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Protein

Indole-3-acetaldehyde oxidase

Gene

AAO1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

(Indol-3-yl)acetaldehyde + H2O + O2 = (indol-3-yl)acetate + H2O2.3 Publications

Cofactori

Protein has several cofactor binding sites:
  • [2Fe-2S] clusterBy similarityNote: Binds 2 [2Fe-2S] clusters.By similarity
  • FADBy similarity
  • Mo-molybdopterinBy similarityNote: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.By similarity

Enzyme regulationi

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.1 Publication

Kineticsi

Kinetic values were obtained with the AO-alpha dimer.

  1. KM=14 µM for heptaldehyde1 Publication
  2. KM=19 µM for protocatechualdehyde1 Publication
  3. KM=0.74 µM for benzaldehyde1 Publication
  4. KM=4.4 µM for indole-3-aldehyde1 Publication
  5. KM=39 µM for indole-3-acetaldehyde1 Publication
  6. KM=20 µM for cinnamaldehyde1 Publication
  7. KM=22 µM for citral1 Publication
  1. Vmax=7.1 nmol/min/mg enzyme with heptaldehyde as substrate1 Publication
  2. Vmax=8.0 nmol/min/mg enzyme with protocatechualdehyde as substrate1 Publication
  3. Vmax=17 nmol/min/mg enzyme with benzaldehyde as substrate1 Publication
  4. Vmax=6.9 nmol/min/mg enzyme with IAld as substrate1 Publication
  5. Vmax=7.3 nmol/min/mg enzyme with IAAld as substrate1 Publication
  6. Vmax=3.8 nmol/min/mg enzyme with cinnamaldehyde as substrate1 Publication
  7. Vmax=38 nmol/min/mg enzyme with citral as substrate1 Publication

pH dependencei

Optimum pH is 8.1 Publication

Temperature dependencei

Optimum temperature is 65 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi60 – 601Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi65 – 651Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation
Metal bindingi68 – 681Iron-sulfur (2Fe-2S)PROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • abscisic acid biosynthetic process Source: UniProtKB-KW
  • auxin biosynthetic process Source: TAIR
  • xanthine catabolic process Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Abscisic acid biosynthesis, Auxin biosynthesis

Keywords - Ligandi

2Fe-2S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding, Molybdenum, NAD

Enzyme and pathway databases

BioCyciARA:GQT-975-MONOMER.
MetaCyc:AT5G20960-MONOMER.
BRENDAi1.2.3.1. 399.
SABIO-RKQ7G193.

Names & Taxonomyi

Protein namesi
Recommended name:
Indole-3-acetaldehyde oxidase (EC:1.2.3.7)
Short name:
IAA oxidase
Alternative name(s):
Aldehyde oxidase 1
Short name:
AO-1
Short name:
AtAO-1
Short name:
AtAO1
Gene namesi
Name:AAO1
Synonyms:AO1
Ordered Locus Names:At5g20960
ORF Names:F22D1.130
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 5

Organism-specific databases

TAIRiAT5G20960.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 13681368Indole-3-acetaldehyde oxidasePRO_0000166109Add
BLAST

Proteomic databases

PaxDbiQ7G193.
PRIDEiQ7G193.

Expressioni

Tissue specificityi

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.5 Publications

Gene expression databases

GenevisibleiQ7G193. AT.

Interactioni

Subunit structurei

Aldehyde oxidases (AO) are homodimers and heterodimers of AO subunits. AO-alpha is an AAO1 homodimer; AO-beta is an AAO1-AAO2 heterodimer.1 Publication

Protein-protein interaction databases

BioGridi17496. 1 interaction.
IntActiQ7G193. 1 interaction.
STRINGi3702.AT5G20960.1.

Structurei

3D structure databases

ProteinModelPortaliQ7G193.
SMRiQ7G193. Positions 21-192, 597-1349.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 108902Fe-2S ferredoxin-typePROSITE-ProRule annotationAdd
BLAST
Domaini246 – 427182FAD-binding PCMH-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the xanthine dehydrogenase family.Curated
Contains 1 2Fe-2S ferredoxin-type domain.PROSITE-ProRule annotation
Contains 1 FAD-binding PCMH-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
InParanoidiQ7G193.
KOiK11817.
OMAiYHTINSK.
OrthoDBiEOG093600DW.
PhylomeDBiQ7G193.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q7G193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEKAIDEDK VEAMKSSKTS LVFAINGQRF ELELSSIDPS TTLVDFLRNK
60 70 80 90 100
TPFKSVKLGC GEGGCGACVV LLSKYDPLLE KVDEFTISSC LTLLCSIDGC
110 120 130 140 150
SITTSDGLGN SRVGFHAVHE RIAGFHATQC GFCTPGMSVS MFSALLNADK
160 170 180 190 200
SHPPPRSGFS NLTAVEAEKA VSGNLCRCTG YRPLVDACKS FAADVDIEDL
210 220 230 240 250
GFNAFCKKGE NRDEVLRRLP CYDHTSSHVC TFPEFLKKEI KNDMSLHSRK
260 270 280 290 300
YRWSSPVSVS ELQGLLEVEN GLSVKLVAGN TSTGYYKEEK ERKYERFIDI
310 320 330 340 350
RKIPEFTMVR SDEKGVELGA CVTISKAIEV LREEKNVSVL AKIATHMEKI
360 370 380 390 400
ANRFVRNTGT IGGNIMMAQR KQFPSDLATI LVAAQATVKI MTSSSSQEQF
410 420 430 440 450
TLEEFLQQPP LDAKSLLLSL EIPSWHSAKK NGSSEDSILL FETYRAAPRP
460 470 480 490 500
LGNALAFLNA AFSAEVTEAL DGIVVNDCQL VFGAYGTKHA HRAKKVEEFL
510 520 530 540 550
TGKVISDEVL MEAISLLKDE IVPDKGTSNP GYRSSLAVTF LFEFFGSLTK
560 570 580 590 600
KNAKTTNGWL NGGCKEIGFD QNVESLKPEA MLSSAQQIVE NQEHSPVGKG
610 620 630 640 650
ITKAGACLQA SGEAVYVDDI PAPENCLYGA FIYSTMPLAR IKGIRFKQNR
660 670 680 690 700
VPEGVLGIIT YKDIPKGGQN IGTNGFFTSD LLFAEEVTHC AGQIIAFLVA
710 720 730 740 750
DSQKHADIAA NLVVIDYDTK DLKPPILSLE EAVENFSLFE VPPPLRGYPV
760 770 780 790 800
GDITKGMDEA EHKILGSKIS FGSQYFFYME TQTALAVPDE DNCMVVYSST
810 820 830 840 850
QTPEFVHQTI AGCLGVPENN VRVITRRVGG GFGGKAVKSM PVAAACALAA
860 870 880 890 900
SKMQRPVRTY VNRKTDMITT GGRHPMKVTY SVGFKSNGKI TALDVEVLLD
910 920 930 940 950
AGLTEDISPL MPKGIQGALM KYDWGALSFN VKVCKTNTVS RTALRAPGDV
960 970 980 990 1000
QGSYIGEAII EKVASYLSVD VDEIRKVNLH TYESLRLFHS AKAGEFSEYT
1010 1020 1030 1040 1050
LPLLWDRIDE FSGFNKRRKV VEEFNASNKW RKRGISRVPA VYAVNMRSTP
1060 1070 1080 1090 1100
GRVSVLGDGS IVVEVQGIEI GQGLWTKVKQ MAAYSLGLIQ CGTTSDELLK
1110 1120 1130 1140 1150
KIRVIQSDTL SMVQGSMTAG STTSEASSEA VRICCDGLVE RLLPVKTALV
1160 1170 1180 1190 1200
EQTGGPVTWD SLISQAYQQS INMSVSSKYM PDSTGEYLNY GIAASEVEVN
1210 1220 1230 1240 1250
VLTGETTILR TDIIYDCGKS LNPAVDLGQI EGAFVQGLGF FMLEEFLMNS
1260 1270 1280 1290 1300
DGLVVTDSTW TYKIPTVDTI PRQFNVEILN SGQHKNRVLS SKASGEPPLL
1310 1320 1330 1340 1350
LAASVHCAVR AAVKEARKQI LSWNSNKQGT DMYFELPVPA TMPIVKEFCG
1360
LDVVEKYLEW KIQQRKNV
Length:1,368
Mass (Da):149,554
Last modified:April 26, 2005 - v2
Checksum:i58C165F4114DC70C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti16 – 161S → G in AAC39509 (PubMed:9655945).Curated
Sequence conflicti150 – 1501K → R in AAC39509 (PubMed:9655945).Curated
Sequence conflicti336 – 3438NVSVLAKI → MFLCWRKY in AAC39509 (PubMed:9655945).Curated
Sequence conflicti624 – 6241E → K in AAC39509 (PubMed:9655945).Curated
Sequence conflicti708 – 7081I → V in AAC39509 (PubMed:9655945).Curated
Sequence conflicti1260 – 12601W → L in AAC39509 (PubMed:9655945).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039895 mRNA. Translation: AAC39509.1.
AB005804 mRNA. Translation: BAA28624.1.
AF296834 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92912.1.
CP002688 Genomic DNA. Translation: AED92913.1.
PIRiT51622.
T52049.
RefSeqiNP_568407.2. NM_122105.2.
NP_851049.1. NM_180718.1.
UniGeneiAt.19954.

Genome annotation databases

EnsemblPlantsiAT5G20960.1; AT5G20960.1; AT5G20960.
AT5G20960.2; AT5G20960.2; AT5G20960.
GeneIDi832221.
GrameneiAT5G20960.1; AT5G20960.1; AT5G20960.
AT5G20960.2; AT5G20960.2; AT5G20960.
KEGGiath:AT5G20960.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF039895 mRNA. Translation: AAC39509.1.
AB005804 mRNA. Translation: BAA28624.1.
AF296834 Genomic DNA. No translation available.
CP002688 Genomic DNA. Translation: AED92912.1.
CP002688 Genomic DNA. Translation: AED92913.1.
PIRiT51622.
T52049.
RefSeqiNP_568407.2. NM_122105.2.
NP_851049.1. NM_180718.1.
UniGeneiAt.19954.

3D structure databases

ProteinModelPortaliQ7G193.
SMRiQ7G193. Positions 21-192, 597-1349.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi17496. 1 interaction.
IntActiQ7G193. 1 interaction.
STRINGi3702.AT5G20960.1.

Proteomic databases

PaxDbiQ7G193.
PRIDEiQ7G193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblPlantsiAT5G20960.1; AT5G20960.1; AT5G20960.
AT5G20960.2; AT5G20960.2; AT5G20960.
GeneIDi832221.
GrameneiAT5G20960.1; AT5G20960.1; AT5G20960.
AT5G20960.2; AT5G20960.2; AT5G20960.
KEGGiath:AT5G20960.

Organism-specific databases

TAIRiAT5G20960.

Phylogenomic databases

eggNOGiKOG0430. Eukaryota.
COG4630. LUCA.
COG4631. LUCA.
HOGENOMiHOG000191197.
InParanoidiQ7G193.
KOiK11817.
OMAiYHTINSK.
OrthoDBiEOG093600DW.
PhylomeDBiQ7G193.

Enzyme and pathway databases

BioCyciARA:GQT-975-MONOMER.
MetaCyc:AT5G20960-MONOMER.
BRENDAi1.2.3.1. 399.
SABIO-RKQ7G193.

Miscellaneous databases

PROiQ7G193.

Gene expression databases

GenevisibleiQ7G193. AT.

Family and domain databases

Gene3Di1.10.150.120. 1 hit.
3.10.20.30. 1 hit.
3.30.365.10. 6 hits.
3.30.43.10. 1 hit.
3.30.465.10. 1 hit.
3.90.1170.50. 1 hit.
InterProiIPR002888. 2Fe-2S-bd.
IPR001041. 2Fe-2S_ferredoxin-type.
IPR006058. 2Fe2S_fd_BS.
IPR000674. Ald_Oxase/Xan_DH_a/b.
IPR016208. Ald_Oxase/xanthine_DH.
IPR008274. AldOxase/xan_DH_Mopterin-bd.
IPR012675. Beta-grasp_dom.
IPR005107. CO_DH_flav_C.
IPR016169. CO_DH_flavot_FAD-bd_sub2.
IPR016166. FAD-bd_2.
IPR016167. FAD-bd_2_sub1.
IPR002346. Mopterin_DH_FAD-bd.
[Graphical view]
PfamiPF01315. Ald_Xan_dh_C. 1 hit.
PF02738. Ald_Xan_dh_C2. 1 hit.
PF03450. CO_deh_flav_C. 1 hit.
PF00941. FAD_binding_5. 1 hit.
PF00111. Fer2. 1 hit.
PF01799. Fer2_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000127. Xanthine_DH. 1 hit.
SMARTiSM01008. Ald_Xan_dh_C. 1 hit.
SM01092. CO_deh_flav_C. 1 hit.
[Graphical view]
SUPFAMiSSF47741. SSF47741. 1 hit.
SSF54292. SSF54292. 1 hit.
SSF54665. SSF54665. 1 hit.
SSF55447. SSF55447. 1 hit.
SSF56003. SSF56003. 1 hit.
SSF56176. SSF56176. 1 hit.
PROSITEiPS00197. 2FE2S_FER_1. 1 hit.
PS51085. 2FE2S_FER_2. 1 hit.
PS51387. FAD_PCMH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiALDO1_ARATH
AccessioniPrimary (citable) accession number: Q7G193
Secondary accession number(s): O49155, O64417
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: April 26, 2005
Last modified: September 7, 2016
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.