ALDO3_ORYSJ
ID ALDO3_ORYSJ Reviewed; 1356 AA.
AC Q852M2; Q10C91;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Probable aldehyde oxidase 3;
DE Short=AO-3;
DE EC=1.2.3.1;
GN OrderedLocusNames=Os03g0790700, LOC_Os03g57680; ORFNames=OSJNBa0087O09.19;
OS Oryza sativa subsp. japonica (Rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
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., Haas B.,
RA Wortman J., Pertea M., Jones K.M., Kim M., Overton L., Tsitrin T.,
RA Fadrosh D., Bera J., Weaver B., Jin S., Johri S., Reardon M., Webb K.,
RA Hill J., Moffat K., Tallon L., Van Aken S., Lewis M., Utterback T.,
RA Feldblyum T., Zismann V., Iobst S., Hsiao J., de Vazeille A.R.,
RA Salzberg S.L., White O., Fraser C.M., Yu Y., Kim H., Rambo T., Currie J.,
RA Collura K., Kernodle-Thompson S., Wei F., Kudrna K., Ammiraju J.S.S.,
RA Luo M., Goicoechea J.L., Wing R.A., Henry D., Oates R., Palmer M.,
RA Pries G., Saski C., Simmons J., Soderlund C., Nelson W., de la Bastide M.,
RA Spiegel L., Nascimento L., Huang E., Preston R., Zutavern T., Palmer L.,
RA O'Shaughnessy A., Dike S., McCombie W.R., Minx P., Cordum H., Wilson R.,
RA Jin W., Lee H.R., Jiang J., Jackson S.;
RT "Sequence, annotation, and analysis of synteny between rice chromosome 3
RT and diverged grass species.";
RL Genome Res. 15:1284-1291(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Nipponbare;
RX PubMed=16100779; DOI=10.1038/nature03895;
RG International rice genome sequencing project (IRGSP);
RT "The map-based sequence of the rice genome.";
RL Nature 436:793-800(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Nipponbare;
RX PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT "Improvement of the Oryza sativa Nipponbare reference genome using next
RT generation sequence and optical map data.";
RL Rice 6:4-4(2013).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Nipponbare;
RG The rice full-length cDNA consortium;
RT "Oryza sativa full length cDNA.";
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an aldehyde + H2O + O2 = a carboxylate + H(+) + H2O2;
CC Xref=Rhea:RHEA:16829, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17478,
CC ChEBI:CHEBI:29067; EC=1.2.3.1;
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250};
CC Note=Binds 2 [2Fe-2S] clusters. {ECO:0000250};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC -!- COFACTOR:
CC Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302; Evidence={ECO:0000250};
CC Note=Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Aldehyde oxidases (AO) are homodimers and heterodimers of AO
CC subunits. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC {ECO:0000305}.
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DR EMBL; AC087096; AAO24918.1; -; Genomic_DNA.
DR EMBL; DP000009; ABF99281.1; -; Genomic_DNA.
DR EMBL; AP014959; BAS86776.1; -; Genomic_DNA.
DR EMBL; AK242113; BAH01196.1; -; mRNA.
DR RefSeq; XP_015630438.1; XM_015774952.1.
DR AlphaFoldDB; Q852M2; -.
DR SMR; Q852M2; -.
DR STRING; 4530.OS03T0790700-01; -.
DR PaxDb; Q852M2; -.
DR PRIDE; Q852M2; -.
DR EnsemblPlants; Os03t0790700-01; Os03t0790700-01; Os03g0790700.
DR GeneID; 4334381; -.
DR Gramene; Os03t0790700-01; Os03t0790700-01; Os03g0790700.
DR KEGG; osa:4334381; -.
DR eggNOG; KOG0430; Eukaryota.
DR HOGENOM; CLU_001681_1_1_1; -.
DR InParanoid; Q852M2; -.
DR OMA; RSEYECH; -.
DR OrthoDB; 48717at2759; -.
DR PlantReactome; R-OSA-1119374; Abscisic acid biosynthesis.
DR PlantReactome; R-OSA-1119486; IAA biosynthesis I.
DR Proteomes; UP000000763; Chromosome 3.
DR Proteomes; UP000059680; Chromosome 3.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004031; F:aldehyde oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0009688; P:abscisic acid biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009851; P:auxin biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR002888; 2Fe-2S-bd.
DR InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR006058; 2Fe2S_fd_BS.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH.
DR InterPro; IPR008274; AldOxase/xan_DH_Mopterin-bd.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR005107; CO_DH_flav_C.
DR InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR PANTHER; PTHR11908; PTHR11908; 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 SMART; SM01008; Ald_Xan_dh_C; 1.
DR SMART; SM01092; CO_deh_flav_C; 1.
DR SUPFAM; SSF47741; SSF47741; 1.
DR SUPFAM; SSF54292; SSF54292; 1.
DR SUPFAM; SSF54665; SSF54665; 1.
DR SUPFAM; SSF55447; SSF55447; 1.
DR SUPFAM; SSF56003; SSF56003; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS00197; 2FE2S_FER_1; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
PE 2: Evidence at transcript level;
KW 2Fe-2S; Abscisic acid biosynthesis; Auxin biosynthesis; FAD; Flavoprotein;
KW Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..1356
FT /note="Probable aldehyde oxidase 3"
FT /id="PRO_0000247647"
FT DOMAIN 10..97
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT DOMAIN 245..437
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00718"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 49
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 54
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 57
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
FT BINDING 79
FT /ligand="[2Fe-2S] cluster"
FT /ligand_id="ChEBI:CHEBI:190135"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00465"
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
