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UniProtKB/Swiss-Prot entry Q7G192


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ALDO2_ARATH
Primary accession number Q7G192
Secondary accession numbers O49156 O64418
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on April 26, 2005 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 40)
Name and origin of the protein
Protein name Aldehyde oxidase 2
Synonyms AO-2
AtAO-2
AtAO3
EC 1.2.3.1
Gene name
Name: AAO2
Synonyms: AO3
OrderedLocusNames: At3g43600
ORFNames: F22J12.40
From
Arabidopsis thaliana (Mouse-ear cress) [TaxID: 3702] 
Taxonomy Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; Spermatophyta; Magnoliophyta; eudicotyledons; core eudicotyledons; rosids; eurosids II; Brassicales; Brassicaceae; Arabidopsis.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=cv. Columbia;
TISSUE=Seedling hypocotyl;
PubMed=9615466 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048706; PubMed=11130713 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
Nature 408:820-822(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 758-1321, AND TISSUE SPECIFICITY.
STRAIN=cv. Wassilewskija;
TISSUE=Root;
DOI=10.1016/S0167-4781(98)00085-2; PubMed=9655945 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[4]
TISSUE SPECIFICITY, AND SUBSTRATE SPECIFICITY.
DOI=10.1104/pp.116.2.687; PubMed=9489015 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[5]
SUBUNIT, CATALYTIC ACTIVITY, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=10423535 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[6]
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=10739959 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[7]
TISSUE SPECIFICITY.
DOI=10.1046/j.1365-313x.2000.00812.x; PubMed=10972874 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[8]
TISSUE SPECIFICITY.
DOI=10.1093/pcp/pch198; PubMed=15574845 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[9]
SUBUNIT, AND SUBSTRATE SPECIFICITY.
STRAIN=cv. Columbia;
TISSUE=Seedling hypocotyl;
DOI=10.1104/pp.103.036970; PubMed=15064376 [NCBI, ExPASy, EBI, Israel, Japan]
Koiwai H., Nakaminami K., Seo M., Mitsuhashi W., Toyomasu T., Koshiba T.;
"Tissue-specific localization of an abscisic acid biosynthetic enzyme, AAO3, in Arabidopsis.";
Plant Physiol. 134:1697-1707(2004).
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.
  • COFACTOR: Binds 2 2Fe-2S clusters (By similarity).
  • COFACTOR: FAD (By similarity).
  • COFACTOR: 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.
  • BIOPHYSICOCHEMICAL PROPERTIES:
    Kinetic parameters:   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;
    Note=Kinetic values were obtained with the AO-gamma dimer;
    pH dependence:   Optimum pH is 8;
    Temperature dependence:   Optimum temperature is 50 degrees Celsius;
  • SUBUNIT: 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.
  • 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.
  • SIMILARITY: Belongs to the xanthine dehydrogenase family.
  • SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
  • SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB005805; BAA28625.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL391734; CAC05634.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039896; AAC39510.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T51623; T51623.
T52050; T52050.
RefSeq NP_189946.1; -.
UniGene At.462
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase Q7G192.
Enzyme and pathway databases
BioCyc MetaCyc:AT3G43600-MON; -.
Organism-specific databases
GeneFarm 4893; 470.
TAIR At3g43600; -.
Gene expression databases
GermOnline AT3G43600; 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.
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 of domain structure.
Gene3D G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
G3DSA:3.30.390.50; CO_DH_flav_C; 1.
G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
Pfam PF01315; Ald_Xan_dh_C; 1.
PF02738; Ald_Xan_dh_C2; 1.
PF03450; CO_deh_flav_C; 1.
PF00941; FAD_binding_5; 1.
PF00111; Fer2; 1.
PF01799; Fer2_2; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF000127; Xanthine_DH; 1.
ProDom PD186071; 2Fe-2S_bind; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00197; 2FE2S_FER_1; 1.
PS51085; 2FE2S_FER_2; 1.
PS51387; FAD_PCMH; 1.
PS00559; MOLYBDOPTERIN_EUK; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q7G192.
Genome annotation databases
GeneID 823457; -.
GenomeReviews BA000014_GR; AT3G43600.
KEGG ath:AT3G43600; -.
NMPDR fig|3702.1.peg.15566; -.
Other
ProtoNet Q7G192.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
2Fe-2S; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1321  1321     Aldehyde oxidase 2. PRO_0000166110
DOMAIN   1     90  90     2Fe-2S ferredoxin-type. 
DOMAIN   215    404  190     FAD-binding PCMH-type. 
METAL   42     42        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   47     47        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   50     50        Iron-sulfur (2Fe-2S) (By similarity). 
CONFLICT   808    808        K -> N (in Ref. 3; AAC39510). 
CONFLICT   1083   1083        S -> T (in Ref. 3; AAC39510). 
Sequence information
Length: 1321 AA [This is the length of the unprocessed precursor] Molecular weight: 144580 Da [This is the MW of the unprocessed precursor] CRC64: BFF5E02BF0406A4A [This is a checksum on the sequence]
        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 

Q7G192 in FASTA format

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