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Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase 1) (AO-1) (AtAO-1) (AtAO1)

 ALDO1_ARATH             Reviewed;        1368 AA.
Q7G193; O49155; O64417;
26-APR-2005, integrated into UniProtKB/Swiss-Prot.
26-APR-2005, sequence version 2.
05-DEC-2018, entry version 129.
RecName: Full=Indole-3-acetaldehyde oxidase;
Short=IAA oxidase;
EC=1.2.3.7;
AltName: Full=Aldehyde oxidase 1;
Short=AO-1;
Short=AtAO-1;
Short=AtAO1;
Name=AAO1; Synonyms=AO1; OrderedLocusNames=At5g20960;
ORFNames=F22D1.130;
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=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).
[2]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
PubMed=11130714; DOI=10.1038/35048507;
Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K.,
Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S.,
Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T.,
Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M.,
Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R.,
Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J.,
Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M.,
Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M.,
Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P.,
Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C.,
Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N.,
Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J.,
Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S.,
Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W.,
Ramsperger U., Wedler H., Balke K., Wedler E., Peters S.,
van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R.,
Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S.,
Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W.,
Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H.,
Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.;
"Sequence and analysis of chromosome 5 of the plant Arabidopsis
thaliana.";
Nature 408:823-826(2000).
[4]
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).
[5]
FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY, AND CATALYTIC
ACTIVITY.
STRAIN=cv. Columbia;
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, ACTIVITY REGULATION, AND CATALYTIC
ACTIVITY.
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).
-!- FUNCTION: In higher plants aldehyde oxidases (AO) appear to be
homo- and heterodimeric assemblies of AO subunits with probably
different physiological functions. AO-alpha may be involved in the
biosynthesis of auxin, and in biosynthesis of abscisic acid (ABA)
in seeds. In vitro, AO-alpha uses heptaldehyde,
protocatechualdehyde, benzaldehyde, indole-3-aldehyde (IAld),
indole-3-acetaldehyde (IAAld), cinnamaldehyde and citral as
substrates; AO-beta uses IAAld, IAld and naphtaldehyde as
substrates. {ECO:0000269|PubMed:9489015}.
-!- CATALYTIC ACTIVITY:
Reaction=H2O + indole-3-acetaldehyde + O2 = (indol-3-yl)acetate +
H(+) + H2O2; Xref=Rhea:RHEA:16277, ChEBI:CHEBI:15377,
ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
ChEBI:CHEBI:18086, ChEBI:CHEBI:30854; EC=1.2.3.7;
Evidence={ECO:0000269|PubMed:10423535,
ECO:0000269|PubMed:10739959, ECO:0000269|PubMed:9489015};
-!- 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};
-!- ACTIVITY REGULATION: Strongly inhibited by iodoacetate and
potassium cyanide (KCN). Weakly inhibited by 2-mercaptoethanol,
dithiothreitol (DTT), menadione, estradiol, 4'-(9-
acridinylamino)methanesulfon-m-anisidine (mAMSA), allopurinol and
tritonX-100. Not affected by p-chloromercuribenzoate.
{ECO:0000269|PubMed:10739959}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=14 uM for heptaldehyde {ECO:0000269|PubMed:10739959};
KM=19 uM for protocatechualdehyde {ECO:0000269|PubMed:10739959};
KM=0.74 uM for benzaldehyde {ECO:0000269|PubMed:10739959};
KM=4.4 uM for indole-3-aldehyde {ECO:0000269|PubMed:10739959};
KM=39 uM for indole-3-acetaldehyde
{ECO:0000269|PubMed:10739959};
KM=20 uM for cinnamaldehyde {ECO:0000269|PubMed:10739959};
KM=22 uM for citral {ECO:0000269|PubMed:10739959};
Vmax=7.1 nmol/min/mg enzyme with heptaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=8.0 nmol/min/mg enzyme with protocatechualdehyde as
substrate {ECO:0000269|PubMed:10739959};
Vmax=17 nmol/min/mg enzyme with benzaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=6.9 nmol/min/mg enzyme with IAld as substrate
{ECO:0000269|PubMed:10739959};
Vmax=7.3 nmol/min/mg enzyme with IAAld as substrate
{ECO:0000269|PubMed:10739959};
Vmax=3.8 nmol/min/mg enzyme with cinnamaldehyde as substrate
{ECO:0000269|PubMed:10739959};
Vmax=38 nmol/min/mg enzyme with citral as substrate
{ECO:0000269|PubMed:10739959};
Note=Kinetic values were obtained with the AO-alpha dimer.;
pH dependence:
Optimum pH is 8. {ECO:0000269|PubMed:10739959};
Temperature dependence:
Optimum temperature is 65 degrees Celsius.
{ECO:0000269|PubMed:10739959};
-!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of
AO subunits. AO-alpha is an AAO1 homodimer; AO-beta is an AAO1-
AAO2 heterodimer. {ECO:0000269|PubMed:10423535}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- TISSUE SPECIFICITY: Predominantly expressed in roots, seedlings,
mature siliques and seeds, and to lower extent in stems and
rosettes. In seedlings, mostly expressed in lower part of
hypocotyls and roots. {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; AF039895; AAC39509.1; -; mRNA.
EMBL; AB005804; BAA28624.1; -; mRNA.
EMBL; AF296834; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CP002688; AED92912.1; -; Genomic_DNA.
EMBL; CP002688; AED92913.1; -; Genomic_DNA.
PIR; T51622; T51622.
PIR; T52049; T52049.
RefSeq; NP_568407.2; NM_122105.3.
RefSeq; NP_851049.1; NM_180718.2.
UniGene; At.19954; -.
ProteinModelPortal; Q7G193; -.
SMR; Q7G193; -.
BioGrid; 17496; 1.
IntAct; Q7G193; 1.
STRING; 3702.AT5G20960.1; -.
PaxDb; Q7G193; -.
PRIDE; Q7G193; -.
EnsemblPlants; AT5G20960.1; AT5G20960.1; AT5G20960.
EnsemblPlants; AT5G20960.2; AT5G20960.2; AT5G20960.
GeneID; 832221; -.
Gramene; AT5G20960.1; AT5G20960.1; AT5G20960.
Gramene; AT5G20960.2; AT5G20960.2; AT5G20960.
KEGG; ath:AT5G20960; -.
Araport; AT5G20960; -.
TAIR; locus:2147127; AT5G20960.
eggNOG; KOG0430; Eukaryota.
eggNOG; COG4630; LUCA.
eggNOG; COG4631; LUCA.
HOGENOM; HOG000191197; -.
InParanoid; Q7G193; -.
KO; K11817; -.
OMA; AKATWVE; -.
OrthoDB; EOG093600DW; -.
PhylomeDB; Q7G193; -.
BioCyc; ARA:AT5G20960-MONOMER; -.
BioCyc; MetaCyc:AT5G20960-MONOMER; -.
BRENDA; 1.2.3.1; 399.
Reactome; R-ATH-964975; Vitamins B6 activation to pyridoxal phosphate.
SABIO-RK; Q7G193; -.
PRO; PR:Q7G193; -.
Proteomes; UP000006548; Chromosome 5.
ExpressionAtlas; Q7G193; baseline and differential.
Genevisible; Q7G193; AT.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0071949; F:FAD binding; IEA:InterPro.
GO; GO:0050302; F:indole-3-acetaldehyde oxidase activity; IDA:TAIR.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0009851; P:auxin biosynthetic process; IMP:TAIR.
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_PCMH.
InterPro; IPR036318; FAD-bd_PCMH-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 1368 Indole-3-acetaldehyde oxidase.
/FTId=PRO_0000166109.
DOMAIN 19 108 2Fe-2S ferredoxin-type.
{ECO:0000255|PROSITE-ProRule:PRU00465}.
DOMAIN 246 427 FAD-binding PCMH-type.
{ECO:0000255|PROSITE-ProRule:PRU00718}.
METAL 60 60 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 65 65 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
METAL 68 68 Iron-sulfur (2Fe-2S).
{ECO:0000255|PROSITE-ProRule:PRU00465}.
CONFLICT 16 16 S -> G (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 150 150 K -> R (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 336 343 NVSVLAKI -> MFLCWRKY (in Ref. 1;
AAC39509). {ECO:0000305}.
CONFLICT 624 624 E -> K (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 708 708 I -> V (in Ref. 1; AAC39509).
{ECO:0000305}.
CONFLICT 1260 1260 W -> L (in Ref. 1; AAC39509).
{ECO:0000305}.
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


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EIAAB10105 COX7A2,COX7AL,Cytochrome c oxidase subunit 7A2, mitochondrial,Cytochrome c oxidase subunit VIIaL,Cytochrome c oxidase subunit VIIa-L,Cytochrome c oxidase subunit VIIa-liver_heart,Homo sapiens,Human
EIAAB08786 Canis familiaris,Canis lupus familiaris,COX8B,COX8H,Cytochrome c oxidase polypeptide VIII-heart,Cytochrome c oxidase subunit 8-1,Cytochrome c oxidase subunit 8B, mitochondrial,Cytochrome c oxidase sub
EIAAB10086 COX VIa-M,COX6A,COX6A2,COX6AH,COXVIAH,Cytochrome c oxidase polypeptide VIa-heart,Cytochrome c oxidase subunit 6A2, mitochondrial,Cytochrome c oxidase subunit VIA-muscle,Homo sapiens,Human


 

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