ALDO2_ARATH
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 03-AUG-2022, entry version 141.
DE RecName: Full=Indole-3-acetaldehyde oxidase;
DE Short=IAA oxidase;
DE EC=1.2.3.7;
DE AltName: Full=Aldehyde oxidase 2;
DE Short=AO-2;
DE Short=AtAO-2;
DE Short=AtAO3;
GN Name=AAO2; Synonyms=AO3; OrderedLocusNames=At3g43600; ORFNames=F22J12.40;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Columbia; TISSUE=Seedling hypocotyl;
RX PubMed=9615466; DOI=10.1093/oxfordjournals.pcp.a029387;
RA Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S., Liotenberg S.,
RA Marion-Poll A., Caboche M., Kamiya Y., Koshiba T.;
RT "Molecular cloning and characterization of aldehyde oxidases in Arabidopsis
RT thaliana.";
RL Plant Cell Physiol. 39:433-442(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., 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., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., 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 thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 758-1321, AND TISSUE SPECIFICITY.
RC STRAIN=cv. Wassilewskija; TISSUE=Root;
RX 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 [5]
RP TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
RX 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 [6]
RP SUBUNIT, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10423535; DOI=10.1093/oxfordjournals.jbchem.a022463;
RA Akaba S., Seo M., Dohmae N., Takio K., Sekimoto H., Kamiya Y., Furuya N.,
RA Komano T., Koshiba T.;
RT "Production of homo- and hetero-dimeric isozymes from two aldehyde oxidase
RT genes of Arabidopsis thaliana.";
RL J. Biochem. 126:395-401(1999).
RN [7]
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=10739959; DOI=10.1093/oxfordjournals.jbchem.a022654;
RA Koiwai H., Akaba S., Seo M., Komano T., Koshiba T.;
RT "Functional expression of two Arabidopsis aldehyde oxidases in the yeast
RT Pichia pastoris.";
RL J. Biochem. 127:659-664(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=10972874; DOI=10.1046/j.1365-313x.2000.00812.x;
RA Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T.;
RT "Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana.";
RL Plant J. 23:481-488(2000).
RN [9]
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 family
RT revealed a major role of AAO3 in ABA biosynthesis in seeds.";
RL Plant Cell Physiol. 45:1694-1703(2004).
RN [10]
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., 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 homo- and
CC heterodimeric assemblies of AO subunits with probably different
CC physiological functions. In vitro, AO-gamma uses heptaldehyde,
CC benzaldehyde, naphthaldehyde and cinnamaldehyde as substrates; AO-beta
CC uses indole-3-acetaldehyde (IAAld), indole-3-aldehyde (IAld) and
CC naphtaldehyde; the AAO2-AAO3 dimer uses abscisic aldehyde.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate + H(+)
CC + H2O2; Xref=Rhea:RHEA:16277, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18086,
CC ChEBI:CHEBI:30854; EC=1.2.3.7;
CC Evidence={ECO:0000269|PubMed:10423535};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- ACTIVITY REGULATION: Strongly inhibited by iodoacetate, potassium
CC cyanide (KCN), 2-mercaptoethanol, dithiothreitol (DTT), p-
CC chloromercuribenzoate, menadione and estradiol. Weakly inhibited by 4'-
CC (9-acridinylamino)methanesulfon-m-anisidine (mAMSA) and tritonX-100.
CC Not affected by allopurinol. {ECO:0000269|PubMed:10739959}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=57 uM for heptaldehyde {ECO:0000269|PubMed:10739959};
CC KM=7.7 uM for benzaldehyde {ECO:0000269|PubMed:10739959};
CC KM=0.33 uM for naphthaldehyde {ECO:0000269|PubMed:10739959};
CC KM=410 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959};
CC Vmax=24 nmol/min/mg enzyme with heptaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=8.7 nmol/min/mg enzyme with benzaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=65 nmol/min/mg enzyme with naphthaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=20 nmol/min/mg enzyme with cinnamaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Note=Kinetic values were obtained with the AO-gamma dimer.;
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:10739959};
CC Temperature dependence:
CC Optimum temperature is 50 degrees Celsius.
CC {ECO:0000269|PubMed:10739959};
CC -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers 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 {ECO:0000269|PubMed:10423535, ECO:0000269|PubMed:15064376}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Weakly expressed in roots, leaves and seedlings. In
CC seedlings, mostly expressed in lower part of hypocotyls. Detectable in
CC seeds and mature siliques at low levels. {ECO:0000269|PubMed:10972874,
CC ECO:0000269|PubMed:15574845, ECO:0000269|PubMed:9489015,
CC ECO:0000269|PubMed:9615466, ECO:0000269|PubMed:9655945}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AB005805; BAA28625.1; -; mRNA.
DR EMBL; AL391734; CAC05634.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE77812.1; -; Genomic_DNA.
DR EMBL; AF039896; AAC39510.1; -; mRNA.
DR PIR; T51623; T51623.
DR PIR; T52050; T52050.
DR RefSeq; NP_189946.1; NM_114228.3.
DR AlphaFoldDB; Q7G192; -.
DR SMR; Q7G192; -.
DR STRING; 3702.AT3G43600.1; -.
DR PaxDb; Q7G192; -.
DR PRIDE; Q7G192; -.
DR ProteomicsDB; 244827; -.
DR EnsemblPlants; AT3G43600.1; AT3G43600.1; AT3G43600.
DR GeneID; 823457; -.
DR Gramene; AT3G43600.1; AT3G43600.1; AT3G43600.
DR KEGG; ath:AT3G43600; -.
DR Araport; AT3G43600; -.
DR TAIR; locus:2079834; AT3G43600.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_1_1; -.
DR InParanoid; Q7G192; -.
DR OMA; IPGPNYV; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q7G192; -.
DR BioCyc; ARA:AT3G43600-MON; -.
DR BioCyc; MetaCyc:AT3G43600-MON; -.
DR BRENDA; 1.2.3.1; 399.
DR SABIO-RK; Q7G192; -.
DR PRO; PR:Q7G192; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q7G192; baseline and differential.
DR Genevisible; Q7G192; AT.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004031; F:aldehyde oxidase activity; IDA:TAIR.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00207; fer2; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.43.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR11908; PTHR11908; 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 SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 1: Evidence at protein level;
KW 2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis; Cytoplasm; FAD;
KW Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..1321
FT /note="Indole-3-acetaldehyde oxidase"
FT /id="PRO_0000166110"
FT DOMAIN 1..90
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 215..404
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 42
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 47
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 50
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT CONFLICT 808
FT /note="K -> N (in Ref. 4; AAC39510)"
FT /evidence="ECO:0000305"
FT CONFLICT 1083
FT /note="S -> T (in Ref. 4; AAC39510)"
FT /evidence="ECO:0000305"
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
