ALDO1_ARATH
ID ALDO1_ARATH Reviewed; 1368 AA.
AC Q7G193; O49155; O64417;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Indole-3-acetaldehyde oxidase;
DE Short=IAA oxidase;
DE EC=1.2.3.7;
DE AltName: Full=Aldehyde oxidase 1;
DE Short=AO-1;
DE Short=AtAO-1;
DE Short=AtAO1;
GN Name=AAO1; Synonyms=AO1; OrderedLocusNames=At5g20960; ORFNames=F22D1.130;
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=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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(2000).
RN [4]
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 [5]
RP FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND CATALYTIC
RP ACTIVITY.
RC STRAIN=cv. Columbia;
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, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
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).
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-alpha may be involved in the
CC biosynthesis of auxin, and in biosynthesis of abscisic acid (ABA) in
CC seeds. In vitro, AO-alpha uses heptaldehyde, protocatechualdehyde,
CC benzaldehyde, indole-3-aldehyde (IAld), indole-3-acetaldehyde (IAAld),
CC cinnamaldehyde and citral as substrates; AO-beta uses IAAld, IAld and
CC naphtaldehyde as substrates. {ECO:0000269|PubMed:9489015}.
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; Evidence={ECO:0000269|PubMed:10423535,
CC ECO:0000269|PubMed:10739959, ECO:0000269|PubMed:9489015};
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 and potassium
CC cyanide (KCN). Weakly inhibited by 2-mercaptoethanol, dithiothreitol
CC (DTT), menadione, estradiol, 4'-(9-acridinylamino)methanesulfon-m-
CC anisidine (mAMSA), allopurinol and tritonX-100. Not affected by p-
CC chloromercuribenzoate. {ECO:0000269|PubMed:10739959}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 uM for heptaldehyde {ECO:0000269|PubMed:10739959};
CC KM=19 uM for protocatechualdehyde {ECO:0000269|PubMed:10739959};
CC KM=0.74 uM for benzaldehyde {ECO:0000269|PubMed:10739959};
CC KM=4.4 uM for indole-3-aldehyde {ECO:0000269|PubMed:10739959};
CC KM=39 uM for indole-3-acetaldehyde {ECO:0000269|PubMed:10739959};
CC KM=20 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959};
CC KM=22 uM for citral {ECO:0000269|PubMed:10739959};
CC Vmax=7.1 nmol/min/mg enzyme with heptaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=8.0 nmol/min/mg enzyme with protocatechualdehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=17 nmol/min/mg enzyme with benzaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=6.9 nmol/min/mg enzyme with IAld as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=7.3 nmol/min/mg enzyme with IAAld as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=3.8 nmol/min/mg enzyme with cinnamaldehyde as substrate
CC {ECO:0000269|PubMed:10739959};
CC Vmax=38 nmol/min/mg enzyme with citral as substrate
CC {ECO:0000269|PubMed:10739959};
CC Note=Kinetic values were obtained with the AO-alpha dimer.;
CC pH dependence:
CC Optimum pH is 8. {ECO:0000269|PubMed:10739959};
CC Temperature dependence:
CC Optimum temperature is 65 degrees Celsius.
CC {ECO:0000269|PubMed:10739959};
CC -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of AO
CC subunits. AO-alpha is an AAO1 homodimer; AO-beta is an AAO1-AAO2
CC heterodimer. {ECO:0000269|PubMed:10423535}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in roots, seedlings, mature
CC siliques and seeds, and to lower extent in stems and rosettes. In
CC seedlings, mostly expressed in lower part of hypocotyls and roots.
CC {ECO:0000269|PubMed:10972874, ECO:0000269|PubMed:15574845,
CC ECO:0000269|PubMed:9489015, ECO:0000269|PubMed:9615466,
CC ECO:0000269|PubMed:9655945}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AF039895; AAC39509.1; -; mRNA.
DR EMBL; AB005804; BAA28624.1; -; mRNA.
DR EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CP002688; AED92912.1; -; Genomic_DNA.
DR EMBL; CP002688; AED92913.1; -; Genomic_DNA.
DR PIR; T51622; T51622.
DR PIR; T52049; T52049.
DR RefSeq; NP_568407.2; NM_122105.3.
DR RefSeq; NP_851049.1; NM_180718.2.
DR AlphaFoldDB; Q7G193; -.
DR SMR; Q7G193; -.
DR BioGRID; 17496; 1.
DR IntAct; Q7G193; 1.
DR STRING; 3702.AT5G20960.1; -.
DR PaxDb; Q7G193; -.
DR PRIDE; Q7G193; -.
DR ProteomicsDB; 244869; -.
DR EnsemblPlants; AT5G20960.1; AT5G20960.1; AT5G20960.
DR EnsemblPlants; AT5G20960.2; AT5G20960.2; AT5G20960.
DR GeneID; 832221; -.
DR Gramene; AT5G20960.1; AT5G20960.1; AT5G20960.
DR Gramene; AT5G20960.2; AT5G20960.2; AT5G20960.
DR KEGG; ath:AT5G20960; -.
DR Araport; AT5G20960; -.
DR TAIR; locus:2147127; AT5G20960.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_2_1; -.
DR InParanoid; Q7G193; -.
DR OMA; HWYWPKT; -.
DR OrthoDB; 48717at2759; -.
DR PhylomeDB; Q7G193; -.
DR BioCyc; ARA:AT5G20960-MON; -.
DR BioCyc; MetaCyc:AT5G20960-MON; -.
DR BRENDA; 1.2.3.1; 399.
DR BRENDA; 1.2.3.7; 399.
DR SABIO-RK; Q7G193; -.
DR PRO; PR:Q7G193; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q7G193; baseline and differential.
DR Genevisible; Q7G193; AT.
DR GO; GO:0009536; C:plastid; HDA:TAIR.
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; IDA:TAIR.
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; IMP:TAIR.
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..1368
FT /note="Indole-3-acetaldehyde oxidase"
FT /id="PRO_0000166109"
FT DOMAIN 19..108
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 246..427
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT BINDING 60
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 65
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 68
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT CONFLICT 16
FT /note="S -> G (in Ref. 1; AAC39509)"
FT /evidence="ECO:0000305"
FT CONFLICT 150
FT /note="K -> R (in Ref. 1; AAC39509)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..343
FT /note="NVSVLAKI -> MFLCWRKY (in Ref. 1; AAC39509)"
FT /evidence="ECO:0000305"
FT CONFLICT 624
FT /note="E -> K (in Ref. 1; AAC39509)"
FT /evidence="ECO:0000305"
FT CONFLICT 708
FT /note="I -> V (in Ref. 1; AAC39509)"
FT /evidence="ECO:0000305"
FT CONFLICT 1260
FT /note="W -> L (in Ref. 1; AAC39509)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1368 AA; 149554 MW; 58C165F4114DC70C CRC64;
MGEKAIDEDK VEAMKSSKTS LVFAINGQRF ELELSSIDPS TTLVDFLRNK TPFKSVKLGC
GEGGCGACVV LLSKYDPLLE KVDEFTISSC LTLLCSIDGC SITTSDGLGN SRVGFHAVHE
RIAGFHATQC GFCTPGMSVS MFSALLNADK SHPPPRSGFS NLTAVEAEKA VSGNLCRCTG
YRPLVDACKS FAADVDIEDL GFNAFCKKGE NRDEVLRRLP CYDHTSSHVC TFPEFLKKEI
KNDMSLHSRK YRWSSPVSVS ELQGLLEVEN GLSVKLVAGN TSTGYYKEEK ERKYERFIDI
RKIPEFTMVR SDEKGVELGA CVTISKAIEV LREEKNVSVL AKIATHMEKI ANRFVRNTGT
IGGNIMMAQR KQFPSDLATI LVAAQATVKI MTSSSSQEQF TLEEFLQQPP LDAKSLLLSL
EIPSWHSAKK NGSSEDSILL FETYRAAPRP LGNALAFLNA AFSAEVTEAL DGIVVNDCQL
VFGAYGTKHA HRAKKVEEFL TGKVISDEVL MEAISLLKDE IVPDKGTSNP GYRSSLAVTF
LFEFFGSLTK KNAKTTNGWL NGGCKEIGFD QNVESLKPEA MLSSAQQIVE NQEHSPVGKG
ITKAGACLQA SGEAVYVDDI PAPENCLYGA FIYSTMPLAR IKGIRFKQNR VPEGVLGIIT
YKDIPKGGQN IGTNGFFTSD LLFAEEVTHC AGQIIAFLVA DSQKHADIAA NLVVIDYDTK
DLKPPILSLE EAVENFSLFE VPPPLRGYPV GDITKGMDEA EHKILGSKIS FGSQYFFYME
TQTALAVPDE DNCMVVYSST QTPEFVHQTI AGCLGVPENN VRVITRRVGG GFGGKAVKSM
PVAAACALAA SKMQRPVRTY VNRKTDMITT GGRHPMKVTY SVGFKSNGKI TALDVEVLLD
AGLTEDISPL MPKGIQGALM KYDWGALSFN VKVCKTNTVS RTALRAPGDV QGSYIGEAII
EKVASYLSVD VDEIRKVNLH TYESLRLFHS AKAGEFSEYT LPLLWDRIDE FSGFNKRRKV
VEEFNASNKW RKRGISRVPA VYAVNMRSTP GRVSVLGDGS IVVEVQGIEI GQGLWTKVKQ
MAAYSLGLIQ CGTTSDELLK KIRVIQSDTL SMVQGSMTAG STTSEASSEA VRICCDGLVE
RLLPVKTALV EQTGGPVTWD SLISQAYQQS INMSVSSKYM PDSTGEYLNY GIAASEVEVN
VLTGETTILR TDIIYDCGKS LNPAVDLGQI EGAFVQGLGF FMLEEFLMNS DGLVVTDSTW
TYKIPTVDTI PRQFNVEILN SGQHKNRVLS SKASGEPPLL LAASVHCAVR AAVKEARKQI
LSWNSNKQGT DMYFELPVPA TMPIVKEFCG LDVVEKYLEW KIQQRKNV
