX-100. Not affected by allopurinol.
{ECO:0000269|PubMed:10739959}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=57 uM for heptaldehyde {ECO:0000269|PubMed:10739959};
KM=7.7 uM for benzaldehyde {ECO:0000269|PubMed:10739959};
KM=0.33 uM for naphthaldehyde {ECO:0000269|PubMed:10739959};
KM=410 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959};
Vmax=24 nmol/min/mg enzyme with heptaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=8.7 nmol/min/mg enzyme with benzaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=65 nmol/min/mg enzyme with naphthaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=20 nmol/min/mg enzyme with cinnamaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Note=Kinetic values were obtained with the AO-gamma dimer.;
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:10739959};
Temperature dependence:
Optimum temperature is 50 degrees Celsius.
{ECO:0000269|PubMed:10739959};
-!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of
AO subunits. AO-beta is a AAO1-AAO2 heterodimer; AO-gamma is a
AAO2 homodimer. AAO2 also forms a dimer with AAO3.
{ECO:0000269|PubMed:10423535, ECO:0000269|PubMed:15064376}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- TISSUE SPECIFICITY: Weakly expressed in roots, leaves and
seedlings. In seedlings, mostly expressed in lower part of
hypocotyls. Detectable in seeds and mature siliques at low levels.
{ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15574845,
ECO:0000269|PubMed:9489015, ECO:0000269|PubMed:9615466,
ECO:0000269|PubMed:9655945}.
-!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
{ECO:0000305}.
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EMBL; AB005805; BAA28625.1; -; mRNA.
EMBL; AL391734; CAC05634.1; -; Genomic_DNA.
EMBL; CP002686; AEE77812.1; -; Genomic_DNA.
EMBL; AF039896; AAC39510.1; -; mRNA.
PIR; T51623; T51623.
PIR; T52050; T52050.
RefSeq; NP_189946.1; NM_114228.3.
UniGene; At.462; -.
ProteinModelPortal; Q7G192; -.
SMR; Q7G192; -.
STRING; 3702.AT3G43600.1; -.
PaxDb; Q7G192; -.
PRIDE; Q7G192; -.
EnsemblPlants; AT3G43600.1; AT3G43600.1; AT3G43600.
GeneID; 823457; -.
Gramene; AT3G43600.1; AT3G43600.1; AT3G43600.
KEGG; ath:AT3G43600; -.
Araport; AT3G43600; -.
TAIR; locus:2079834; AT3G43600.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
InParanoid; Q7G192; -.
KO; K11817; -.
OMA; VVFCKIA; -.
OrthoDB; EOG093600DW; -.
PhylomeDB; Q7G192; -.
BioCyc; ARA:AT3G43600-MONOMER; -.
BioCyc; MetaCyc:AT3G43600-MONOMER; -.
BRENDA; 1.2.3.1; 399.
Reactome; R-ATH-964975; Vitamins B6 activation to pyridoxal phosphate.
SABIO-RK; Q7G192; -.
PRO; PR:Q7G192; -.
Proteomes; UP000006548; Chromosome 3.
ExpressionAtlas; Q7G192; baseline and differential.
Genevisible; Q7G192; AT.
GO; GO:0005829; C:cytosol; IDA:TAIR.
GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0004031; F:aldehyde oxidase activity; IDA:TAIR.
GO; GO:0009055; F:electron transfer activity; IEA:InterPro.
GO; GO:0050660; F:flavin adenine dinucleotide binding; IBA:GO_Central.
GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IEA:UniProtKB-EC.
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:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
CDD; cd00207; fer2; 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; IPR005107; CO_DH_flav_C.
InterPro; IPR036683; CO_DH_flav_C_dom_sf.
InterPro; IPR016166; FAD-bd_2.
InterPro; IPR036318; FAD-bd_2-like_sf.
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 1321 Indole-3-acetaldehyde oxidase.
/FTId=PRO_0000166110.
DOMAIN 1 90 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 215 404 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
METAL 42 42 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 47 47 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 50 50 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
CONFLICT 808 808 K -> N (in Ref. 4; AAC39510).
{ECO:0000305}.
CONFLICT 1083 1083 S -> T (in Ref. 4; AAC39510).
{ECO:0000305}.
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


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