Reviewed, UniProtKB/Swiss-Prot Q7G193 (ALDO1_ARATH)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase 1
      Short name(s)=AO-1, AtAO-1, AtAO1
    EC=1.2.3.1

Gene names

Name:	AAO1
Synonyms:	AO1
Ordered Locus Names:	At5g20960
ORF Names:	F22D1.130

Organism

Arabidopsis thaliana (Mouse-ear cress) [Complete proteome]

Taxonomic identifier

3702 [NCBI]

Taxonomic lineage

Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › rosids › eurosids II › Brassicales › Brassicaceae › Arabidopsis

Protein attributes

Sequence length	1368 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

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.
Catalytic activity	An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2).
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Molybdopterin By similarity.
Enzyme 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.
Subunit structure	Aldehyde oxidases (AO) are homo- and heterodimers of AO subunits. AO-alpha is an AAO1 homodimer; AO-beta is an AAO1-AAO2 heterodimer.
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.
Sequence similarities	Belongs to the xanthine dehydrogenase family. Contains 1 2Fe-2S ferredoxin-type domain. Contains 1 FAD-binding PCMH-type domain.
Biophysicochemical properties	Kinetic parameters: Kinetic values were obtained with the AO-alpha dimer. KM=14 µM for heptaldehyde KM=19 µM for protocatechualdehyde KM=0.74 µM for benzaldehyde KM=4.4 µM for indole-3-aldehyde KM=39 µM for indole-3-acetaldehyde KM=20 µM for cinnamaldehyde KM=22 µM for citral Vmax=7.1 nmol/min/mg enzyme with heptaldehyde as substrate Vmax=8.0 nmol/min/mg enzyme with protocatechualdehyde as substrate Vmax=17 nmol/min/mg enzyme with benzaldehyde as substrate Vmax=6.9 nmol/min/mg enzyme with IAld as substrate Vmax=7.3 nmol/min/mg enzyme with IAAld as substrate Vmax=3.8 nmol/min/mg enzyme with cinnamaldehyde as substrate Vmax=38 nmol/min/mg enzyme with citral as substrate pH dependence: Optimum pH is 8. Temperature dependence: Optimum temperature is 65 degrees Celsius.

Ontologies

Keywords
Biological process	Abscisic acid biosynthesis Auxin biosynthesis
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Molecular function	aldehyde oxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 1368	1368	Aldehyde oxidase 1
Regions
	Domain	19 – 108	90	2Fe-2S ferredoxin-type
	Domain	246 – 427	182	FAD-binding PCMH-type
Sites
	Metal binding	60	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	65	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	68	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	16	1	S → G in AAC39509. Ref.1
	Sequence conflict	150	1	K → R in AAC39509. Ref.1
	Sequence conflict	336 – 343	8	NVSVLAKI → MFLCWRKY in AAC39509. Ref.1
	Sequence conflict	624	1	E → K in AAC39509. Ref.1
	Sequence conflict	708	1	I → V in AAC39509. Ref.1
	Sequence conflict	1260	1	W → L in AAC39509. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q7G193-1 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: 58C165F4114DC70C	FASTA	1,368	149,554
	10 20 30 40 50 60 MGEKAIDEDK VEAMKSSKTS LVFAINGQRF ELELSSIDPS TTLVDFLRNK TPFKSVKLGC 70 80 90 100 110 120 GEGGCGACVV LLSKYDPLLE KVDEFTISSC LTLLCSIDGC SITTSDGLGN SRVGFHAVHE 130 140 150 160 170 180 RIAGFHATQC GFCTPGMSVS MFSALLNADK SHPPPRSGFS NLTAVEAEKA VSGNLCRCTG 190 200 210 220 230 240 YRPLVDACKS FAADVDIEDL GFNAFCKKGE NRDEVLRRLP CYDHTSSHVC TFPEFLKKEI 250 260 270 280 290 300 KNDMSLHSRK YRWSSPVSVS ELQGLLEVEN GLSVKLVAGN TSTGYYKEEK ERKYERFIDI 310 320 330 340 350 360 RKIPEFTMVR SDEKGVELGA CVTISKAIEV LREEKNVSVL AKIATHMEKI ANRFVRNTGT 370 380 390 400 410 420 IGGNIMMAQR KQFPSDLATI LVAAQATVKI MTSSSSQEQF TLEEFLQQPP LDAKSLLLSL 430 440 450 460 470 480 EIPSWHSAKK NGSSEDSILL FETYRAAPRP LGNALAFLNA AFSAEVTEAL DGIVVNDCQL 490 500 510 520 530 540 VFGAYGTKHA HRAKKVEEFL TGKVISDEVL MEAISLLKDE IVPDKGTSNP GYRSSLAVTF 550 560 570 580 590 600 LFEFFGSLTK KNAKTTNGWL NGGCKEIGFD QNVESLKPEA MLSSAQQIVE NQEHSPVGKG 610 620 630 640 650 660 ITKAGACLQA SGEAVYVDDI PAPENCLYGA FIYSTMPLAR IKGIRFKQNR VPEGVLGIIT 670 680 690 700 710 720 YKDIPKGGQN IGTNGFFTSD LLFAEEVTHC AGQIIAFLVA DSQKHADIAA NLVVIDYDTK 730 740 750 760 770 780 DLKPPILSLE EAVENFSLFE VPPPLRGYPV GDITKGMDEA EHKILGSKIS FGSQYFFYME 790 800 810 820 830 840 TQTALAVPDE DNCMVVYSST QTPEFVHQTI AGCLGVPENN VRVITRRVGG GFGGKAVKSM 850 860 870 880 890 900 PVAAACALAA SKMQRPVRTY VNRKTDMITT GGRHPMKVTY SVGFKSNGKI TALDVEVLLD 910 920 930 940 950 960 AGLTEDISPL MPKGIQGALM KYDWGALSFN VKVCKTNTVS RTALRAPGDV QGSYIGEAII 970 980 990 1000 1010 1020 EKVASYLSVD VDEIRKVNLH TYESLRLFHS AKAGEFSEYT LPLLWDRIDE FSGFNKRRKV 1030 1040 1050 1060 1070 1080 VEEFNASNKW RKRGISRVPA VYAVNMRSTP GRVSVLGDGS IVVEVQGIEI GQGLWTKVKQ 1090 1100 1110 1120 1130 1140 MAAYSLGLIQ CGTTSDELLK KIRVIQSDTL SMVQGSMTAG STTSEASSEA VRICCDGLVE 1150 1160 1170 1180 1190 1200 RLLPVKTALV EQTGGPVTWD SLISQAYQQS INMSVSSKYM PDSTGEYLNY GIAASEVEVN 1210 1220 1230 1240 1250 1260 VLTGETTILR TDIIYDCGKS LNPAVDLGQI EGAFVQGLGF FMLEEFLMNS DGLVVTDSTW 1270 1280 1290 1300 1310 1320 TYKIPTVDTI PRQFNVEILN SGQHKNRVLS SKASGEPPLL LAASVHCAVR AAVKEARKQI 1330 1340 1350 1360 LSWNSNKQGT DMYFELPVPA TMPIVKEFCG LDVVEKYLEW KIQQRKNV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Biochemical and genetic characterization of three molybdenum cofactor hydroxylases in Arabidopsis thaliana." Hoff T., Frandsen G.I., Rocher A., Mundy J. Biochim. Biophys. Acta 1398:397-402(1998) [PubMed: 9655945] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Root.
[2]	"Molecular cloning and characterization of aldehyde oxidases in Arabidopsis thaliana." Sekimoto H., Seo M., Kawakami N., Komano T., Desloire S., Liotenberg S., Marion-Poll A., Caboche M., Kamiya Y., Koshiba T. Plant Cell Physiol. 39:433-442(1998) [PubMed: 9615466] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: cv. Columbia. Tissue: Seedling hypocotyl.
[3]	"Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana." 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. Nature 408:823-826(2000) [PubMed: 11130714] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[4]	"Higher activity of an aldehyde oxidase in the auxin-overproducing superroot1 mutant of Arabidopsis thaliana." Seo M., Akaba S., Oritani T., Delarue M., Bellini C., Caboche M., Koshiba T. Plant Physiol. 116:687-693(1998) [PubMed: 9489015] [Abstract] Cited for: FUNCTION, TISSUE SPECIFICITY, SUBSTRATE SPECIFICITY.
[5]	"Production of homo- and hetero-dimeric isozymes from two aldehyde oxidase genes of Arabidopsis thaliana." Akaba S., Seo M., Dohmae N., Takio K., Sekimoto H., Kamiya Y., Furuya N., Komano T., Koshiba T. J. Biochem. 126:395-401(1999) [PubMed: 10423535] [Abstract] Cited for: SUBUNIT, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY.
[6]	"Functional expression of two Arabidopsis aldehyde oxidases in the yeast Pichia pastoris." Koiwai H., Akaba S., Seo M., Komano T., Koshiba T. J. Biochem. 127:659-664(2000) [PubMed: 10739959] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION.
[7]	"Abscisic aldehyde oxidase in leaves of Arabidopsis thaliana." Seo M., Koiwai H., Akaba S., Komano T., Oritani T., Kamiya Y., Koshiba T. Plant J. 23:481-488(2000) [PubMed: 10972874] [Abstract] Cited for: TISSUE SPECIFICITY.
[8]	"Comparative studies on the Arabidopsis aldehyde oxidase (AAO) gene family revealed a major role of AAO3 in ABA biosynthesis in seeds." Seo M., Aoki H., Koiwai H., Kamiya Y., Nambara E., Koshiba T. Plant Cell Physiol. 45:1694-1703(2004) [PubMed: 15574845] [Abstract] Cited for: TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF039895 mRNA. Translation: AAC39509.1. AB005804 mRNA. Translation: BAA28624.1. AF296834 Genomic DNA. No translation available.
PIR	T51622. T52049.
RefSeq	NP_568407.2. NP_851049.1.
UniGene	At.19954
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Genome annotation databases
GeneID	832221.
GenomeReviews	Gene locus AT5G20960 in contig BA000015_GR.
KEGG	ath:AT5G20960.
NMPDR	fig|3702.1.peg.24312.
Organism-specific databases
GeneFarm	4892. 470.
TAIR	At5g20960.
Gene expression databases
GermOnline	AT5G20960. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DHase_a/b. IPR016208. Ald_Oxase/xanthine_DHase. IPR008274. AldOxase/xan_DHase_Mopterin-bd. IPR012675. b-grasp_ferredoxin-like. IPR005107. CO_DHase_flav_C. IPR016169. CO_DHase_flavot_FAD-bd_sub2. IPR001041. Ferredoxin. IPR002346. Mopterin_DHase_FAD-bd. IPR000572. OxRdtase_Mopterin-bd. [Graphical view]
Gene3D	G3DSA:3.30.365.10. Ald_xan_DH_mo_bd. 2 hits. G3DSA:3.90.1170.50. Aldxan_DH_hamm. 1 hit. G3DSA:3.30.390.50. CO_DH_flav_C. 1 hit. G3DSA:3.30.465.10. CO_DH_flavoprot_FAD-bd_sub2. 1 hit. G3DSA:3.10.20.30. Ferredoxin_fold. 1 hit.
Pfam	PF01315. 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]
PIRSF	PIRSF000127. Xanthine_DH. 1 hit.
ProDom	PD186071. 2Fe-2S_bind. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00197. 2FE2S_FER_1. 1 hit. PS51085. 2FE2S_FER_2. 1 hit. PS51387. FAD_PCMH. 1 hit. PS00559. MOLYBDOPTERIN_EUK. False negative. [Graphical view]
BLOCKS	Search...
Other Resources
ProtoNet	Search...

Entry information

Entry name

ALDO1_ARATH

Accession

Primary (citable) accession number: Q7G193
Secondary accession number(s): O49155, O64417

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	July 22, 2008
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)