Reviewed, UniProtKB/Swiss-Prot Q7G192 (ALDO2_ARATH)

Names and origin

Protein names

Recommended name:
    Aldehyde oxidase 2
      Short name=AO-2
      Short name=AtAO-2
      Short name=AtAO3
    EC=1.2.3.1

Gene names

Name:	AAO2
Synonyms:	AO3
Ordered Locus Names:	At3g43600
ORF Names:	F22J12.40

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	1321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	In higher plant aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. In vitro, AO-gamma uses heptaldehyde, benzaldehyde, naphthaldehyde and cinnamaldehyde as substrates; AO-beta uses indole-3-acetaldehyde (IAAld), indole-3-aldehyde (IAld) and naphtaldehyde; the AAO2-AAO3 dimer uses abscisic aldehyde.
Catalytic activity	An aldehyde + H2O + O2 = a carboxylic acid + H2O2. Ref.5
Cofactor	Binds 2 2Fe-2S clusters By similarity. FAD By similarity. Molybdopterin By similarity.
Enzyme regulation	Strongly inhibited by iodoacetate, potassium cyanide (KCN), 2-mercaptoethanol, dithiothreitol (DTT), p-chloromercuribenzoate, menadione and estradiol. Weakly inhibited by 4'-(9-acridinylamino)methanesulfon-m-anisidine (mAMSA) and tritonX-100. Not affected by allopurinol. Ref.6
Subunit structure	Aldehyde oxidases (AO) are homo- and heterodimers of AO subunits. AO-beta is a AAO1-AAO2 heterodimer; AO-gamma is a AAO2 homodimer. AAO2 also forms a dimer with AAO3. Ref.5 Ref.9
Tissue specificity	Weakly expressed in roots, leaves and seedlings. In seedlings, mostly expressed in lower part of hypocotyls. Detectable in seeds and mature siliques at low levels. Ref.1 Ref.3 Ref.4 Ref.7 Ref.8
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-gamma dimer. KM=57 µM for heptaldehyde KM=7.7 µM for benzaldehyde KM=0.33 µM for naphthaldehyde KM=410 µM for cinnamaldehyde Vmax=24 nmol/min/mg enzyme with heptaldehyde as substrate Vmax=8.7 nmol/min/mg enzyme with benzaldehyde as substrate Vmax=65 nmol/min/mg enzyme with naphthaldehyde as substrate Vmax=20 nmol/min/mg enzyme with cinnamaldehyde as substrate pH dependence: Optimum pH is 8. Temperature dependence: Optimum temperature is 50 degrees Celsius.

Ontologies

Keywords
Ligand	2Fe-2S FAD Flavoprotein Iron Iron-sulfur Metal-binding Molybdenum NAD
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	abscisic acid biosynthetic process Ref.7 Traceable author statement. Source: TAIR oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW FAD binding Inferred from electronic annotation. Source: InterPro aldehyde oxidase activity Ref.6 Inferred from direct assay. Source: TAIR electron carrier activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW molybdenum ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1321	1321	Aldehyde oxidase 2		PRO_0000166110
Regions
	Domain	1 – 90	90	2Fe-2S ferredoxin-type
	Domain	215 – 404	190	FAD-binding PCMH-type
Sites
	Metal binding	42	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	47	1	Iron-sulfur (2Fe-2S) By similarity
	Metal binding	50	1	Iron-sulfur (2Fe-2S) By similarity
Experimental info
	Sequence conflict	808	1	K → N in AAC39510. Ref.3
	Sequence conflict	1083	1	S → T in AAC39510. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q7G192-1 [UniParc]. Last modified April 26, 2005. Version 2. Checksum: BFF5E02BF0406A4A	FASTA	1,321	144,580
	10 20 30 40 50 60 MSLVFAINGQ RFELELSSVD PSTTLLEFLR YQTSFKSVKL SCGEGGCGAC VVLLSKFDPV 70 80 90 100 110 120 LQKVEDFTVS SCLTLLCSVN HCNITTSEGL GNSRDGFHPI HKRLSGFHAS QCGFCTPGMS 130 140 150 160 170 180 VSLFSALLDA DKSQYSDLTV VEAEKAVSGN LCRCTGYRPI VDACKSFASD VDIEDLGLNS 190 200 210 220 230 240 FCRKGDKDSS SLTRFDSEKR ICTFPEFLKD EIKSVDSGMY RWCSPASVEE LSSLLEACKA 250 260 270 280 290 300 NSNTVSMKLV AGNTSMGYYK DEREQNYDKY IDITRIPHLK EIRENQNGVE IGSVVTISKV 310 320 330 340 350 360 IAALKEIRVS PGVEKIFGKL ATHMEMIAAR FIRNFGSIGG NLVMAQRKQF PSDMATILLA 370 380 390 400 410 420 AGAFVNIMSS SRGLEKLTLE EFLERSPLEA HDLVLSIEIP FWHSETNSEL FFETYRAAPR 430 440 450 460 470 480 PHGSALAYLN AAFLAEVKDT MVVNCRLAFG AYGTKHAIRC KEIEEFLSGK VITDKVLYEA 490 500 510 520 530 540 ITLLGNVVVP EDGTSNPAYR SSLAPGFLFK FLHTLMTHPT TDKPSNGYHL DPPKPLPMLS 550 560 570 580 590 600 SSQNVPINNE YNPVGQPVTK VGASLQASGE AVYVDDIPSP TNCLYGAFIY SKKPFARIKG 610 620 630 640 650 660 IHFKDDLVPT GVVAVISRKD VPKGGKNIGM KIGLGSDQLF AEDFTTSVGE CIAFVVADTQ 670 680 690 700 710 720 RHADAAVNLA VVEYETEDLE PPILSVEDAV KKSSLFDIIP FLYPQQVGDT SKGMAEADHQ 730 740 750 760 770 780 ILSSEIRLGS QYVFYMETQT ALAVGDEDNC IVVYSSTQTP QYVQSSVAAC LGIPENNIRV 790 800 810 820 830 840 ITRRVGGGFG GKSVKSMPVA TACALAAKKL QRPVRTYVNR KTDMIMTGGR HPMKITYSVG 850 860 870 880 890 900 FKSTGKITAL ELEILIDAGA SYGFSMFIPS NLIGSLKKYN WGALSFDIKL CKTNLLSRAI 910 920 930 940 950 960 MRSPGDVQGT YIAEAIIENI ASSLSLEVDT IRKINLHTHE SLALFYKDGA GEPHEYTLSS 970 980 990 1000 1010 1020 MWDKVGVSSK FEERVSVVRE FNESNMWRKR GISRVPIIYE VLLFATPGRV SVLSDGTIVV 1030 1040 1050 1060 1070 1080 EIGGIELGQG LWTKVKQMTS YALGMLQCDG TEELLEKIRV IQSDSLSMVQ GNFTGGSTTS 1090 1100 1110 1120 1130 1140 EGSCAAVRLC CETLVERLKP LMERSDGPIT WNELISQAYA QSVNLSASDL YTPKDTPMQY 1150 1160 1170 1180 1190 1200 LNYGTAVSEV EVDLVTGQTT VLQTDILYDC GKSLNPAVDL GQIEGSFVQG LGFFMLEEYI 1210 1220 1230 1240 1250 1260 EDPEGLLLTD STWTYKIPTV DTIPKQFNVE ILNGGCHEKR VLSSKASGEP PLLLAASVHC 1270 1280 1290 1300 1310 1320 ATRQAVKEAR KQLCMWKGEN GSSGSAFQLP VPATMPVVKE LCGLDIIESY LEWKLHDNSN L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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.
[2]	"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana." Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B., Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M., Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V., Choisne N., Artiguenave F. , Robert C., Brottier P., Wincker P., Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H., Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H., Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A., Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H., Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J., Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B., Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D., de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E., Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G., Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X., Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M., Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B., Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J., Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C., Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y., Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K., Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S. Nature 408:820-822(2000) [PubMed: 11130713] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: cv. Columbia.
[3]	"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] OF 758-1321, TISSUE SPECIFICITY. Strain: cv. Wassilewskija. Tissue: Root.
[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: 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.
[9]	"Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis." Koiwai H., Nakaminami K., Seo M., Mitsuhashi W., Toyomasu T., Koshiba T. Plant Physiol. 134:1697-1707(2004) [PubMed: 15064376] [Abstract] Cited for: SUBUNIT, SUBSTRATE SPECIFICITY. Strain: cv. Columbia. Tissue: Seedling hypocotyl.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AB005805 mRNA. Translation: BAA28625.1. AL391734 Genomic DNA. Translation: CAC05634.1. AF039896 mRNA. Translation: AAC39510.1.
IPI	IPI00529435.
PIR	T51623. T52050.
RefSeq	NP_189946.1.
UniGene	At.462
3D structure databases
HSSP	HSSP built from PDB template 1FO4 based on UniProtKB P80457.
ModBase	Search...
Proteomic databases
PRIDE	Q7G192.
Genome annotation databases
GeneID	823457.
GenomeReviews	Gene locus AT3G43600 in contig BA000014_GR.
KEGG	ath:AT3G43600.
NMPDR	fig|3702.1.peg.15566.
Organism-specific databases
GeneFarm	4893. 470.
TAIR	At3g43600.
Phylogenomic databases
OMA	Q7G192. SRDGFHP.
Enzyme and pathway databases
BioCyc	MetaCyc:AT3G43600-MON.
BRENDA	1.2.3.1. 302.
Gene expression databases
GermOnline	AT3G43600. Arabidopsis thaliana.
Family and domain databases
InterPro	IPR002888. 2Fe-2S_bd. IPR006058. 2Fe2S_fd_BS. IPR000674. Ald_Oxase/Xan_DH_a/b. IPR016208. Ald_Oxase/xanthine_DH. IPR008274. AldOxase/xan_DH_Mopterin-bd. IPR005107. CO_DH_flav_C. IPR016169. CO_DH_flavot_FAD-bd_sub2. IPR016166. FAD-bd_2. IPR001041. Ferredoxin. IPR002346. Mopterin_DH_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.
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]
ProtoNet	Search...

Entry information

Entry name

ALDO2_ARATH

Accession

Primary (citable) accession number: Q7G192
Secondary accession number(s): O49156, O64418

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 26, 2005
Last sequence update:	April 26, 2005
Last modified:	June 16, 2009
This is version 48 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

PPAP (Plant Proteome Annotation Project)