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UniProtKB/Swiss-Prot entry Q7G191


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

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Entry information
Entry name ALDO4_ARATH
Primary accession number Q7G191
Secondary accession numbers O23027 O49157 Q7GB29
Integrated into Swiss-Prot on April 26, 2005
Sequence was last modified on April 26, 2005 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 37)
Name and origin of the protein
Protein name Aldehyde oxidase 4
Synonyms AO-4
AtAO-4
AtAO2
EC 1.2.3.1
Gene name
Name: AAO4
Synonyms: AO2
OrderedLocusNames: At1g04580
ORFNames: T1G11.17
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 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=cv. Columbia;
TISSUE=Rosette leaf;
Seo M., Koshiba T.;
"Arabidopsis aldehyde oxidase cDNA.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=cv. Columbia;
DOI=10.1038/35048500; PubMed=11130712 [NCBI, ExPASy, EBI, Israel, Japan]
Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
"Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
Nature 408:816-820(2000).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 1082-1337.
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]
INDUCTION, AND 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).
[5]
TISSUE SPECIFICITY, AND MUTANT AAO4-1.
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).
Comments
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
AB037271; BAA90299.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC002376; AAB80640.1; ALT_SEQ; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF039897; AAC39511.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR D86178; D86178.
T52051; T52051.
RefSeq NP_563711.1; -.
UniGene At.465
3D structure databases
HSSP P80457; 1FO4. [HSSP ENTRY / PDB]
ModBase Q7G191.
Organism-specific databases
GeneFarm 4895; 470.
TAIR At1g04580; -.
Gene expression databases
GermOnline AT1G04580; Arabidopsis thaliana.
Ontologies
GO
GO:0004031; Molecular function: aldehyde oxidase activity (inferred from electronic annotation from EC).
QuickGo view.
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 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.
G3DSA:3.10.20.30; Ferredoxin_fold; 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 Q7G191.
Genome annotation databases
GeneID 839488; -.
GenomeReviews CT485782_GR; AT1G04580.
KEGG ath:AT1G04580; -.
NMPDR fig|3702.1.peg.605; -.
Other
ProtoNet Q7G191.
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   1337  1337     Aldehyde oxidase 4. PRO_0000166112
DOMAIN   4     91  88     2Fe-2S ferredoxin-type. 
DOMAIN   225    409  185     FAD-binding PCMH-type. 
METAL   43     43        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   48     48        Iron-sulfur (2Fe-2S) (By similarity). 
METAL   51     51        Iron-sulfur (2Fe-2S) (By similarity). 
CONFLICT   1257   1257        V -> I (in Ref. 3; AAC39511). 
Sequence information
Length: 1337 AA [This is the length of the unprocessed precursor] Molecular weight: 147304 Da [This is the MW of the unprocessed precursor] CRC64: 8DCF487FA3F7D6B8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MAGDDLVFAV NGEKFEVLSV NPSTTLLEFL RSNTCFKSVK LSCGEGGCGA CIVILSKYDP 

        70         80         90        100        110        120 
VLDQVEEYSI NSCLTLLCSL NGCSITTSDG LGNTEKGFHP IHKRFAGFHA SQCGFCTPGM 

       130        140        150        160        170        180 
CISLYSALSK AHNSQSSPDY LTALAAEKSI AGNLCRCTGY RPIADACKSF ASDVDIEDLG 

       190        200        210        220        230        240 
FNSFWRKGES REEMLKKLPP YNPEKDLITF PDFLKEKIKC QHNVLDQTRY HWSTPGSVAE 

       250        260        270        280        290        300 
LQEILATTNP GKDRGLIKLV VGNTGTGYYK EEKQYGRYID ISHIPEMSMI KKDDREIEIG 

       310        320        330        340        350        360 
AVVTISKVID ALMEENTSAY VFKKIGVHME KVANHFIRNS GSIGGNLVMA QSKSFPSDIT 

       370        380        390        400        410        420 
TLLLAADASV HMINAGRHEK LRMGEYLVSP PILDTKTVLL KVHIPRWIAS STTGLLFETY 

       430        440        450        460        470        480 
RAALRPIGSA LPYINAAFLA VVSHDASSSG IIVDKCRLAF GSYGGYHSIR AREVEDFLTG 

       490        500        510        520        530        540 
KILSHSVLYE AVRLLKGIIV PSIDTSYSEY KKSLAVGFLF DFLYPLIESG SWDSEGKHID 

       550        560        570        580        590        600 
GHIDPTICLP LLSSAQQVFE SKEYHPVGEA IIKFGAEMQA SGEAVYVDDI PSLPHCLHGA 

       610        620        630        640        650        660 
FIYSTKPLAW IKSVGFSGNV TPIGVLAVIT FKDIPEVGQN IGYITMFGTG LLFADEVTIS 

       670        680        690        700        710        720 
AGQIIALVVA DTQKHADMAA HLAVVEYDSR NIGTPVLSVE DAVKRSSLFE VPPEYQPEPV 

       730        740        750        760        770        780 
GDISKGMAEA DRKIRSVELR LGSQYFFYME TQTALALPDE DNCLVVYSST QAPEFTQTVI 

       790        800        810        820        830        840 
ATCLGIPEHN VRVITRRVGG GFGGKAIKSM PVATACALAA KKMQRPVRIY VNRKTDMIMA 

       850        860        870        880        890        900 
GGRHPLKITY SVGFRSDGKL TALDLNLFID AGSDVDVSLV MPQNIMNSLR KYDWGALSFD 

       910        920        930        940        950        960 
IKVCKTNLPS RTSLRAPGEV QGSYIAESII ENVASSLKMD VDVVRRINLH TYESLRKFYK 

       970        980        990       1000       1010       1020 
QAAGEPDEYT LPLLWDKLEV SADFRRRAES VKEFNRCNIW RKRGISRVPI IHLVIHRPTP 

      1030       1040       1050       1060       1070       1080 
GKVSILNDGS VAVEVAGIEV GQGLWTKVQQ MVAYGLGMIK CEGSDDLLER IRLLQTDTLS 

      1090       1100       1110       1120       1130       1140 
MSQSSYTAGS TTSENCCEAV RLCCGILVER LRPTMNQILE NARSVTWDML IQQANAQSVD 

      1150       1160       1170       1180       1190       1200 
LSARTFYKPE SSSAEYLNYG VGASEVEVDL VTGRTEIIRS DIIYDCGKSL NPAVDLGQIE 

      1210       1220       1230       1240       1250       1260 
GAFVQGIGFF MYEEYTTNEN GLVNEEGTWD YKIPTIDTIP KQFNVQILNS GHHKNRVLSS 

      1270       1280       1290       1300       1310       1320 
KASGEPPLLV AASVHCATRS AIREARKQYL SWNCIDDDHR ERCDLGFELP VPATMPVVKQ 

      1330 
LCGLESIEKY LEWKTYP 

Q7G191 in FASTA format

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