ID   ALDO3_ORYSJ             Reviewed;        1356 AA.
AC   Q852M2;
DT   25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-NOV-2008, entry version 39.
DE   RecName: Full=Probable aldehyde oxidase 3;
DE            Short=AO-3;
DE            EC=1.2.3.1;
GN   OrderedLocusNames=Os03g0790700, LOC_Os03g57680;
GN   ORFNames=OSJNBa0087O09.19;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BEP clade;
OC   Ehrhartoideae; Oryzeae; Oryza.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16109971; DOI=10.1101/gr.3869505;
RG   The rice chromosome 3 sequencing consortium;
RA   Buell C.R., Yuan Q., Ouyang S., Liu J., Zhu W., Wang A., Maiti R.,
RA   Haas B., Wortman J., Pertea M., Jones K.M., Kim M., Overton L.,
RA   Tsitrin T., Fadrosh D., Bera J., Weaver B., Jin S., Johri S.,
RA   Reardon M., Webb K., Hill J., Moffat K., Tallon L., Van Aken S.,
RA   Lewis M., Utterback T., Feldblyum T., Zismann V., Iobst S., Hsiao J.,
RA   de Vazeille A.R., Salzberg S.L., White O., Fraser C.M., Yu Y.,
RA   Kim H.-I., Rambo T., Currie J., Collura K., Kernodle-Thompson S.,
RA   Wei F., Kudrna K., Ammiraju J.S.S., Luo M., Goicoechea J.L.,
RA   Wing R.A., Henry D., Oates R., Palmer M., Pries G., Saski C.,
RA   Simmons J., Soderlund C., Nelson W., de la Bastide M., Spiegel L.,
RA   Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA   O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H.,
RA   Wilson R., Jin W., Lee H.R., Jiang J., Jackson S.;
RT   "Sequence, annotation, and analysis of synteny between rice chromosome
RT   3 and diverged grass species.";
RL   Genome Res. 15:1284-1291(2005).
CC   -!- CATALYTIC ACTIVITY: An aldehyde + H(2)O + O(2) = a carboxylic acid
CC       + H(2)O(2).
CC   -!- COFACTOR: Binds 2 2Fe-2S clusters (By similarity).
CC   -!- COFACTOR: FAD (By similarity).
CC   -!- COFACTOR: Molybdopterin (By similarity).
CC   -!- SUBUNIT: Aldehyde oxidases (AO) are homo- and heterodimers of AO
CC       subunits (By similarity).
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain.
CC   -!- SIMILARITY: Contains 1 FAD-binding PCMH-type domain.
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DR   EMBL; AC087096; AAO24918.1; -; Genomic_DNA.
DR   RefSeq; NP_001051517.1; -.
DR   UniGene; Os.88638; -.
DR   HSSP; P80457; 1FO4.
DR   GeneID; 4334381; -.
DR   KEGG; osa:4334381; -.
DR   Gramene; Q852M2; -.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0004031; F:aldehyde oxidase activity; IEA:EC.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR002888; 2Fe-2S_bd.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DHase_a/b.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DHase.
DR   InterPro; IPR008274; AldOxase/xan_DHase_Mopterin-bd.
DR   InterPro; IPR005107; CO_DHase_flav_C.
DR   InterPro; IPR016169; CO_DHase_flavot_FAD-bd_sub2.
DR   InterPro; IPR001041; Ferredoxin.
DR   InterPro; IPR002346; Mopterin_DHase_FAD-bd.
DR   Gene3D; G3DSA:3.30.365.10; Ald_xan_DH_mo_bd; 2.
DR   Gene3D; G3DSA:3.90.1170.50; Aldxan_DH_hamm; 1.
DR   Gene3D; G3DSA:3.30.390.50; CO_DH_flav_C; 1.
DR   Gene3D; G3DSA:3.30.465.10; CO_DH_flavoprot_FAD-bd_sub2; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 1.
DR   Pfam; PF02738; Ald_Xan_dh_C2; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   Pfam; PF00111; Fer2; 1.
DR   Pfam; PF01799; Fer2_2; 1.
DR   PIRSF; PIRSF000127; Xanthine_DH; 1.
DR   ProDom; PD186071; 2Fe-2S_bind; 1.
DR   PROSITE; PS00197; 2FE2S_FER_1; 1.
DR   PROSITE; PS51085; 2FE2S_FER_2; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   3: Inferred from homology;
KW   2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis; FAD;
KW   Flavoprotein; Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD;
KW   Oxidoreductase.
FT   CHAIN         1   1356       Probable aldehyde oxidase 3.
FT                                /FTId=PRO_0000247647.
FT   DOMAIN       10     97       2Fe-2S ferredoxin-type.
FT   DOMAIN      245    437       FAD-binding PCMH-type.
FT   METAL        49     49       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        54     54       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        57     57       Iron-sulfur (2Fe-2S) (By similarity).
FT   METAL        79     79       Iron-sulfur (2Fe-2S) (By similarity).
SQ   SEQUENCE   1356 AA;  145336 MW;  899961AA38FEE51E CRC64;
     MGSEAAAAAR AVVVAVNGER YEAVGVDPST TLLEFLRTRT PVRGPKLGCG EGGCGACVVV
     VSKYDAVADE VTEFSASSCL TLLGSLHHCA VTTSEGIGNS RDGFHAVQRR LSGFHASQCG
     FCTPGMCMSI YSALAKADKA SGRPAPPTGF SKITAAEAEK AVSGNLCRCT GYRPIVDACK
     SFAADVDLED LGLNAFWKKG VDDEHADINK LPAYSGGAAV CTFPEFLKSE IRSSMGQANG
     DTSAVVVTGD GWFHPKSVEE FHRLFDSNLF DERSVKIVAS NTGSGVYKDQ DLHDKYINIS
     QIPELSAINR SSKGVEIGAV VSISQAIDIL SDGGAVFRKI ADHLSKVASP FVRNTATIGG
     NIIMAQRLSF SSDIATVLLA AGSTVTIQVA AKRMCITLEE FLKQPPCDSR TLLVSISIPD
     WGSDDGITFQ TFRAAPRPLG NAVSYVNSAF LARSSVDGSS GSHLIEDVCL AFGPFGAKHA
     IRAREVEKFL KGKLVSAPVI LEAVRLLKGV VSPAEGTTHP EYRVSLAVSY LFKFLSSLTN
     GLDEPENANV PNGSFTNGTA NGIVDSSPEK HSNVDSSYLP IKSRQEMVFS DEYRPIGKPI
     EKTGAELQAS GEAVYVDDIS APKDCLYGAF IYSTHPHAHI KGVNFRSSLA SQKVITVITL
     KDIPTNGKNI GSCSPMLGDE ALFVDPVSEF AGQNIGVVIA ETQKYAYMAA KQSVIEYSTE
     NLQPPILTVE DAVQHNSYFQ VPPFLAPTPI GEFNQAMSEA DHKIIDGEVK LESQYYFYME
     TQTALAIPDE DNCITLYVSA QLPEITQNTV ARCLGIPYHN VRIITRRVGG GFGGKAMKAI
     HVATACAVAA FKLRRPVRMY LDRKTDMIMA GGRHPMKVKY SVGFKSDGKI TGLHVDLRIN
     CGISPDCSPA LPVAIVGALK KYNWGALSFD IKLCKTNVSS KSAMRAPGDA QGSFIAEAIV
     EHIASTLSVD TNAIRRKNLH DFESLKVFYG NSAGDPSTYS LVTIFDKLAS SPEYQQRAAV
     VEHFNAGSRW KKRGISCVPI TYDVRLRPSP GKVSIMNDGS IAVEVGGVEI GQGLWTKVKQ
     MTAFALGQLC DDGGEGLLDK VRVIQADTLS MIQGGFTGGS TTSETSCEAV RKSCAALVER
     LKPIKEKAGT LPWKSLIAQA SMASVKLTEH AYWTPDPTFT SYLNYGAAIS EVEVDVLTGE
     TTILRSDLVY DCGQSLNPAV DLGQVEGAFV QGIGFFTNEE YTTNSDGLVI NDGTWTYKIP
     TVDTIPKQFN VELINSARDH KRVLSSKASG EPPLLLASSV HCAMREAIRA ARKEFAGAGG
     SSLTFQMDVP ATMPIVKELC GLDVVERDLE SFAAKA
//